data_4073
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Backbone 1H, 13C and 15N Chemical Shift Assignments for Oxidized Human
Ferredoxin
;
_BMRB_accession_number 4073
_BMRB_flat_file_name bmr4073.str
_Entry_type original
_Submission_date 1997-11-20
_Accession_date 1997-11-20
_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 Xia Bin . .
2 Volkman Brian F. .
3 Markley John L. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 185
"13C chemical shifts" 264
"15N chemical shifts" 89
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
1997-11-20 original author 'original release'
2002-04-08 update BMRB 'update of relationships'
stop_
loop_
_Related_BMRB_accession_number
_Relationship
4073 'Chemical Shift of Oxidized Human Ferredoxin'
5337 'Complete assignments of 1H, 13C and 15N Chemical Shifts for Oxidized Human Adrenodoxin (4-114)'
stop_
_Original_release_date 2016-09-15
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full
;
Xia, B., Volkman, B. F. , and Markley, J. L., "Evidence for Oxidation-State-Dependent
Conformational Changes in Human Ferredoxin from Multinuclear, Multidimensional NMR
Spectroscopy," Biochemistry 37, 3965-3973 (1998).
;
_Citation_title
;
Evidence for Oxidation-State-Dependent Conformational Changes in Human
Ferredoxin from Multinuclear, Multidimensional NMR Spectroscopy
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 98191359
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Xia Bin . .
2 Volkman Brian F. .
3 Markley John L. .
stop_
_Journal_abbreviation Biochemistry
_Journal_volume 37
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 3965
_Page_last 3973
_Year 1998
_Details .
loop_
_Keyword
'F2S2 cluster'
'HuFd reduced'
NMR
adrenodoxin
'human ferrodoxin (HuFd)'
stop_
save_
#######################################
# Cited references within the entry #
#######################################
save_citation_one
_Saveframe_category citation
_Citation_full
;
Xia, B., Cheng, H., Skjeldal, L., Coghlan, V. M., Vickery, L. E.,
and Markley, J. L., Biochemistry 34, 180-187, (1995).
;
_Citation_title
;
Multinuclear magnetic resonance and mutagenesis studies of the histidine residues of human mitochondrial ferredoxin.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 7819194
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Xia B . .
2 Cheng H . .
3 Skjeldal L . .
4 Coghlan 'V M' M. .
5 Vickery 'L E' E. .
6 Markley 'J L' L. .
stop_
_Journal_abbreviation Biochemistry
_Journal_name_full Biochemistry
_Journal_volume 34
_Journal_issue 1
_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 180
_Page_last 187
_Year 1995
_Details
;
Human mitochondrial ferredoxin is a [2Fe-2S] protein that functions to transfer
electrons from NADPH-dependent ferredoxin reductase to cytochrome P450 enzymes.
Two of the three histidines of human ferredoxin are strictly conserved in the
sequences of all known vertebrate ferredoxins, and one of these (His56) is
adjacent to Cys55, which serves as one of the ligands to the iron-sulfur
cluster. All but 16 of its residues show sequence identity with those of bovine
ferredoxin. It has been proposed for bovine ferredoxin that His56 hydrogen
bonds with a labile sulfur and that the reduction of the iron-sulfur center is
accompanied by the uptake of a proton by this histidine [Lambeth, J. D.,
Seybert, D. W., Lancaster, J. R., Jr., Salerno, J. C., & Kamin, H. (1982) Mol.
Cell. Biochem. 45, 13-31]. In this paper, we report procedures for labeling
human ferredoxin uniformly with 15N using 15NH4Cl and selectively with 13C by
the incorporation of [U-13C]histidine. Most of the imidazole 1H, 13C, and 15N
resonances of the three histidines have been assigned by heteronuclear
two-dimensional single- and multiple-bond correlation spectroscopy.
Site-directed mutagenesis was used in assigning the NMR signals from His56. The
pKa values of His10 (6.5) and His62 (5.8) in oxidized human ferredoxin were
found to be similar to those reported previously for the corresponding residues
of bovine ferredoxin [Greenfield, N. J., Wu, X., & Jordan, F. (1989) Biochim.
Biophys. Acta 995, 246-254; Miura, S., Tamita, S., & Ichikawa, Y. (1991) J.
Biol. Chem. 266, 19212-19216].(ABSTRACT TRUNCATED AT 250 WORDS)
;
save_
save_citation_two
_Saveframe_category citation
_Citation_full
;
Xia B., Cheng H., Bandarian V., Reed G. H., & Markley J. L.,
Biochemistry 35, 9488-9495,(1996).
;
_Citation_title
;
Human ferredoxin: overproduction in Escherichia coli, reconstitution in vitro, and spectroscopic studies of iron-sulfur cluster ligand cysteine-to-serine mutants.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 8755728
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Xia B. . .
2 Cheng H. . .
3 Bandarian V. . .
4 Reed G.H. H. .
5 Markley J.L. L. .
stop_
_Journal_abbreviation Biochemistry
_Journal_name_full Biochemistry
_Journal_volume 35
_Journal_issue 29
_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 9488
_Page_last 9495
_Year 1996
_Details
;
Human ferredoxin, the human equivalent of bovine adrenodoxin, is a small
iron-sulfur protein with one [2Fe-2S] cluster. It functions, as do other
vertebrate ferredoxins, to transfer electrons during the processes of steroid
hormone synthesis. A DNA fragment encoding the mature form of human ferredoxin
was cloned into an expression vector under control of the T7 RNA
polymerase/promoter system. The protein was overproduced in Escherichia coli,
and the [2Fe-2S] cluster was incorporated into the protein by in vitro
reconstitution. The overall yield was approximately 30 mg of purified,
reconstituted ferredoxin per liter of culture. Four of the five cysteines in
human ferredoxin are coordinated to the iron-sulfur cluster. First, the
non-ligand cysteine (cysteine-95) was mutated to alanine, and then double
mutants were created in which each of the other four cysteines (at positions
46, 52, 55, and 92) were mutated individually to serine. The wild-type
ferredoxin and each of the five mutant proteins were studied by UV-visible
spectroscopy and electron paramagnetic resonance spectroscopy. The EPR gav
values of all five mutants were very similar to that of wild-type human
ferredoxin. In the reduced state, three of the cysteine-to-serine mutants
exhibited axial EPR spectra similar to that of wild-type, but one of the double
mutants (C52S/C95A) exhibited a rhombic EPR spectrum. The UV-visible
spectroscopic properties of the wild-type and the C95A mutant ferredoxins were
identical, but those of the other cysteine-to-serine mutant proteins of human
ferredoxin were quite different from those of the wild-type protein and each
other. These results, along with those from cysteine-to-serine mutations in
other ferredoxins, provide the basis for a more comprehensive theoretical and
practical understanding of the features important to the ligation of [2Fe-2S]
clusters, although they do not yet permit determination of which two cysteines
ligate Fe(II) and which ligate Fe(III) in the reduced protein.
;
save_
save_citation_three
_Saveframe_category citation
_Citation_full 'Chylla, R. A. & Markley, J. L. J. Magn. Reson. (Series B) 102, 148-154, (1993)'
_Citation_title .
_Citation_status .
_Citation_type .
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Chylla R. . .
2 Markley J.L. L. .
stop_
_Journal_abbreviation .
_Journal_name_full .
_Journal_volume .
_Journal_issue .
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first .
_Page_last .
_Year .
_Details .
save_
##################################
# Molecular system description #
##################################
save_system_HuFd-ox
_Saveframe_category molecular_system
_Mol_system_name 'oxidized human ferredoxin'
_Abbreviation_common HuFd-ox
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
HuFd-ox $HuFd-ox
2Fe2S $FE
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic yes
_System_thiol_state .
loop_
_Biological_function
'cholesterol biosynthesis'
'electron transfer'
stop_
_Database_query_date .
_Details 'oxidized form of the protein'
save_
########################
# Monomeric polymers #
########################
save_HuFd-ox
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'human ferredoxin'
_Name_variant HuFd-ox
_Abbreviation_common HuFd
_Molecular_mass 13800
_Mol_thiol_state .
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 124
_Mol_residue_sequence
;
SSSEDKITVHFINRDGETLT
TKGKVGDSLLDVVVENNLDI
DGFGACEGTLACSTCHLIFE
DHIYEKLDAITDEENDMLDL
AYGLTDRSRLGCQICLTKSM
DNMTVRVPETVADARQSIDV
GKTS
;
loop_
_Residue_seq_code
_Residue_label
1 SER 2 SER 3 SER 4 GLU 5 ASP
6 LYS 7 ILE 8 THR 9 VAL 10 HIS
11 PHE 12 ILE 13 ASN 14 ARG 15 ASP
16 GLY 17 GLU 18 THR 19 LEU 20 THR
21 THR 22 LYS 23 GLY 24 LYS 25 VAL
26 GLY 27 ASP 28 SER 29 LEU 30 LEU
31 ASP 32 VAL 33 VAL 34 VAL 35 GLU
36 ASN 37 ASN 38 LEU 39 ASP 40 ILE
41 ASP 42 GLY 43 PHE 44 GLY 45 ALA
46 CYS 47 GLU 48 GLY 49 THR 50 LEU
51 ALA 52 CYS 53 SER 54 THR 55 CYS
56 HIS 57 LEU 58 ILE 59 PHE 60 GLU
61 ASP 62 HIS 63 ILE 64 TYR 65 GLU
66 LYS 67 LEU 68 ASP 69 ALA 70 ILE
71 THR 72 ASP 73 GLU 74 GLU 75 ASN
76 ASP 77 MET 78 LEU 79 ASP 80 LEU
81 ALA 82 TYR 83 GLY 84 LEU 85 THR
86 ASP 87 ARG 88 SER 89 ARG 90 LEU
91 GLY 92 CYS 93 GLN 94 ILE 95 CYS
96 LEU 97 THR 98 LYS 99 SER 100 MET
101 ASP 102 ASN 103 MET 104 THR 105 VAL
106 ARG 107 VAL 108 PRO 109 GLU 110 THR
111 VAL 112 ALA 113 ASP 114 ALA 115 ARG
116 GLN 117 SER 118 ILE 119 ASP 120 VAL
121 GLY 122 LYS 123 THR 124 SER
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date .
save_
#############
# Ligands #
#############
save_FE
_Saveframe_category ligand
_Mol_type non-polymer
_Name_common "FE (FE (III) ION)"
_BMRB_code .
_PDB_code FE
_Molecular_mass 55.845
_Mol_charge 3
_Mol_paramagnetic .
_Mol_aromatic no
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Mon Jul 11 10:30:25 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
FE FE FE . 3 . ?
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
$HuFd-ox Human 9609 . . Homo sapiens
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Variant
_Vector_type
_Vector_name
$HuFd-ox 'recombinant technology' 'E. coli' Escherichia coli BL21 (DE3)pLysS plasmid HuFd/pET9a
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
$HuFd-ox . mM 1 2 '[U-99.8% 15N]'
Tris-HCl 50 mM . . .
stop_
save_
save_sample_two
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Concentration_min_value
_Concentration_max_value
_Isotopic_labeling
$HuFd-ox . mM 1 2 '[U-99% 13C; U-99.8% 15N]'
Tris-HCl 50 mM . . .
stop_
save_
############################
# Computer software used #
############################
save_software_Felix
_Saveframe_category software
_Name FELIX
_Version '2.30 & 95.0'
loop_
_Vendor
_Address
_Electronic_address
'Molecular Simulations, San Diego, CA' . .
stop_
loop_
_Task
'used for all FT of data'
stop_
_Details .
save_
save_software_Peakpick
_Saveframe_category software
_Name Peakpick
_Version 1.1
loop_
_Vendor
_Address
_Electronic_address
'Molecular Simulations, San Diego, CA' . .
stop_
loop_
_Task
'used for peakpicking all data'
stop_
_Details .
_Citation_label $citation_three
save_
save_software_PPFLX
_Saveframe_category software
_Name PPFLX
_Version 1.1
loop_
_Vendor
_Address
_Electronic_address
'Molecular Simulations, San Diego, CA' . .
stop_
loop_
_Task
'used for peakpicking all data'
stop_
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_one
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DMX500
_Field_strength 500
_Details .
save_
save_spectrometer_two
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DMX600
_Field_strength 600
_Details .
save_
save_spectrometer_three
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DMX750
_Field_strength 750
_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_3D_HNCO_2
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D_HNCO
_Sample_label .
save_
save_3D_HNCA_3
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D_HNCA
_Sample_label .
save_
save_3D_HN(CO)CA_4
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D_HN(CO)CA
_Sample_label .
save_
save_3D_HNCACB_5
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D_HNCACB
_Sample_label .
save_
save_3D_CBCA(CO)NH_6
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D_CBCA(CO)NH
_Sample_label .
save_
save_3D_HCACO_7
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D_HCACO
_Sample_label .
save_
save_3D_15N-TOCSYd_8
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D_15N-TOCSYd
_Sample_label .
save_
save_3D_15N-NOESYd_9
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D_15N-NOESYd
_Sample_label .
save_
save_3D_15N-TOCSYe_10
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D_15N-TOCSYe
_Sample_label .
save_
save_3D_15N-NOESY_11
_Saveframe_category NMR_applied_experiment
_Experiment_name 3D_15N-NOESY
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_HuFd-ox
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 7.4 0.1 pH
temperature 295 1 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chem_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
DSS C 13 'methyl protons' ppm 0.00 external indirect . . .
DSS H 1 'methyl protons' ppm 0.00 internal direct . . .
DSS N 15 'methyl protons' ppm 0.00 external indirect . . .
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
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
2D_1H-15N_HSQC
stop_
loop_
_Sample_label
$sample_one
stop_
_Sample_conditions_label $sample_conditions_HuFd-ox
_Chem_shift_reference_set_label $chem_shift_reference
_Mol_system_component_name HuFd-ox
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 . 2 SER CA C 58.51 . 1
2 . 2 SER CB C 64.15 . 1
3 . 3 SER H H 8.63 . 1
4 . 3 SER HA H 4.44 . 1
5 . 3 SER C C 174.84 . 1
6 . 3 SER CA C 59.01 . 1
7 . 3 SER CB C 63.74 . 1
8 . 3 SER N N 118.62 . 1
9 . 4 GLU H H 8.44 . 1
10 . 4 GLU HA H 4.31 . 1
11 . 4 GLU C C 176.15 . 1
12 . 4 GLU CA C 56.71 . 1
13 . 4 GLU CB C 30.33 . 1
14 . 4 GLU N N 122.58 . 1
15 . 5 ASP H H 8.32 . 1
16 . 5 ASP HA H 4.61 . 1
17 . 5 ASP C C 175.68 . 1
18 . 5 ASP CA C 54.59 . 1
19 . 5 ASP CB C 41.13 . 1
20 . 5 ASP N N 121.84 . 1
21 . 6 LYS H H 8.11 . 1
22 . 6 LYS HA H 4.88 . 1
23 . 6 LYS C C 176.27 . 1
24 . 6 LYS CA C 55.49 . 1
25 . 6 LYS CB C 35.55 . 1
26 . 6 LYS N N 120.62 . 1
27 . 7 ILE H H 9.03 . 1
28 . 7 ILE HA H 4.47 . 1
29 . 7 ILE C C 175.02 . 1
30 . 7 ILE CA C 59.02 . 1
31 . 7 ILE CB C 40.92 . 1
32 . 7 ILE N N 119.32 . 1
33 . 8 THR H H 8.90 . 1
34 . 8 THR HA H 4.73 . 1
35 . 8 THR C C 174.18 . 1
36 . 8 THR CA C 63.49 . 1
37 . 8 THR CB C 69.17 . 1
38 . 8 THR N N 122.61 . 1
39 . 9 VAL H H 8.56 . 1
40 . 9 VAL HA H 4.21 . 1
41 . 9 VAL C C 173.52 . 1
42 . 9 VAL CA C 61.15 . 1
43 . 9 VAL CB C 35.72 . 1
44 . 9 VAL N N 125.50 . 1
45 . 10 HIS H H 8.65 . 1
46 . 10 HIS HA H 5.41 . 1
47 . 10 HIS C C 174.61 . 1
48 . 10 HIS CA C 54.22 . 1
49 . 10 HIS CB C 31.18 . 1
50 . 10 HIS N N 126.08 . 1
51 . 11 PHE H H 9.65 . 1
52 . 11 PHE HA H 5.18 . 1
53 . 11 PHE C C 175.63 . 1
54 . 11 PHE CA C 55.68 . 1
55 . 11 PHE CB C 41.89 . 1
56 . 11 PHE N N 123.24 . 1
57 . 12 ILE H H 9.11 . 1
58 . 12 ILE HA H 4.72 . 1
59 . 12 ILE C C 176.24 . 1
60 . 12 ILE CA C 60.47 . 1
61 . 12 ILE CB C 37.14 . 1
62 . 12 ILE N N 123.60 . 1
63 . 13 ASN H H 8.98 . 1
64 . 13 ASN HA H 4.68 . 1
65 . 13 ASN C C 177.29 . 1
66 . 13 ASN CA C 51.27 . 1
67 . 13 ASN CB C 38.93 . 1
68 . 13 ASN N N 125.92 . 1
69 . 14 ARG H H 8.67 . 1
70 . 14 ARG HA H 4.05 . 1
71 . 14 ARG C C 176.30 . 1
72 . 14 ARG CA C 59.33 . 1
73 . 14 ARG CB C 29.56 . 1
74 . 14 ARG N N 119.96 . 1
75 . 15 ASP H H 7.72 . 1
76 . 15 ASP HA H 4.61 . 1
77 . 15 ASP C C 177.02 . 1
78 . 15 ASP CA C 53.57 . 1
79 . 15 ASP CB C 40.70 . 1
80 . 15 ASP N N 116.90 . 1
81 . 16 GLY H H 8.22 . 1
82 . 16 GLY HA2 H 4.24 . 2
83 . 16 GLY HA3 H 3.52 . 2
84 . 16 GLY C C 174.39 . 1
85 . 16 GLY CA C 45.30 . 1
86 . 16 GLY N N 109.11 . 1
87 . 17 GLU H H 8.02 . 1
88 . 17 GLU HA H 4.29 . 1
89 . 17 GLU C C 175.62 . 1
90 . 17 GLU CA C 56.03 . 1
91 . 17 GLU CB C 30.41 . 1
92 . 17 GLU N N 123.16 . 1
93 . 18 THR H H 8.80 . 1
94 . 18 THR HA H 4.90 . 1
95 . 18 THR C C 177.02 . 1
96 . 18 THR CA C 63.17 . 1
97 . 18 THR CB C 69.27 . 1
98 . 18 THR N N 120.01 . 1
99 . 19 LEU H H 10.12 . 1
100 . 19 LEU HA H 4.81 . 1
101 . 19 LEU C C 175.69 . 1
102 . 19 LEU CA C 53.40 . 1
103 . 19 LEU CB C 42.79 . 1
104 . 19 LEU N N 132.44 . 1
105 . 20 THR H H 8.96 . 1
106 . 20 THR HA H 4.97 . 1
107 . 20 THR C C 174.23 . 1
108 . 20 THR CA C 63.97 . 1
109 . 20 THR CB C 70.16 . 1
110 . 20 THR N N 123.88 . 1
111 . 21 THR H H 8.87 . 1
112 . 21 THR HA H 4.71 . 1
113 . 21 THR C C 171.96 . 1
114 . 21 THR CA C 60.27 . 1
115 . 21 THR CB C 70.50 . 1
116 . 21 THR N N 123.66 . 1
117 . 22 LYS H H 8.05 . 1
118 . 22 LYS HA H 5.62 . 1
119 . 22 LYS C C 176.57 . 1
120 . 22 LYS CA C 53.95 . 1
121 . 22 LYS CB C 36.10 . 1
122 . 22 LYS N N 118.92 . 1
123 . 23 GLY H H 8.93 . 1
124 . 23 GLY HA2 H 4.73 . 2
125 . 23 GLY HA3 H 3.32 . 2
126 . 23 GLY C C 171.11 . 1
127 . 23 GLY CA C 43.99 . 1
128 . 23 GLY N N 108.10 . 1
129 . 24 LYS H H 8.85 . 1
130 . 24 LYS HA H 4.71 . 1
131 . 24 LYS C C 176.48 . 1
132 . 24 LYS CA C 55.08 . 1
133 . 24 LYS CB C 33.47 . 1
134 . 24 LYS N N 122.11 . 1
135 . 25 VAL H H 8.50 . 1
136 . 25 VAL HA H 3.22 . 1
137 . 25 VAL C C 177.60 . 1
138 . 25 VAL CA C 65.81 . 1
139 . 25 VAL CB C 31.67 . 1
140 . 25 VAL N N 123.28 . 1
141 . 26 GLY H H 8.91 . 1
142 . 26 GLY HA2 H 4.56 . 2
143 . 26 GLY HA3 H 3.58 . 2
144 . 26 GLY C C 174.54 . 1
145 . 26 GLY CA C 45.26 . 1
146 . 26 GLY N N 117.60 . 1
147 . 27 ASP H H 8.24 . 1
148 . 27 ASP HA H 4.74 . 1
149 . 27 ASP C C 176.56 . 1
150 . 27 ASP CA C 54.77 . 1
151 . 27 ASP CB C 41.48 . 1
152 . 27 ASP N N 123.94 . 1
153 . 28 SER H H 9.80 . 1
154 . 28 SER HA H 4.36 . 1
155 . 28 SER CA C 57.18 . 1
156 . 28 SER CB C 66.03 . 1
157 . 28 SER N N 119.15 . 1
158 . 29 LEU H H 8.31 . 1
159 . 29 LEU HA H 4.58 . 1
160 . 29 LEU CA C 58.04 . 1
161 . 29 LEU CB C 41.04 . 1
162 . 29 LEU N N 119.60 . 1
163 . 30 LEU C C 175.32 . 1
164 . 30 LEU CA C 55.71 . 1
165 . 31 ASP H H 7.74 . 1
166 . 31 ASP HA H 4.38 . 1
167 . 31 ASP C C 177.78 . 1
168 . 31 ASP CA C 58.05 . 1
169 . 31 ASP N N 121.84 . 1
170 . 32 VAL H H 7.82 . 1
171 . 32 VAL HA H 3.85 . 1
172 . 32 VAL C C 178.88 . 1
173 . 32 VAL CA C 66.27 . 1
174 . 32 VAL CB C 32.19 . 1
175 . 32 VAL N N 117.97 . 1
176 . 33 VAL H H 7.52 . 1
177 . 33 VAL HA H 3.06 . 1
178 . 33 VAL C C 178.01 . 1
179 . 33 VAL CA C 67.33 . 1
180 . 33 VAL CB C 32.31 . 1
181 . 33 VAL N N 122.43 . 1
182 . 34 VAL H H 8.48 . 1
183 . 34 VAL HA H 3.76 . 1
184 . 34 VAL C C 181.07 . 1
185 . 34 VAL CA C 66.36 . 1
186 . 34 VAL CB C 32.57 . 1
187 . 34 VAL N N 119.47 . 1
188 . 35 GLU H H 9.22 . 1
189 . 35 GLU HA H 4.03 . 1
190 . 35 GLU C C 177.91 . 1
191 . 35 GLU CA C 59.35 . 1
192 . 35 GLU CB C 29.41 . 1
193 . 35 GLU N N 121.19 . 1
194 . 36 ASN H H 7.21 . 1
195 . 36 ASN HA H 4.73 . 1
196 . 36 ASN C C 173.10 . 1
197 . 36 ASN CA C 53.51 . 1
198 . 36 ASN CB C 39.68 . 1
199 . 36 ASN N N 112.04 . 1
200 . 37 ASN H H 7.90 . 1
201 . 37 ASN HA H 4.40 . 1
202 . 37 ASN C C 174.88 . 1
203 . 37 ASN CA C 54.08 . 1
204 . 37 ASN CB C 37.43 . 1
205 . 37 ASN N N 118.37 . 1
206 . 38 LEU H H 7.84 . 1
207 . 38 LEU HA H 4.02 . 1
208 . 38 LEU C C 178.19 . 1
209 . 38 LEU CA C 55.57 . 1
210 . 38 LEU CB C 42.11 . 1
211 . 38 LEU N N 115.97 . 1
212 . 39 ASP H H 8.68 . 1
213 . 39 ASP HA H 4.55 . 1
214 . 39 ASP C C 174.70 . 1
215 . 39 ASP CA C 53.53 . 1
216 . 39 ASP CB C 39.41 . 1
217 . 39 ASP N N 123.55 . 1
218 . 40 ILE H H 7.67 . 1
219 . 40 ILE HA H 4.20 . 1
220 . 40 ILE C C 175.98 . 1
221 . 40 ILE CA C 60.09 . 1
222 . 40 ILE CB C 38.70 . 1
223 . 40 ILE N N 124.76 . 1
224 . 41 ASP H H 8.63 . 1
225 . 41 ASP HA H 4.37 . 1
226 . 41 ASP C C 178.43 . 1
227 . 41 ASP CA C 56.93 . 1
228 . 41 ASP CB C 41.64 . 1
229 . 41 ASP N N 128.35 . 1
230 . 42 GLY H H 9.15 . 1
231 . 42 GLY HA2 H 4.11 . 2
232 . 42 GLY HA3 H 3.80 . 2
233 . 42 GLY C C 174.08 . 1
234 . 42 GLY CA C 46.24 . 1
235 . 42 GLY N N 114.75 . 1
236 . 43 PHE H H 7.71 . 1
237 . 43 PHE HA H 4.60 . 1
238 . 43 PHE CA C 59.42 . 1
239 . 43 PHE CB C 41.05 . 1
240 . 43 PHE N N 121.68 . 1
241 . 59 PHE H H 8.79 . 1
242 . 59 PHE HA H 4.56 . 1
243 . 59 PHE C C 175.60 . 1
244 . 59 PHE CA C 58.59 . 1
245 . 59 PHE CB C 43.53 . 1
246 . 59 PHE N N 128.40 . 1
247 . 60 GLU H H 9.11 . 1
248 . 60 GLU HA H 4.36 . 1
249 . 60 GLU C C 178.88 . 1
250 . 60 GLU CA C 56.93 . 1
251 . 60 GLU CB C 32.33 . 1
252 . 60 GLU N N 119.55 . 1
253 . 61 ASP H H 9.41 . 1
254 . 61 ASP HA H 4.13 . 1
255 . 61 ASP C C 177.64 . 1
256 . 61 ASP CA C 59.14 . 1
257 . 61 ASP CB C 41.10 . 1
258 . 61 ASP N N 124.59 . 1
259 . 62 HIS H H 8.55 . 1
260 . 62 HIS HA H 4.52 . 1
261 . 62 HIS C C 176.96 . 1
262 . 62 HIS CA C 58.75 . 1
263 . 62 HIS CB C 29.58 . 1
264 . 62 HIS N N 114.63 . 1
265 . 63 ILE H H 6.33 . 1
266 . 63 ILE HA H 3.89 . 1
267 . 63 ILE C C 178.13 . 1
268 . 63 ILE CA C 59.92 . 1
269 . 63 ILE CB C 36.53 . 1
270 . 63 ILE N N 120.80 . 1
271 . 64 TYR H H 8.72 . 1
272 . 64 TYR HA H 3.58 . 1
273 . 64 TYR C C 177.70 . 1
274 . 64 TYR CA C 61.76 . 1
275 . 64 TYR CB C 39.66 . 1
276 . 64 TYR N N 120.57 . 1
277 . 65 GLU H H 7.88 . 1
278 . 65 GLU HA H 4.14 . 1
279 . 65 GLU C C 176.53 . 1
280 . 65 GLU CA C 58.18 . 1
281 . 65 GLU CB C 30.02 . 1
282 . 65 GLU N N 113.85 . 1
283 . 66 LYS H H 7.22 . 1
284 . 66 LYS HA H 4.48 . 1
285 . 66 LYS C C 176.84 . 1
286 . 66 LYS CA C 54.80 . 1
287 . 66 LYS CB C 33.34 . 1
288 . 66 LYS N N 116.52 . 1
289 . 67 LEU H H 6.85 . 1
290 . 67 LEU HA H 4.06 . 1
291 . 67 LEU C C 177.19 . 1
292 . 67 LEU CA C 54.69 . 1
293 . 67 LEU CB C 41.50 . 1
294 . 67 LEU N N 120.64 . 1
295 . 68 ASP H H 9.18 . 1
296 . 68 ASP HA H 4.32 . 1
297 . 68 ASP C C 175.60 . 1
298 . 68 ASP CA C 54.72 . 1
299 . 68 ASP CB C 40.96 . 1
300 . 68 ASP N N 123.38 . 1
301 . 69 ALA H H 8.30 . 1
302 . 69 ALA HA H 4.00 . 1
303 . 69 ALA C C 178.45 . 1
304 . 69 ALA CA C 52.68 . 1
305 . 69 ALA CB C 18.81 . 1
306 . 69 ALA N N 123.03 . 1
307 . 70 ILE H H 8.52 . 1
308 . 70 ILE HA H 4.67 . 1
309 . 70 ILE C C 176.75 . 1
310 . 70 ILE CA C 63.23 . 1
311 . 70 ILE CB C 39.35 . 1
312 . 70 ILE N N 125.25 . 1
313 . 71 THR H H 8.25 . 1
314 . 71 THR HA H 4.51 . 1
315 . 71 THR C C 175.68 . 1
316 . 71 THR CA C 61.18 . 1
317 . 71 THR CB C 72.33 . 1
318 . 71 THR N N 120.05 . 1
319 . 72 ASP H H 9.12 . 1
320 . 72 ASP HA H 4.31 . 1
321 . 72 ASP C C 177.82 . 1
322 . 72 ASP CA C 57.88 . 1
323 . 72 ASP CB C 40.20 . 1
324 . 72 ASP N N 123.46 . 1
325 . 73 GLU H H 9.00 . 1
326 . 73 GLU HA H 4.05 . 1
327 . 73 GLU C C 179.58 . 1
328 . 73 GLU CA C 60.74 . 1
329 . 73 GLU CB C 29.32 . 1
330 . 73 GLU N N 117.93 . 1
331 . 74 GLU H H 7.57 . 1
332 . 74 GLU HA H 4.02 . 1
333 . 74 GLU C C 178.11 . 1
334 . 74 GLU CA C 59.43 . 1
335 . 74 GLU CB C 29.17 . 1
336 . 74 GLU N N 120.30 . 1
337 . 75 ASN H H 8.65 . 1
338 . 75 ASN HA H 4.36 . 1
339 . 75 ASN C C 177.12 . 1
340 . 75 ASN CA C 57.20 . 1
341 . 75 ASN CB C 39.16 . 1
342 . 75 ASN N N 120.64 . 1
343 . 76 ASP H H 8.37 . 1
344 . 76 ASP HA H 4.32 . 1
345 . 76 ASP C C 178.76 . 1
346 . 76 ASP CA C 57.34 . 1
347 . 76 ASP CB C 40.42 . 1
348 . 76 ASP N N 117.86 . 1
349 . 77 MET H H 7.05 . 1
350 . 77 MET HA H 4.57 . 1
351 . 77 MET C C 180.05 . 1
352 . 77 MET CA C 55.78 . 1
353 . 77 MET CB C 34.85 . 1
354 . 77 MET N N 116.67 . 1
355 . 78 LEU H H 8.93 . 1
356 . 78 LEU HA H 3.83 . 1
357 . 78 LEU C C 178.64 . 1
358 . 78 LEU CA C 57.96 . 1
359 . 78 LEU CB C 41.61 . 1
360 . 78 LEU N N 124.74 . 1
361 . 79 ASP H H 8.04 . 1
362 . 79 ASP HA H 4.40 . 1
363 . 79 ASP C C 177.78 . 1
364 . 79 ASP CA C 56.91 . 1
365 . 79 ASP CB C 41.24 . 1
366 . 79 ASP N N 116.31 . 1
367 . 80 LEU H H 7.07 . 1
368 . 80 LEU HA H 4.39 . 1
369 . 80 LEU C C 177.44 . 1
370 . 80 LEU CA C 53.99 . 1
371 . 80 LEU CB C 42.60 . 1
372 . 80 LEU N N 117.42 . 1
373 . 81 ALA H H 7.92 . 1
374 . 81 ALA HA H 4.22 . 1
375 . 81 ALA C C 177.30 . 1
376 . 81 ALA CA C 52.51 . 1
377 . 81 ALA CB C 19.32 . 1
378 . 81 ALA N N 125.16 . 1
379 . 82 TYR H H 8.43 . 1
380 . 82 TYR HA H 4.46 . 1
381 . 82 TYR C C 177.02 . 1
382 . 82 TYR CA C 58.42 . 1
383 . 82 TYR CB C 38.96 . 1
384 . 82 TYR N N 123.92 . 1
385 . 83 GLY H H 8.52 . 1
386 . 83 GLY HA2 H 4.97 . 2
387 . 83 GLY HA3 H 3.71 . 2
388 . 83 GLY C C 174.76 . 1
389 . 83 GLY CA C 46.55 . 1
390 . 83 GLY N N 113.66 . 1
391 . 84 LEU H H 7.31 . 1
392 . 84 LEU HA H 3.89 . 1
393 . 84 LEU C C 176.69 . 1
394 . 84 LEU CA C 57.00 . 1
395 . 84 LEU CB C 42.79 . 1
396 . 84 LEU N N 119.14 . 1
397 . 85 THR H H 8.93 . 1
398 . 85 THR HA H 4.97 . 1
399 . 85 THR C C 174.88 . 1
400 . 85 THR CA C 60.16 . 1
401 . 85 THR CB C 74.50 . 1
402 . 85 THR N N 118.66 . 1
403 . 86 ASP H H 8.57 . 1
404 . 86 ASP HA H 4.55 . 1
405 . 86 ASP C C 176.09 . 1
406 . 86 ASP CA C 54.29 . 1
407 . 86 ASP CB C 39.74 . 1
408 . 86 ASP N N 118.69 . 1
409 . 87 ARG H H 8.39 . 1
410 . 87 ARG HA H 4.26 . 1
411 . 87 ARG C C 175.75 . 1
412 . 87 ARG CA C 53.73 . 1
413 . 87 ARG CB C 30.02 . 1
414 . 87 ARG N N 120.57 . 1
415 . 88 SER H H 7.07 . 1
416 . 88 SER HA H 5.48 . 1
417 . 88 SER C C 174.64 . 1
418 . 88 SER CA C 60.72 . 1
419 . 88 SER CB C 65.48 . 1
420 . 88 SER N N 120.81 . 1
421 . 89 ARG H H 9.46 . 1
422 . 89 ARG HA H 4.87 . 1
423 . 89 ARG CA C 52.93 . 1
424 . 89 ARG CB C 34.17 . 1
425 . 89 ARG N N 118.98 . 1
426 . 94 ILE HA H 4.25 . 1
427 . 94 ILE C C 174.06 . 1
428 . 94 ILE CA C 58.01 . 1
429 . 94 ILE CB C 37.05 . 1
430 . 95 CYS H H 8.20 . 1
431 . 95 CYS HA H 5.00 . 1
432 . 95 CYS C C 175.16 . 1
433 . 95 CYS CA C 57.50 . 1
434 . 95 CYS CB C 29.33 . 1
435 . 95 CYS N N 124.34 . 1
436 . 96 LEU H H 9.05 . 1
437 . 96 LEU HA H 4.76 . 1
438 . 96 LEU C C 178.97 . 1
439 . 96 LEU CA C 55.64 . 1
440 . 96 LEU CB C 42.46 . 1
441 . 96 LEU N N 121.35 . 1
442 . 97 THR H H 7.86 . 1
443 . 97 THR HA H 4.68 . 1
444 . 97 THR C C 175.30 . 1
445 . 97 THR CA C 59.42 . 1
446 . 97 THR CB C 71.69 . 1
447 . 97 THR N N 114.58 . 1
448 . 98 LYS H H 9.28 . 1
449 . 98 LYS HA H 3.92 . 1
450 . 98 LYS C C 179.19 . 1
451 . 98 LYS CA C 59.55 . 1
452 . 98 LYS CB C 32.08 . 1
453 . 98 LYS N N 122.12 . 1
454 . 99 SER H H 8.22 . 1
455 . 99 SER HA H 4.30 . 1
456 . 99 SER C C 174.77 . 1
457 . 99 SER CA C 60.42 . 1
458 . 99 SER CB C 62.69 . 1
459 . 99 SER N N 113.39 . 1
460 . 100 MET H H 7.73 . 1
461 . 100 MET HA H 4.16 . 1
462 . 100 MET C C 174.12 . 1
463 . 100 MET CA C 56.92 . 1
464 . 100 MET CB C 32.37 . 1
465 . 100 MET N N 121.20 . 1
466 . 101 ASP H H 7.27 . 1
467 . 101 ASP HA H 4.41 . 1
468 . 101 ASP C C 177.82 . 1
469 . 101 ASP CA C 57.02 . 1
470 . 101 ASP CB C 40.94 . 1
471 . 101 ASP N N 118.59 . 1
472 . 102 ASN H H 10.06 . 1
473 . 102 ASN HA H 3.88 . 1
474 . 102 ASN C C 174.34 . 1
475 . 102 ASN CA C 55.90 . 1
476 . 102 ASN CB C 38.01 . 1
477 . 102 ASN N N 123.28 . 1
478 . 103 MET H H 8.48 . 1
479 . 103 MET HA H 4.70 . 1
480 . 103 MET C C 173.08 . 1
481 . 103 MET CA C 56.67 . 1
482 . 103 MET CB C 31.45 . 1
483 . 103 MET N N 118.84 . 1
484 . 104 THR H H 8.69 . 1
485 . 104 THR HA H 5.47 . 1
486 . 104 THR C C 175.97 . 1
487 . 104 THR CA C 61.83 . 1
488 . 104 THR CB C 70.59 . 1
489 . 104 THR N N 117.57 . 1
490 . 105 VAL H H 9.19 . 1
491 . 105 VAL HA H 4.62 . 1
492 . 105 VAL CA C 58.32 . 1
493 . 105 VAL CB C 34.48 . 1
494 . 105 VAL N N 123.32 . 1
495 . 106 ARG H H 8.44 . 1
496 . 106 ARG HA H 4.31 . 1
497 . 106 ARG CA C 54.57 . 1
498 . 106 ARG CB C 33.96 . 1
499 . 106 ARG N N 121.33 . 1
500 . 108 PRO HA H 4.30 . 1
501 . 108 PRO C C 176.32 . 1
502 . 108 PRO CA C 62.95 . 1
503 . 108 PRO CB C 32.38 . 1
504 . 109 GLU H H 8.69 . 1
505 . 109 GLU HA H 4.22 . 1
506 . 109 GLU C C 176.48 . 1
507 . 109 GLU CA C 57.22 . 1
508 . 109 GLU CB C 30.91 . 1
509 . 109 GLU N N 121.77 . 1
510 . 110 THR H H 8.38 . 1
511 . 110 THR HA H 4.35 . 1
512 . 110 THR C C 174.09 . 1
513 . 110 THR CA C 61.51 . 1
514 . 110 THR CB C 70.24 . 1
515 . 110 THR N N 115.08 . 1
516 . 111 VAL H H 7.95 . 1
517 . 111 VAL HA H 3.93 . 1
518 . 111 VAL C C 175.46 . 1
519 . 111 VAL CA C 61.87 . 1
520 . 111 VAL CB C 33.20 . 1
521 . 111 VAL N N 122.76 . 1
522 . 112 ALA H H 8.34 . 1
523 . 112 ALA HA H 4.24 . 1
524 . 112 ALA C C 177.55 . 1
525 . 112 ALA CA C 52.47 . 1
526 . 112 ALA CB C 19.67 . 1
527 . 112 ALA N N 129.12 . 1
528 . 113 ASP H H 8.39 . 1
529 . 113 ASP HA H 4.53 . 1
530 . 113 ASP C C 175.09 . 1
531 . 113 ASP CA C 54.62 . 1
532 . 113 ASP CB C 41.16 . 1
533 . 113 ASP N N 121.32 . 1
534 . 114 ALA H H 7.91 . 1
535 . 114 ALA HA H 4.09 . 1
536 . 114 ALA CA C 54.03 . 1
537 . 114 ALA CB C 20.38 . 1
538 . 114 ALA N N 130.28 . 1
stop_
save_