data_4554
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Backbone HN, N, Ca, C' and Cb assignments of the 19 kDa DHFR/NADPH complex at 9C
and pH 7.6
;
_BMRB_accession_number 4554
_BMRB_flat_file_name bmr4554.str
_Entry_type original
_Submission_date 1999-12-10
_Accession_date 1999-12-13
_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 Zaborowski Eduardo . .
2 Chung John . .
3 Kroon Gerard . .
4 Dyson H. Jane .
5 Wright Peter E. .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 147
"13C chemical shifts" 449
"15N chemical shifts" 147
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2000-04-03 original author .
stop_
_Original_release_date 2000-04-03
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Letter to the Editor: Backbone HN, N, Ca, C' and Cb assignments of the
19 kDa DHFR/NADPH complex at 9C and pH 7.6
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Zaborowski Eduardo . .
2 Chung John . .
3 Kroon Gerard . .
4 Dyson H. Jane .
5 Wright Peter E. .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_name_full 'Journal of Biomolecular NMR'
_Journal_volume 16
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 349
_Page_last 350
_Year 2000
_Details .
loop_
_Keyword
'dihydrofolate reductase'
'cofactor complex'
NADPH
stop_
save_
#######################################
# Cited references within the entry #
#######################################
save_ref_1
_Saveframe_category citation
_Citation_full
;
Hsu, M.C., Ho, Y., Huang, F.Y.(1998)
Journal of the Chinese Chemical Society,
45, 115-121.
;
_Citation_title .
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save_ref_2
_Saveframe_category citation
_Citation_full
;
Fierke, C.A., Johnson, K.A., Benkovic, S.J.(1987)
Biochemistry,
26, 4085-4092.
;
_Citation_title 'Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 3307916
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Fierke C.A. A. .
2 Johnson K.A. A. .
3 Benkovic S.J. J. .
stop_
_Journal_abbreviation Biochemistry
_Journal_name_full Biochemistry
_Journal_volume 26
_Journal_issue 13
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
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_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 4085
_Page_last 4092
_Year 1987
_Details
;
A kinetic scheme is presented for Escherichia coli dihydrofolate reductase that
predicts steady-state kinetic parameters and full time course kinetics under a
variety of substrate concentrations and pHs. This scheme was derived from
measuring association and dissociation rate constants and pre-steady-state
transients by using stopped-flow fluorescence and absorbance spectroscopy. The
binding kinetics suggest that during steady-state turnover product dissociation
follows a specific, preferred pathway in which tetrahydrofolate (H4F)
dissociation occurs after NADPH replaces NADP+ in the ternary complex. This
step, H4F dissociation from the E X NADPH X H4F ternary complex, is proposed to
be the rate-limiting step for steady-state turnover at low pH because koff =
VM. The rate constant for hydride transfer from NADPH to dihydrofolate (H2F),
measured by pre-steady-state transients, has a deuterium isotope effect of 3
and is rapid, khyd = 950 s-1, essentially irreversible, Keq = 1700, and pH
dependent, pKa = 6.5, reflecting ionization of a single group in the active
site. This scheme accounts for the apparent pKa = 8.4 observed in the steady
state as due to a change in the rate-determining step from product release at
low pH to hydride transfer above pH 8.4. This kinetic scheme is a necessary
background to analyze the effects of single amino acid substitutions on
individual rate constants.
;
save_
save_ref_3
_Saveframe_category citation
_Citation_full
;
Sawaya, M.R., Kraut, J.(1997)
Biochemistry,
36, 586-603.
;
_Citation_title 'Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 9012674
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Sawaya M.R. R. .
2 Kraut J. . .
stop_
_Journal_abbreviation Biochemistry
_Journal_name_full Biochemistry
_Journal_volume 36
_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 586
_Page_last 603
_Year 1997
_Details
;
The reaction catalyzed by Escherichia coli dihydrofolate reductase (ecDHFR)
cycles through five detectable kinetic intermediates: holoenzyme, Michaelis
complex, ternary product complex, tetrahydrofolate (THF) binary complex, and
THF.NADPH complex. Isomorphous crystal structures analogous to these five
intermediates and to the transition state (as represented by the
methotrexate-NADPH complex) have been used to assemble a 2.1 A resolution movie
depicting loop and subdomain movements during the catalytic cycle (see
Supporting Information). The structures suggest that the M20 loop is
predominantly closed over the reactants in the holoenzyme, Michaelis, and
transition state complexes. But, during the remainder of the cycle, when
nicotinamide is not bound, the loop occludes (protrudes into) the
nicotinamide-ribose binding pocket. Upon changing from the closed to the
occluded conformation, the central portion of the loop rearranges from
beta-sheet to 3(10) helix. The change may occur by way of an irregularly
structured open loop conformation, which could transiently admit a water
molecule into position to protonate N5 of dihydrofolate. From the Michaelis to
the transition state analogue complex, rotation between two halves of ecDHFR,
the adenosine binding subdomain and loop subdomain, closes the
(p-aminobenzoyl)glutamate (pABG) binding crevice by approximately 0.5 A.
Resulting enhancement of contacts with the pABG moiety may stabilize puckering
at C6 of the pteridine ring in the transition state. The subdomain rotation is
further adjusted by cofactor-induced movements (approximately 0.5 A) of helices
B and C, producing a larger pABG cleft in the THF.NADPH analogue complex than
in the THF analogue complex. Such movements may explain how THF release is
assisted by NADPH binding. Subdomain rotation is not observed in vertebrate
DHFR structures, but an analogous loop movement (residues 59-70) appears to
similarly adjust the pABG cleft width, suggesting that these movements are
important for catalysis. Loop movement, also unobserved in vertebrate DHFR
structures, may preferentially weaken NADP+ vs NADPH binding in ecDHFR, an
evolutionary adaptation to reduce product inhibition in the NADP+ rich
environment of prokaryotes.
;
save_
save_ref_4
_Saveframe_category citation
_Citation_full
;
Oppenheimer, N.J.(1982)
in The Pyridine Nucleotide Coenzymes
(Everse, J., Anderson, B., You, K., Eds),
51-89, Academic Press, New York
36, 586-603.
;
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save_ref_5
_Saveframe_category citation
_Citation_full
;
Rafter, G.W. and Colowick, S.P. (1957)
in Methods in Enzymology,
3, 887-890.
;
_Citation_title .
_Citation_status .
_Citation_type .
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
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save_ref_6
_Saveframe_category citation
_Citation_full
;
Grzesiek, S. and Bax, A. (1993)
J. Biomol. NMR,
3, 185-204.
;
_Citation_title 'Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 8477186
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Grzesiek S. . .
2 Bax A. . .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_name_full 'Journal of biomolecular NMR'
_Journal_volume 3
_Journal_issue 2
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
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_Conference_start_date .
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_Thesis_institution .
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_Page_first 185
_Page_last 204
_Year 1993
_Details
;
Experiments and procedures are described that greatly alleviate the sequential
assignment process of uniformly 13C/15N-enriched proteins by determining the
type of amino acid from experiments that correlate side chain with backbone
amide resonances. A recently proposed 3D NMR experiment, CBCA(CO)NH, correlates
C alpha and C beta resonances to the backbone amide 1H and 15N resonances of
the next residue (Grzesiek, S. and Bax, A. (1992) J. Am. Chem. Soc., 114,
6291-6293). An extension of this experiment is described which correlates the
proton H beta and H alpha resonances to the amide 1H and 15N resonances of the
next amino acid, and a detailed product operator description is given. A simple
2D-edited constant-time HSQC experiment is described which rapidly identifies H
beta and C beta resonances of aromatic or Asn/Asp residues. The extent to which
combined knowledge of the C alpha and C beta chemical shift values determines
the amino acid type is investigated, and it is demonstrated that the combined C
alpha and C beta chemical shifts of three or four adjacent residues usually are
sufficient for defining a unique position in the protein sequence.
;
save_
save_ref_7
_Saveframe_category citation
_Citation_full
;
Yamazaki, T., Lee, W., Arrowsmith, C.H., Muhandiram, D.R. and Kay, L.E. (1994)
Journal of the American Chemical Society,
116, 11655-11666.
;
_Citation_title .
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save_ref_8
_Saveframe_category citation
_Citation_full
;
Epstein, D.M., Benkovic, S.J. and Wright, P.E. (1995)
Biochemistry,
34, 11037-11048.
;
_Citation_title 'Dynamics of the dihydrofolate reductase-folate complex: catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 7669761
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Epstein D.M. M. .
2 Benkovic S.J. J. .
3 Wright P.E. E. .
stop_
_Journal_abbreviation Biochemistry
_Journal_name_full Biochemistry
_Journal_volume 34
_Journal_issue 35
_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 .
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_Thesis_institution .
_Thesis_institution_city .
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_Page_first 11037
_Page_last 11048
_Year 1995
_Details
;
Backbone and tryptophan side-chain dynamics of uniformly 15N-labeled Escherichia
coli dihydrofolate reductase were determined for the binary folate complex. The
15N T1 and T2 relaxation times and [1H]-15N heteronuclear NOEs were measured
for 118 protonated backbone nitrogen atoms. The generalized order parameter
(S2), the effective correlation time for internal motions (tau e), and the
contribution to spin-spin relaxation through 15N exchange broadening (Rex) were
determined for each residue by model-free analysis. Back-calculation of the
relaxation rates for each resonance showed that the calculated dynamical
parameters accurately predict the experimental data. Diverse dynamical features
were evident in the DHFR backbone. Six sites exhibited order parameters
significantly below the weighted mean S2 value (for the complex) of 0.81 +/-
0.002: residues G67 and D69 of the adenosine binding domain, and "hinge"
residues K38 and V88, exhibited low S2 (0.29 < or = S2 < or = 0.6) and high tau
e values (700 ps < or = tau e < or = 2 ns), as did sites within the beta
A-alpha B loop and the beta F-beta G loop. Thus, large amplitude backbone
motions, on the picosecond and nanosecond time scales, occurred at regions
implicated in transition-state stabilization and in ligand-dependent
conformational change. Significant Rex values (> or = 1 s-1) were determined
for 45% of assigned resonances, many of which arise from residues surrounding
the folate binding site. The mean S2 values of the occupied folate binding site
and the unoccupied NADPH binding site were similar, indicating the backbone of
the latter is at least as conformationally restricted as that of the occupied
folate site. We conclude that the observed time-dependent structural
fluctuations of the binary complex are in fact associated with catalytic
properties of the molecule.
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save_
save_ref_9
_Saveframe_category citation
_Citation_full
;
Falzone, C.J., Cavanagh, J., Cowart, M., Palmer III, A.G., Matthews, C.R.,
Benkovic, S.J. and Wright, P.E. (1994)
Journal of Biomolecular NMR,
4, 349-366.
;
_Citation_title '1H, 15N and 13C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductase.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 8019142
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Falzone C.J. J. .
2 Cavanagh J. . .
3 Cowart M. . .
4 Palmer A.G. G. 3rd
5 Matthews C.R. R. .
6 Benkovic S.J. J. .
7 Wright P.E. E. .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_name_full 'Journal of biomolecular NMR'
_Journal_volume 4
_Journal_issue 3
_Journal_CSD .
_Book_title .
_Book_chapter_title .
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_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 349
_Page_last 366
_Year 1994
_Details
;
By using fully 15N- and 15N/13C-labeled Escherichia coli dihydrofolate
reductase, the sequence-specific 1H and 15N NMR assignments were achieved for
95% of the backbone resonances and for 90% of the 13C alpha resonances in the
binary folate complex. These assignments were made through a variety of
three-dimensional proton-detected 15N and 13C experiments. A smaller but
significant subset of side-chain 1H and 13C assignments were also determined.
In this complex, only one 15N or 13C resonance was detected per 15N or 13C
protein nucleus, which indicated a single conformation. Proton-detected 13C
experiments were also performed with unlabeled DHFR, complexed with 13C-7/13C-9
folate to probe for multiple conformations of the substrate in its binary
complex. As was found for the protein resonances, only a single bound resonance
corresponding to a productive conformation could be detected for C-7. These
results are consistent with an earlier report based on 1H NMR data [Falzone,
C.J. et al. (1990) Biochemistry, 29, 9667-9677] and suggest that the E. coli
enzyme is not involved in any catalytically unproductive binding modes in the
binary complex. This feature of the E. coli enzyme seems to be unique among the
bacterial forms of DHFR that have been studied to date.
;
save_
##################################
# Molecular system description #
##################################
save_DHFR_NADPH
_Saveframe_category molecular_system
_Mol_system_name 'Dihydrofolate reductase complex with NADPH cofactor'
_Abbreviation_common DHFR_NADPH
_Enzyme_commission_number 1.5.1.3
loop_
_Mol_system_component_name
_Mol_label
DHFR $DHFR
NADPH $NDP
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all free'
loop_
_Biological_function
reductase
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_DHFR
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'Dihydrofolate reductase'
_Abbreviation_common DHFR
_Molecular_mass 18200
_Mol_thiol_state 'all free'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 159
_Mol_residue_sequence
;
MISLIAALAVDRVIGMENAM
PWNLPADLAWFKRNTLNKPV
IMGRHTWESIGRPLPGRKNI
ILSSQPGTDDRVTWVKSVDE
AIAACGDVPEIMVIGGGRVY
EQFLPKAQKLYLTHIDAEVE
GDTHFPDYEPDDWESVFSEF
HDADAQNSHSYCFEILERR
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 ILE 3 SER 4 LEU 5 ILE
6 ALA 7 ALA 8 LEU 9 ALA 10 VAL
11 ASP 12 ARG 13 VAL 14 ILE 15 GLY
16 MET 17 GLU 18 ASN 19 ALA 20 MET
21 PRO 22 TRP 23 ASN 24 LEU 25 PRO
26 ALA 27 ASP 28 LEU 29 ALA 30 TRP
31 PHE 32 LYS 33 ARG 34 ASN 35 THR
36 LEU 37 ASN 38 LYS 39 PRO 40 VAL
41 ILE 42 MET 43 GLY 44 ARG 45 HIS
46 THR 47 TRP 48 GLU 49 SER 50 ILE
51 GLY 52 ARG 53 PRO 54 LEU 55 PRO
56 GLY 57 ARG 58 LYS 59 ASN 60 ILE
61 ILE 62 LEU 63 SER 64 SER 65 GLN
66 PRO 67 GLY 68 THR 69 ASP 70 ASP
71 ARG 72 VAL 73 THR 74 TRP 75 VAL
76 LYS 77 SER 78 VAL 79 ASP 80 GLU
81 ALA 82 ILE 83 ALA 84 ALA 85 CYS
86 GLY 87 ASP 88 VAL 89 PRO 90 GLU
91 ILE 92 MET 93 VAL 94 ILE 95 GLY
96 GLY 97 GLY 98 ARG 99 VAL 100 TYR
101 GLU 102 GLN 103 PHE 104 LEU 105 PRO
106 LYS 107 ALA 108 GLN 109 LYS 110 LEU
111 TYR 112 LEU 113 THR 114 HIS 115 ILE
116 ASP 117 ALA 118 GLU 119 VAL 120 GLU
121 GLY 122 ASP 123 THR 124 HIS 125 PHE
126 PRO 127 ASP 128 TYR 129 GLU 130 PRO
131 ASP 132 ASP 133 TRP 134 GLU 135 SER
136 VAL 137 PHE 138 SER 139 GLU 140 PHE
141 HIS 142 ASP 143 ALA 144 ASP 145 ALA
146 GLN 147 ASN 148 SER 149 HIS 150 SER
151 TYR 152 CYS 153 PHE 154 GLU 155 ILE
156 LEU 157 GLU 158 ARG 159 ARG
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-10-27
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 11492 Dihydrofolate_Reductase_from_E._coli 100.00 158 99.37 99.37 2.54e-111
BMRB 25019 DHFR 100.00 159 100.00 100.00 6.36e-114
PDB 1DDR "Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate And Urea" 100.00 159 100.00 100.00 6.36e-114
PDB 1DDS "Molecule: Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate" 100.00 159 100.00 100.00 6.36e-114
PDB 1DHI "Long-Range Structural Effects In A Second-Site Revertant Of A Mutant Dihydrofolate Reductase" 100.00 159 98.74 99.37 2.37e-112
PDB 1DHJ "Long-Range Structural Effects In A Second-Site Revertant Of A Mutant Dihydrofolate Reductase" 100.00 159 98.11 98.74 3.16e-111
PDB 1DRA "Crystal Structure Of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes And Cooperativi" 100.00 159 98.74 100.00 1.76e-112
PDB 1DRB "Crystal Structure Of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes And Cooperativi" 100.00 159 98.74 99.37 9.71e-112
PDB 1DRE "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.00 159 99.37 100.00 3.90e-113
PDB 1DRH "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" 100.00 159 99.37 100.00 3.90e-113
PDB 1DYH "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" 100.00 159 99.37 100.00 3.90e-113
PDB 1DYI "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" 100.00 159 99.37 100.00 3.90e-113
PDB 1DYJ "Isomorphous Crystal Structures Of Escherichia Coli Dihydrofolate Reductase Complexed With Folate, 5- Deazafolate And 5,10-Didea" 100.00 159 99.37 100.00 3.90e-113
PDB 1JOL "The Crystal Structure Of The Binary Complex Between Folinic Acid (leucovorin) And E. Coli Dihydrofolate Reductase" 100.00 159 99.37 100.00 3.90e-113
PDB 1JOM "The Crystal Structure Of The Binary Complex Between Folinic Acid (leucovorin) And E. Coli Dihydrofolate Reductase" 100.00 159 99.37 100.00 3.90e-113
PDB 1RA1 "Dihydrofolate Reductase Complexed With Nicotinamide Adenine Dinucleotide Phosphate (Reduced Form)" 100.00 159 99.37 100.00 3.90e-113
PDB 1RA2 "Dihydrofolate Reductase Complexed With Folate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.00 159 99.37 100.00 3.90e-113
PDB 1RA3 "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (oxidized Form)" 100.00 159 99.37 100.00 3.90e-113
PDB 1RA8 "Dihydrofolate Reductase Complexed With Folate And 2- Monophosphoadenosine 5'-diphosphoribose" 100.00 159 99.37 100.00 3.90e-113
PDB 1RA9 "Dihydrofolate Reductase Complexed With Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.00 159 99.37 100.00 3.90e-113
PDB 1RB2 "Dihydrofolate Reductase Complexed With Folate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.00 159 99.37 100.00 3.90e-113
PDB 1RB3 "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (oxidized Form)" 100.00 159 99.37 100.00 3.90e-113
PDB 1RC4 "Dihydrofolate Reductase Complexed With 5,10- Dideazatetrahydrofolate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized " 100.00 159 99.37 100.00 3.90e-113
PDB 1RD7 "Dihydrofolate Reductase Complexed With Folate" 100.00 159 99.37 100.00 3.90e-113
PDB 1RE7 "Dihydrofolate Reductase Complexed With Folate" 100.00 159 99.37 100.00 3.90e-113
PDB 1RF7 "Structure Of Dihydrofolate Reductase Complexed With Dihydrofolate" 100.00 159 99.37 100.00 3.90e-113
PDB 1RG7 "Dihydrofolate Reductase Complexed With Methotrexate" 100.00 159 99.37 100.00 3.90e-113
PDB 1RH3 "Dihydrofolate Reductase Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (Reduced Form)" 100.00 159 99.37 100.00 3.90e-113
PDB 1RX1 "Dihydrofolate Reductase (e.c.1.5.1.3) Complexed With Nicotinamide Adenine Dinucleotide Phosphate (reduced Form)" 100.00 159 99.37 100.00 3.90e-113
PDB 1RX2 "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With With Folate And Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form" 100.00 159 99.37 100.00 3.90e-113
PDB 1RX3 "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Methotrexate And Nicotinamide Adenine Dinucleotide Phosphate (Reduced Form" 100.00 159 99.37 100.00 3.90e-113
PDB 1RX4 "Dihydrofolate Reductase (e.c.1.5.1.3) Complexed With 5,10- Dideazatetrahydrofolate And 2'-monophosphoadenosine 5'- Diphosphorib" 100.00 159 99.37 100.00 3.90e-113
PDB 1RX5 "Dihydrofolate Reductase (e.c.1.5.1.3) Complexed With 5,10- Dideazatetrahydrofolate" 100.00 159 99.37 100.00 3.90e-113
PDB 1RX6 "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With 5,10- Dideazatetrahydrofolate And Nicotinamide Adenine Dinucleotide Phosph" 100.00 159 99.37 100.00 3.90e-113
PDB 1RX7 "Structure Of Dihydrofolate Reductase Complexed With Folate" 100.00 159 99.37 100.00 3.90e-113
PDB 1RX8 "Dihydrofolate Reductase Complexed With Folate And 2'- Monophosphoadenosine 5'-Diphosphoribose" 100.00 159 99.37 100.00 3.90e-113
PDB 1RX9 "Dihydrofolate Reductase (E.C.1.5.1.3) Complexed With Nicotinamide Adenine Dinucleotide Phosphate (Oxidized Form)" 100.00 159 99.37 100.00 3.90e-113
PDB 1TDR "Expression, Characterization, And Crystallographic Analysis Of Telluromethionyl Dihydrofolate Reductase" 100.00 159 98.74 100.00 1.40e-112
PDB 2ANO "Crystal Structure Of E.coli Dihydrofolate Reductase In Complex With Nadph And The Inhibitor Ms-sh08-17" 100.00 159 99.37 100.00 3.90e-113
PDB 2ANQ "Crystal Structure Of E.coli Dhfr In Complex With Nadph And The Inhibitor Compound 10a." 100.00 159 99.37 100.00 3.90e-113
PDB 2DRC "Investigation Of The Functional Role Of Tryptophan-22 In Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis" 100.00 159 98.74 100.00 4.05e-112
PDB 2INQ "Neutron Crystal Structure Of Escherichia Coli Dihydrofolate Reductase Bound To The Anti-Cancer Drug, Methotrexate" 100.00 159 99.37 100.00 3.90e-113
PDB 3DAU "Crystal Structure Of The Ternary Mtx Nadph Complex Of Escherichia Coli Dihydrofolate Reductase" 100.00 159 100.00 100.00 6.36e-114
PDB 3DRC "Investigation Of The Functional Role Of Tryptophan-22 In Escherichia Coli Dihydrofolate Reductase By Site-Directed Mutagenesis" 100.00 159 99.37 100.00 3.90e-113
PDB 3K74 "Disruption Of Protein Dynamics By An Allosteric Effector Antibody" 100.00 159 100.00 100.00 6.36e-114
PDB 3KFY "Dynamic Switching And Partial Occupancies Of A Small Molecule Inhibitor Complex Of Dhfr" 100.00 159 99.37 100.00 3.90e-113
PDB 3OCH "Chemically Self-Assembled Antibody Nanorings (Csans): Design And Characterization Of An Anti-Cd3 Igm Biomimetic" 100.00 159 99.37 100.00 3.90e-113
PDB 3QL0 "Crystal Structure Of N23pp/s148a Mutant Of E. Coli Dihydrofolate Reductase" 100.63 160 98.13 98.75 3.74e-110
PDB 3QL3 "Re-refined Coordinates For Pdb Entry 1rx2" 100.00 159 99.37 100.00 3.90e-113
PDB 3QYL "Sensitivity Of Receptor Internal Motions To Ligand Binding Affinity And Kinetic Off-rate" 100.00 159 99.37 100.00 3.90e-113
PDB 3QYO "Sensitivity Of Receptor Internal Motions To Ligand Binding Affinity And Kinetic Off-rate" 100.00 159 99.37 100.00 3.90e-113
PDB 3R33 "Evidence For Dynamic Motion In Proteins As A Mechanism For Ligand Dissociation" 100.00 159 99.37 100.00 3.90e-113
PDB 4DFR "Crystal Structures Of Escherichia Coli And Lactobacillus Casei Dihydrofolate Reductase Refined At 1.7 Angstroms Resolution. I. " 100.00 159 98.74 100.00 1.40e-112
PDB 4EIG "Ca1698 Camel Antibody Fragment In Complex With Dhfr" 100.00 159 100.00 100.00 6.36e-114
PDB 4EIZ "Structure Of Nb113 Bound To Apodhfr" 100.00 159 100.00 100.00 6.36e-114
PDB 4EJ1 "Binding Of Nb113 Camelid Antibody Fragment With The Binary Dhfr:folate Complex" 100.00 159 100.00 100.00 6.36e-114
PDB 4FHB "Enhancing Dhfr Catalysis By Binding Of An Allosteric Regulator Nanobody (nb179)" 100.00 159 100.00 100.00 6.36e-114
PDB 4I13 "Nanobody Ca1697 Binding To The Dhfr.folate Binary Complex" 100.00 159 100.00 100.00 6.36e-114
PDB 4I1N "R104a-ca1697 Nanobody Binding To The Binary Dhfr.folate Complex" 100.00 159 100.00 100.00 6.36e-114
PDB 4KJJ "Cryogenic Wt Dhfr" 100.00 159 100.00 100.00 6.36e-114
PDB 4KJK "Room Temperature Wt Dhfr" 100.00 159 100.00 100.00 6.36e-114
PDB 4KJL "Room Temperature N23pps148a Dhfr" 100.63 160 98.13 98.75 3.74e-110
PDB 4NX6 "Single Room Temperature Model Of Dhfr" 100.00 159 100.00 100.00 6.36e-114
PDB 4NX7 "Single Cryogenic Temperature Model Of Dhfr" 100.00 159 100.00 100.00 6.36e-114
PDB 4P3Q "Room-temperature Wt Dhfr, Time-averaged Ensemble" 100.00 159 100.00 100.00 6.36e-114
PDB 4P3R "Cryogenic Wt Dhfr, Time-averaged Ensemble" 100.00 159 100.00 100.00 6.36e-114
PDB 4P66 "Electrostatics Of Active Site Microenvironments Of E. Coli Dhfr" 100.00 159 98.11 98.11 1.21e-110
PDB 4P68 "Electrostatics Of Active Site Microenvironments For E. Coli Dhfr" 100.00 159 98.11 98.11 1.01e-110
PDB 4PSS "Multiconformer Model For Escherichia Coli Dihydrofolate Reductase At 100k" 100.00 159 99.37 99.37 2.15e-112
PDB 4PST "Multiconformer Model For Escherichia Coli Dihydrofolate Reductase At 277 K" 100.00 159 99.37 99.37 2.15e-112
PDB 4PSY "100k Crystal Structure Of Escherichia Coli Dihydrofolate Reductase" 100.00 159 99.37 99.37 2.15e-112
PDB 4PTH "Ensemble Model For Escherichia Coli Dihydrofolate Reductase At 100k" 100.00 159 99.37 99.37 2.15e-112
PDB 4PTJ "Ensemble Model For Escherichia Coli Dihydrofolate Reductase At 277k" 100.00 159 99.37 99.37 2.15e-112
PDB 4QLE "Crystal Structure Of I14a Dhfr Mutant Complexed With Folate And Nadp+" 100.00 159 99.37 99.37 3.99e-113
PDB 4QLF "Crystal Structure Of I14g Dhfr Mutant Complexed With Folate And Nadp+" 100.00 159 99.37 99.37 1.27e-112
PDB 4QLG "Crystal Structure Of I14v Dhfr Mutant Complexed With Folate And Nadp+" 100.00 159 99.37 100.00 1.05e-113
PDB 4RGC "277k Crystal Structure Of Escherichia Coli Dihydrofolate Reductase" 100.00 159 99.37 99.37 2.15e-112
PDB 5CC9 "L28f E.coli Dihydrofolate Reductase Complexed With 5,10- Dideazatetrahydrofolate And Oxidized Nicotinamide Adenine Dinucleotide" 100.00 159 99.37 99.37 2.47e-113
PDB 5CCC "Wild-type E.coli Dihydrofolate Reductase Complexed With 5,10- Dideazatetrahydrofolate And Oxidized Nicotinamide Adenine Dinucle" 100.00 159 100.00 100.00 6.36e-114
PDB 5DFR "Crystal Structure Of Unliganded Escherichia Coli Dihydrofolate Reductase. Ligand-Induced Conformational Changes And Cooperativi" 100.00 159 99.37 100.00 3.90e-113
PDB 6DFR "Crystal Structures Of Escherichia Coli Dihydrofolate Reductase. The Nadp+ Holoenzyme And The Folate(Dot)nadp+ Ternary Complex. " 100.00 159 99.37 100.00 3.90e-113
PDB 7DFR "Crystal Structures Of Escherichia Coli Dihydrofolate Reductase. The Nadp+ Holoenzyme And The Folate(Dot)nadp+ Ternary Complex. " 100.00 159 99.37 100.00 3.90e-113
DBJ BAA05974 "fusion protein, composed of HCV p21 (NS2), E.coli dihydroforate reductase, substrate polypeptide for HCV serine proteinase and " 99.37 847 100.00 100.00 1.17e-105
DBJ BAB33474 "dihydrofolate reductase type I; trimethoprim resistance [Escherichia coli O157:H7 str. Sakai]" 100.00 159 99.37 99.37 2.37e-112
DBJ BAB96616 "dihydrofolate reductase [Escherichia coli str. K12 substr. W3110]" 100.00 159 100.00 100.00 6.36e-114
DBJ BAG75573 "dihydrofolate reductase [Escherichia coli SE11]" 100.00 159 100.00 100.00 6.36e-114
DBJ BAI23410 "dihydrofolate reductase [Escherichia coli O26:H11 str. 11368]" 100.00 159 100.00 100.00 6.36e-114
EMBL CAA28755 "unnamed protein product [Escherichia coli]" 100.00 159 98.74 99.37 5.15e-112
EMBL CAD01243 "dihydrofolate reductase type I [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 159 97.48 98.74 6.99e-112
EMBL CAP74618 "Dihydrofolate reductase [Escherichia coli LF82]" 100.00 159 100.00 100.00 6.36e-114
EMBL CAQ30568 "dihydrofolate reductase [Escherichia coli BL21(DE3)]" 100.00 159 100.00 100.00 6.36e-114
EMBL CAQ87642 "dihydrofolate reductase [Escherichia fergusonii ATCC 35469]" 100.00 159 100.00 100.00 6.36e-114
GB AAA87976 "dihydrofolate reductase [Escherichia coli]" 100.00 159 100.00 100.00 6.36e-114
GB AAC73159 "dihydrofolate reductase [Escherichia coli str. K-12 substr. MG1655]" 100.00 159 100.00 100.00 6.36e-114
GB AAG54351 "dihydrofolate reductase type I; trimethoprim resistance [Escherichia coli O157:H7 str. EDL933]" 100.00 159 99.37 99.37 2.37e-112
GB AAN41711 "dihydrofolate reductase type I [Shigella flexneri 2a str. 301]" 100.00 159 100.00 100.00 6.36e-114
GB AAN78554 "Dihydrofolate reductase [Escherichia coli CFT073]" 100.00 204 100.00 100.00 9.78e-114
PIR AC0513 "dihydrofolate reductase type I [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 159 97.48 98.74 6.99e-112
REF NP_308078 "dihydrofolate reductase [Escherichia coli O157:H7 str. Sakai]" 100.00 159 99.37 99.37 2.37e-112
REF NP_414590 "dihydrofolate reductase [Escherichia coli str. K-12 substr. MG1655]" 100.00 159 100.00 100.00 6.36e-114
REF NP_454699 "dihydrofolate reductase type I [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 159 97.48 98.74 6.99e-112
REF NP_706004 "dihydrofolate reductase [Shigella flexneri 2a str. 301]" 100.00 159 100.00 100.00 6.36e-114
REF WP_000378105 "MULTISPECIES: dihydrofolate reductase [Proteobacteria]" 100.00 196 100.00 100.00 1.16e-113
SP P0ABQ4 "RecName: Full=Dihydrofolate reductase" 100.00 159 100.00 100.00 6.36e-114
SP P0ABQ5 "RecName: Full=Dihydrofolate reductase" 100.00 159 100.00 100.00 6.36e-114
SP P0ABQ6 "RecName: Full=Dihydrofolate reductase" 100.00 159 100.00 100.00 6.36e-114
stop_
save_
#############
# Ligands #
#############
save_NDP
_Saveframe_category ligand
_Mol_type non-polymer
_Name_common "NDP (NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE)"
_BMRB_code .
_PDB_code NDP
_Molecular_mass 745.421
_Mol_charge 0
_Mol_paramagnetic .
_Mol_aromatic yes
_Details
;
Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Mon Jul 18 09:25:37 2011
;
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
PA PA P . 0 . ?
O1A O1A O . 0 . ?
O2A O2A O . 0 . ?
O5B O5B O . 0 . ?
C5B C5B C . 0 . ?
C4B C4B C . 0 . ?
O4B O4B O . 0 . ?
C3B C3B C . 0 . ?
O3B O3B O . 0 . ?
C2B C2B C . 0 . ?
O2B O2B O . 0 . ?
C1B C1B C . 0 . ?
N9A N9A N . 0 . ?
C8A C8A C . 0 . ?
N7A N7A N . 0 . ?
C5A C5A C . 0 . ?
C6A C6A C . 0 . ?
N6A N6A N . 0 . ?
N1A N1A N . 0 . ?
C2A C2A C . 0 . ?
N3A N3A N . 0 . ?
C4A C4A C . 0 . ?
O3 O3 O . 0 . ?
PN PN P . 0 . ?
O1N O1N O . 0 . ?
O2N O2N O . 0 . ?
O5D O5D O . 0 . ?
C5D C5D C . 0 . ?
C4D C4D C . 0 . ?
O4D O4D O . 0 . ?
C3D C3D C . 0 . ?
O3D O3D O . 0 . ?
C2D C2D C . 0 . ?
O2D O2D O . 0 . ?
C1D C1D C . 0 . ?
N1N N1N N . 0 . ?
C2N C2N C . 0 . ?
C3N C3N C . 0 . ?
C7N C7N C . 0 . ?
O7N O7N O . 0 . ?
N7N N7N N . 0 . ?
C4N C4N C . 0 . ?
C5N C5N C . 0 . ?
C6N C6N C . 0 . ?
P2B P2B P . 0 . ?
O1X O1X O . 0 . ?
O2X O2X O . 0 . ?
O3X O3X O . 0 . ?
HOA2 HOA2 H . 0 . ?
H51A H51A H . 0 . ?
H52A H52A H . 0 . ?
H4B H4B H . 0 . ?
H3B H3B H . 0 . ?
HO3A HO3A H . 0 . ?
H2B H2B H . 0 . ?
H1B H1B H . 0 . ?
H8A H8A H . 0 . ?
H61A H61A H . 0 . ?
H62A H62A H . 0 . ?
H2A H2A H . 0 . ?
H21N H21N H . 0 . ?
H51N H51N H . 0 . ?
H52N H52N H . 0 . ?
H4D H4D H . 0 . ?
H3D H3D H . 0 . ?
HO3N HO3N H . 0 . ?
H2D H2D H . 0 . ?
HO2N HO2N H . 0 . ?
H1D H1D H . 0 . ?
H2N H2N H . 0 . ?
H71N H71N H . 0 . ?
H72N H72N H . 0 . ?
H41N H41N H . 0 . ?
H42N H42N H . 0 . ?
H5N H5N H . 0 . ?
H6N H6N H . 0 . ?
HOP2 HOP2 H . 0 . ?
HOP3 HOP3 H . 0 . ?
stop_
loop_
_Bond_order
_Bond_atom_one_atom_name
_Bond_atom_two_atom_name
_PDB_bond_atom_one_atom_name
_PDB_bond_atom_two_atom_name
DOUB PA O1A ? ?
SING PA O2A ? ?
SING PA O5B ? ?
SING PA O3 ? ?
SING O2A HOA2 ? ?
SING O5B C5B ? ?
SING C5B C4B ? ?
SING C5B H51A ? ?
SING C5B H52A ? ?
SING C4B O4B ? ?
SING C4B C3B ? ?
SING C4B H4B ? ?
SING O4B C1B ? ?
SING C3B O3B ? ?
SING C3B C2B ? ?
SING C3B H3B ? ?
SING O3B HO3A ? ?
SING C2B O2B ? ?
SING C2B C1B ? ?
SING C2B H2B ? ?
SING O2B P2B ? ?
SING C1B N9A ? ?
SING C1B H1B ? ?
SING N9A C8A ? ?
SING N9A C4A ? ?
DOUB C8A N7A ? ?
SING C8A H8A ? ?
SING N7A C5A ? ?
SING C5A C6A ? ?
DOUB C5A C4A ? ?
SING C6A N6A ? ?
DOUB C6A N1A ? ?
SING N6A H61A ? ?
SING N6A H62A ? ?
SING N1A C2A ? ?
DOUB C2A N3A ? ?
SING C2A H2A ? ?
SING N3A C4A ? ?
SING O3 PN ? ?
DOUB PN O1N ? ?
SING PN O2N ? ?
SING PN O5D ? ?
SING O2N H21N ? ?
SING O5D C5D ? ?
SING C5D C4D ? ?
SING C5D H51N ? ?
SING C5D H52N ? ?
SING C4D O4D ? ?
SING C4D C3D ? ?
SING C4D H4D ? ?
SING O4D C1D ? ?
SING C3D O3D ? ?
SING C3D C2D ? ?
SING C3D H3D ? ?
SING O3D HO3N ? ?
SING C2D O2D ? ?
SING C2D C1D ? ?
SING C2D H2D ? ?
SING O2D HO2N ? ?
SING C1D N1N ? ?
SING C1D H1D ? ?
SING N1N C2N ? ?
SING N1N C6N ? ?
DOUB C2N C3N ? ?
SING C2N H2N ? ?
SING C3N C7N ? ?
SING C3N C4N ? ?
DOUB C7N O7N ? ?
SING C7N N7N ? ?
SING N7N H71N ? ?
SING N7N H72N ? ?
SING C4N C5N ? ?
SING C4N H41N ? ?
SING C4N H42N ? ?
DOUB C5N C6N ? ?
SING C5N H5N ? ?
SING C6N H6N ? ?
DOUB P2B O1X ? ?
SING P2B O2X ? ?
SING P2B O3X ? ?
SING O2X HOP2 ? ?
SING O3X HOP3 ? ?
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
_Strain
_Plasmid
$DHFR 'E. coli' 562 Eubacteria . Escherichia coli K12 pET-22b+
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
_Vendor_name
_Details
$DHFR 'recombinant technology' 'E. coli' . . K12 plasmid pET-22b+ . .
$NDP vendor . . . . . . Sigma 'Enzymatically reduced'
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
$DHFR 1.0 mM '[U-13C; U-15N]'
NADPH 40.0 mM .
'potassium phosphate' 70.0 mM .
KCl 25.0 mM .
D2O 7 % '[U-99.99% 2H]'
NaN3 0.02 % .
DTT 1 mM .
DSS 20 uM .
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$DHFR 1.0 mM '[U-13C; U-15N; U-2H]'
NADPH 40.0 mM .
'potassium phosphate' 40.0 mM .
KCl 25.0 mM .
D2O 7 % .
NaN3 0.02 % .
DTT 1.0 mM .
DSS 20.0 uM .
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version .
loop_
_Task
'spectrum processing'
stop_
_Details .
save_
save_NMRView
_Saveframe_category software
_Name NMRView
_Version .
loop_
_Task
'spectrum analysis and assignment'
stop_
_Details .
save_
save_seq_prob
_Saveframe_category software
_Name seq_prob
_Version .
loop_
_Task
'sequence specific assignment'
stop_
_Details .
_Citation_label $ref_6
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AMX
_Field_strength 500
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AMX-II
_Field_strength 500
_Details .
save_
save_NMR_spectrometer_3
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AMX
_Field_strength 600
_Details .
save_
save_NMR_spectrometer_4
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_15N-HSQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name 15N-HSQC
_Sample_label .
save_
save_HNCA_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_Sample_label .
save_
save_HNCACB_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_Sample_label .
save_
save_CBCA(CO)NH_4
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCA(CO)NH
_Sample_label .
save_
save_HNCO_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_Sample_label .
save_
save_HN(CA)CO_6
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CA)CO
_Sample_label .
save_
save_15N-HSQC-NOESY-HSQC_7
_Saveframe_category NMR_applied_experiment
_Experiment_name 15N-HSQC-NOESY-HSQC
_Sample_label .
save_
save_ddHNCA_8
_Saveframe_category NMR_applied_experiment
_Experiment_name ddHNCA
_Sample_label .
save_
save_ddHN(CO)CA_9
_Saveframe_category NMR_applied_experiment
_Experiment_name ddHN(CO)CA
_Sample_label .
save_
save_ddHN(CA)CB_10
_Saveframe_category NMR_applied_experiment
_Experiment_name ddHN(CA)CB
_Sample_label .
save_
save_ddHN(CO)CACB_11
_Saveframe_category NMR_applied_experiment
_Experiment_name ddHN(CO)CACB
_Sample_label .
save_
save_dd_-_deuterium_decoupled_experiments_12
_Saveframe_category NMR_applied_experiment
_Experiment_name 'dd - deuterium decoupled experiments'
_Sample_label .
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name 15N-HSQC
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCACB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_4
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCA(CO)NH
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_6
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CA)CO
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_7
_Saveframe_category NMR_applied_experiment
_Experiment_name 15N-HSQC-NOESY-HSQC
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_8
_Saveframe_category NMR_applied_experiment
_Experiment_name ddHNCA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_9
_Saveframe_category NMR_applied_experiment
_Experiment_name ddHN(CO)CA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_10
_Saveframe_category NMR_applied_experiment
_Experiment_name ddHN(CA)CB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_11
_Saveframe_category NMR_applied_experiment
_Experiment_name ddHN(CO)CACB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_12
_Saveframe_category NMR_applied_experiment
_Experiment_name 'dd - deuterium decoupled experiments'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 7.6 0.1 n/a
temperature 282 0.1 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference_set_1
_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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0
DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118
DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530
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_assigned_chemical_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Experiment_label
15N-HSQC
HNCA
HNCACB
CBCA(CO)NH
HNCO
HN(CA)CO
15N-HSQC-NOESY-HSQC
ddHNCA
ddHN(CO)CA
ddHN(CA)CB
ddHN(CO)CACB
'dd - deuterium decoupled experiments'
stop_
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $cond_1
_Chem_shift_reference_set_label $chemical_shift_reference_set_1
_Mol_system_component_name DHFR
_Text_data_format .
_Text_data .
loop_
_Atom_shift_assign_ID
_Residue_author_seq_code
_Residue_seq_code
_Residue_label
_Atom_name
_Atom_type
_Chem_shift_value
_Chem_shift_value_error
_Chem_shift_ambiguity_code
1 . 1 MET CA C 55.509 . 1
2 . 1 MET CB C 32.998 . 1
3 . 2 ILE N N 124.139 . 1
4 . 2 ILE H H 9.428 . 1
5 . 2 ILE CA C 61.227 . 1
6 . 2 ILE CB C 39.116 . 1
7 . 2 ILE C C 174.439 . 1
8 . 3 SER N N 125.727 . 1
9 . 3 SER H H 9.414 . 1
10 . 3 SER CA C 56.372 . 1
11 . 3 SER CB C 65.647 . 1
12 . 3 SER C C 173.602 . 1
13 . 4 LEU N N 121.477 . 1
14 . 4 LEU H H 8.503 . 1
15 . 4 LEU CA C 53.446 . 1
16 . 4 LEU CB C 43.633 . 1
17 . 4 LEU C C 175.507 . 1
18 . 5 ILE N N 119.082 . 1
19 . 5 ILE H H 8.468 . 1
20 . 5 ILE CA C 57.940 . 1
21 . 5 ILE CB C 41.612 . 1
22 . 5 ILE C C 172.998 . 1
23 . 6 ALA N N 128.256 . 1
24 . 6 ALA H H 8.672 . 1
25 . 6 ALA CA C 52.264 . 1
26 . 6 ALA CB C 26.631 . 1
27 . 6 ALA C C 174.299 . 1
28 . 7 ALA N N 127.606 . 1
29 . 7 ALA H H 10.408 . 1
30 . 7 ALA CA C 50.950 . 1
31 . 7 ALA CB C 20.864 . 1
32 . 7 ALA C C 174.717 . 1
33 . 8 LEU N N 122.570 . 1
34 . 8 LEU H H 9.139 . 1
35 . 8 LEU CA C 54.017 . 1
36 . 8 LEU CB C 45.871 . 1
37 . 8 LEU C C 175.972 . 1
38 . 9 ALA N N 126.109 . 1
39 . 9 ALA H H 8.644 . 1
40 . 9 ALA CA C 49.915 . 1
41 . 9 ALA CB C 19.396 . 1
42 . 9 ALA C C 176.204 . 1
43 . 10 VAL N N 117.960 . 1
44 . 10 VAL H H 7.636 . 1
45 . 10 VAL CA C 65.081 . 1
46 . 10 VAL CB C 31.628 . 1
47 . 10 VAL C C 177.970 . 1
48 . 11 ASP N N 122.427 . 1
49 . 11 ASP H H 9.247 . 1
50 . 11 ASP CA C 56.037 . 1
51 . 11 ASP CB C 38.734 . 1
52 . 11 ASP C C 174.903 . 1
53 . 12 ARG N N 107.745 . 1
54 . 12 ARG H H 8.530 . 1
55 . 12 ARG CA C 57.354 . 1
56 . 12 ARG CB C 27.627 . 1
57 . 12 ARG C C 175.740 . 1
58 . 13 VAL N N 120.461 . 1
59 . 13 VAL H H 7.100 . 1
60 . 13 VAL CA C 66.022 . 1
61 . 13 VAL CB C 33.050 . 1
62 . 14 ILE CA C 60.770 . 1
63 . 14 ILE CB C 41.092 . 1
64 . 14 ILE C C 175.577 . 1
65 . 15 GLY N N 105.202 . 1
66 . 15 GLY H H 7.318 . 1
67 . 15 GLY CA C 45.156 . 1
68 . 15 GLY C C 170.884 . 1
69 . 16 MET N N 119.421 . 1
70 . 16 MET H H 8.763 . 1
71 . 16 MET CA C 55.335 . 1
72 . 16 MET CB C 34.818 . 1
73 . 17 GLU N N 130.383 . 1
74 . 17 GLU H H 10.204 . 1
75 . 17 GLU CA C 57.611 . 1
76 . 17 GLU CB C 27.052 . 1
77 . 17 GLU C C 175.577 . 1
78 . 18 ASN N N 114.761 . 1
79 . 18 ASN H H 9.778 . 1
80 . 18 ASN CA C 54.293 . 1
81 . 18 ASN CB C 38.749 . 1
82 . 18 ASN C C 175.577 . 1
83 . 19 ALA N N 119.752 . 1
84 . 19 ALA H H 7.572 . 1
85 . 19 ALA CA C 50.367 . 1
86 . 19 ALA CB C 22.174 . 1
87 . 19 ALA C C 176.367 . 1
88 . 20 MET N N 120.626 . 1
89 . 20 MET H H 8.543 . 1
90 . 20 MET CA C 52.916 . 1
91 . 20 MET CB C 32.114 . 1
92 . 21 PRO CA C 62.534 . 1
93 . 21 PRO CB C 28.919 . 1
94 . 21 PRO C C 173.881 . 1
95 . 22 TRP N N 116.084 . 1
96 . 22 TRP H H 7.259 . 1
97 . 22 TRP CA C 57.283 . 1
98 . 22 TRP CB C 29.010 . 1
99 . 22 TRP C C 173.649 . 1
100 . 23 ASN N N 116.606 . 1
101 . 23 ASN H H 8.943 . 1
102 . 23 ASN CA C 53.318 . 1
103 . 23 ASN CB C 40.188 . 1
104 . 23 ASN C C 173.091 . 1
105 . 24 LEU N N 126.273 . 1
106 . 24 LEU H H 9.394 . 1
107 . 24 LEU CA C 51.668 . 1
108 . 24 LEU CB C 43.763 . 1
109 . 25 PRO CA C 65.319 . 1
110 . 25 PRO CB C 31.490 . 1
111 . 25 PRO C C 179.294 . 1
112 . 26 ALA N N 120.775 . 1
113 . 26 ALA H H 9.436 . 1
114 . 26 ALA CA C 55.064 . 1
115 . 26 ALA CB C 19.304 . 1
116 . 26 ALA C C 181.385 . 1
117 . 27 ASP N N 117.260 . 1
118 . 27 ASP H H 7.740 . 1
119 . 27 ASP CA C 57.083 . 1
120 . 27 ASP CB C 43.412 . 1
121 . 27 ASP C C 177.598 . 1
122 . 28 LEU N N 118.610 . 1
123 . 28 LEU H H 7.568 . 1
124 . 28 LEU CA C 58.210 . 1
125 . 28 LEU CB C 40.330 . 1
126 . 28 LEU C C 180.316 . 1
127 . 29 ALA N N 120.365 . 1
128 . 29 ALA H H 7.734 . 1
129 . 29 ALA CA C 55.091 . 1
130 . 29 ALA CB C 18.052 . 1
131 . 29 ALA C C 178.795 . 1
132 . 30 TRP N N 123.417 . 1
133 . 30 TRP H H 7.308 . 1
134 . 30 TRP CA C 59.982 . 1
135 . 30 TRP CB C 29.996 . 1
136 . 30 TRP C C 177.738 . 1
137 . 31 PHE N N 122.806 . 1
138 . 31 PHE H H 9.373 . 1
139 . 31 PHE CA C 63.312 . 1
140 . 31 PHE CB C 38.873 . 1
141 . 31 PHE C C 179.526 . 1
142 . 32 LYS N N 121.564 . 1
143 . 32 LYS H H 8.556 . 1
144 . 32 LYS CA C 60.460 . 1
145 . 32 LYS CB C 32.522 . 1
146 . 32 LYS C C 178.016 . 1
147 . 33 ARG N N 116.397 . 1
148 . 33 ARG H H 7.884 . 1
149 . 33 ARG CA C 58.692 . 1
150 . 33 ARG CB C 29.764 . 1
151 . 33 ARG C C 178.435 . 1
152 . 34 ASN N N 111.439 . 1
153 . 34 ASN H H 7.102 . 1
154 . 34 ASN CA C 54.505 . 1
155 . 34 ASN CB C 39.262 . 1
156 . 35 THR N N 106.642 . 1
157 . 35 THR H H 7.142 . 1
158 . 35 THR CA C 61.829 . 1
159 . 35 THR CB C 70.543 . 1
160 . 35 THR C C 174.485 . 1
161 . 36 LEU N N 124.315 . 1
162 . 36 LEU H H 7.183 . 1
163 . 36 LEU CA C 57.060 . 1
164 . 36 LEU CB C 41.825 . 1
165 . 36 LEU C C 173.997 . 1
166 . 37 ASN N N 115.771 . 1
167 . 37 ASN H H 8.426 . 1
168 . 37 ASN CA C 54.693 . 1
169 . 37 ASN CB C 37.520 . 1
170 . 37 ASN C C 173.382 . 1
171 . 38 LYS N N 119.764 . 1
172 . 38 LYS H H 7.689 . 1
173 . 38 LYS CA C 54.164 . 1
174 . 38 LYS CB C 34.506 . 1
175 . 39 PRO CA C 62.500 . 1
176 . 39 PRO CB C 32.291 . 1
177 . 39 PRO C C 175.600 . 1
178 . 40 VAL N N 111.645 . 1
179 . 40 VAL H H 8.527 . 1
180 . 40 VAL CA C 56.588 . 1
181 . 40 VAL CB C 34.228 . 1
182 . 40 VAL C C 173.718 . 1
183 . 41 ILE N N 121.233 . 1
184 . 41 ILE H H 8.481 . 1
185 . 41 ILE CA C 59.481 . 1
186 . 41 ILE CB C 40.676 . 1
187 . 41 ILE C C 174.834 . 1
188 . 42 MET N N 123.295 . 1
189 . 42 MET H H 9.035 . 1
190 . 42 MET CA C 52.199 . 1
191 . 42 MET CB C 39.636 . 1
192 . 42 MET C C 174.555 . 1
193 . 43 GLY N N 105.432 . 1
194 . 43 GLY H H 9.048 . 1
195 . 43 GLY CA C 44.369 . 1
196 . 43 GLY C C 175.136 . 1
197 . 44 ARG N N 118.763 . 1
198 . 44 ARG H H 7.633 . 1
199 . 44 ARG CA C 61.019 . 1
200 . 44 ARG CB C 30.068 . 1
201 . 44 ARG C C 178.551 . 1
202 . 45 HIS N N 113.616 . 1
203 . 45 HIS H H 7.429 . 1
204 . 45 HIS CA C 57.916 . 1
205 . 45 HIS CB C 27.052 . 1
206 . 45 HIS C C 178.179 . 1
207 . 46 THR N N 121.167 . 1
208 . 46 THR H H 8.076 . 1
209 . 46 THR CA C 68.772 . 1
210 . 46 THR CB C 68.772 . 1
211 . 46 THR C C 176.413 . 1
212 . 47 TRP N N 123.330 . 1
213 . 47 TRP H H 8.331 . 1
214 . 47 TRP CA C 59.650 . 1
215 . 47 TRP CB C 30.276 . 1
216 . 47 TRP C C 177.134 . 1
217 . 48 GLU N N 117.821 . 1
218 . 48 GLU H H 8.199 . 1
219 . 48 GLU CA C 58.884 . 1
220 . 48 GLU CB C 28.577 . 1
221 . 48 GLU C C 178.597 . 1
222 . 49 SER N N 114.305 . 1
223 . 49 SER H H 7.873 . 1
224 . 49 SER CA C 60.489 . 1
225 . 49 SER CB C 63.572 . 1
226 . 49 SER C C 175.901 . 1
227 . 50 ILE N N 120.112 . 1
228 . 50 ILE H H 7.958 . 1
229 . 50 ILE CA C 64.625 . 1
230 . 50 ILE CB C 39.014 . 1
231 . 50 ILE C C 179.248 . 1
232 . 51 GLY N N 106.515 . 1
233 . 51 GLY H H 7.677 . 1
234 . 51 GLY CA C 46.139 . 1
235 . 51 GLY C C 172.534 . 1
236 . 52 ARG N N 116.964 . 1
237 . 52 ARG H H 6.868 . 1
238 . 52 ARG CA C 53.644 . 1
239 . 52 ARG CB C 29.825 . 1
240 . 53 PRO CA C 62.072 . 1
241 . 53 PRO CB C 31.805 . 1
242 . 53 PRO C C 177.041 . 1
243 . 54 LEU N N 126.301 . 1
244 . 54 LEU H H 9.885 . 1
245 . 54 LEU CA C 53.228 . 1
246 . 54 LEU CB C 40.851 . 1
247 . 55 PRO C C 179.743 . 1
248 . 56 GLY N N 112.525 . 1
249 . 56 GLY H H 7.682 . 1
250 . 56 GLY CA C 46.769 . 1
251 . 56 GLY C C 173.161 . 1
252 . 57 ARG N N 116.941 . 1
253 . 57 ARG H H 7.211 . 1
254 . 57 ARG CA C 53.950 . 1
255 . 57 ARG CB C 35.037 . 1
256 . 57 ARG C C 174.787 . 1
257 . 58 LYS N N 123.554 . 1
258 . 58 LYS H H 8.060 . 1
259 . 58 LYS CA C 56.652 . 1
260 . 58 LYS CB C 32.197 . 1
261 . 58 LYS C C 175.066 . 1
262 . 59 ASN N N 125.039 . 1
263 . 59 ASN H H 9.057 . 1
264 . 59 ASN CA C 52.949 . 1
265 . 59 ASN CB C 41.145 . 1
266 . 59 ASN C C 172.650 . 1
267 . 60 ILE N N 126.137 . 1
268 . 60 ILE H H 8.878 . 1
269 . 60 ILE CA C 59.750 . 1
270 . 60 ILE CB C 39.050 . 1
271 . 60 ILE C C 172.557 . 1
272 . 61 ILE N N 127.122 . 1
273 . 61 ILE H H 8.876 . 1
274 . 61 ILE CA C 57.669 . 1
275 . 61 ILE CB C 37.036 . 1
276 . 61 ILE C C 175.879 . 1
277 . 62 LEU N N 125.423 . 1
278 . 62 LEU H H 8.223 . 1
279 . 62 LEU CA C 53.771 . 1
280 . 62 LEU CB C 42.895 . 1
281 . 62 LEU C C 175.740 . 1
282 . 63 SER N N 114.761 . 1
283 . 63 SER H H 8.689 . 1
284 . 63 SER CA C 58.654 . 1
285 . 63 SER CB C 65.012 . 1
286 . 63 SER C C 174.346 . 1
287 . 64 SER N N 122.762 . 1
288 . 64 SER H H 10.221 . 1
289 . 64 SER CA C 60.477 . 1
290 . 64 SER CB C 64.414 . 1
291 . 64 SER C C 175.112 . 1
292 . 65 GLN N N 123.017 . 1
293 . 65 GLN H H 8.652 . 1
294 . 65 GLN CA C 53.124 . 1
295 . 65 GLN CB C 29.513 . 1
296 . 66 PRO CA C 62.826 . 1
297 . 66 PRO CB C 32.010 . 1
298 . 66 PRO C C 177.343 . 1
299 . 67 GLY N N 109.454 . 1
300 . 67 GLY H H 8.134 . 1
301 . 67 GLY CA C 42.550 . 1
302 . 67 GLY C C 174.508 . 1
303 . 68 THR N N 106.177 . 1
304 . 68 THR H H 5.752 . 1
305 . 68 THR CA C 60.312 . 1
306 . 68 THR CB C 69.166 . 1
307 . 68 THR C C 174.346 . 1
308 . 69 ASP N N 120.330 . 1
309 . 69 ASP H H 7.432 . 1
310 . 69 ASP CA C 55.282 . 1
311 . 69 ASP CB C 41.825 . 1
312 . 69 ASP C C 176.390 . 1
313 . 70 ASP N N 126.917 . 1
314 . 70 ASP H H 9.036 . 1
315 . 70 ASP CA C 55.265 . 1
316 . 70 ASP CB C 40.276 . 1
317 . 70 ASP C C 177.203 . 1
318 . 71 ARG N N 118.232 . 1
319 . 71 ARG H H 8.986 . 1
320 . 71 ARG CA C 57.307 . 1
321 . 71 ARG CB C 31.990 . 1
322 . 71 ARG C C 176.111 . 1
323 . 72 VAL N N 108.493 . 1
324 . 72 VAL H H 7.287 . 1
325 . 72 VAL CA C 58.159 . 1
326 . 72 VAL CB C 33.500 . 1
327 . 72 VAL C C 173.068 . 1
328 . 73 THR N N 117.244 . 1
329 . 73 THR H H 8.088 . 1
330 . 73 THR CA C 62.714 . 1
331 . 73 THR CB C 70.249 . 1
332 . 73 THR C C 172.022 . 1
333 . 74 TRP N N 128.837 . 1
334 . 74 TRP H H 8.906 . 1
335 . 74 TRP CA C 56.035 . 1
336 . 74 TRP CB C 28.864 . 1
337 . 74 TRP C C 176.832 . 1
338 . 75 VAL N N 116.622 . 1
339 . 75 VAL H H 9.203 . 1
340 . 75 VAL CA C 58.945 . 1
341 . 75 VAL CB C 35.914 . 1
342 . 75 VAL C C 174.857 . 1
343 . 76 LYS N N 115.584 . 1
344 . 76 LYS H H 8.277 . 1
345 . 76 LYS CA C 55.553 . 1
346 . 76 LYS CB C 34.096 . 1
347 . 76 LYS C C 175.623 . 1
348 . 77 SER N N 108.749 . 1
349 . 77 SER H H 7.223 . 1
350 . 77 SER CA C 57.195 . 1
351 . 77 SER CB C 66.708 . 1
352 . 77 SER C C 174.067 . 1
353 . 78 VAL N N 122.695 . 1
354 . 78 VAL H H 8.968 . 1
355 . 78 VAL CA C 67.094 . 1
356 . 78 VAL CB C 31.443 . 1
357 . 78 VAL C C 177.366 . 1
358 . 79 ASP N N 118.071 . 1
359 . 79 ASP H H 8.615 . 1
360 . 79 ASP CA C 57.585 . 1
361 . 79 ASP CB C 39.714 . 1
362 . 79 ASP C C 180.084 . 1
363 . 80 GLU N N 120.635 . 1
364 . 80 GLU H H 8.000 . 1
365 . 80 GLU CA C 59.202 . 1
366 . 80 GLU CB C 30.731 . 1
367 . 80 GLU C C 179.271 . 1
368 . 81 ALA N N 122.901 . 1
369 . 81 ALA H H 8.264 . 1
370 . 81 ALA CA C 55.487 . 1
371 . 81 ALA CB C 17.961 . 1
372 . 81 ALA C C 177.970 . 1
373 . 82 ILE N N 116.075 . 1
374 . 82 ILE H H 8.027 . 1
375 . 82 ILE CA C 65.674 . 1
376 . 82 ILE CB C 38.706 . 1
377 . 82 ILE C C 180.456 . 1
378 . 83 ALA N N 123.706 . 1
379 . 83 ALA H H 8.175 . 1
380 . 83 ALA CA C 54.979 . 1
381 . 83 ALA CB C 17.970 . 1
382 . 83 ALA C C 180.525 . 1
383 . 84 ALA N N 119.346 . 1
384 . 84 ALA H H 8.075 . 1
385 . 84 ALA CA C 53.776 . 1
386 . 84 ALA CB C 18.072 . 1
387 . 84 ALA C C 177.157 . 1
388 . 85 CYS N N 114.394 . 1
389 . 85 CYS H H 7.402 . 1
390 . 85 CYS CA C 62.015 . 1
391 . 85 CYS CB C 27.847 . 1
392 . 85 CYS C C 175.391 . 1
393 . 86 GLY N N 103.101 . 1
394 . 86 GLY H H 7.287 . 1
395 . 86 GLY CA C 44.919 . 1
396 . 86 GLY C C 173.277 . 1
397 . 87 ASP N N 122.162 . 1
398 . 87 ASP H H 8.665 . 1
399 . 87 ASP CA C 53.206 . 1
400 . 87 ASP CB C 39.505 . 1
401 . 87 ASP C C 175.414 . 1
402 . 88 VAL N N 114.973 . 1
403 . 88 VAL H H 7.316 . 1
404 . 88 VAL CA C 57.906 . 1
405 . 88 VAL CB C 32.322 . 1
406 . 89 PRO CA C 64.519 . 1
407 . 89 PRO CB C 32.203 . 1
408 . 89 PRO C C 177.854 . 1
409 . 90 GLU N N 116.615 . 1
410 . 90 GLU H H 7.729 . 1
411 . 90 GLU CA C 55.820 . 1
412 . 90 GLU CB C 32.845 . 1
413 . 90 GLU C C 173.370 . 1
414 . 91 ILE N N 130.104 . 1
415 . 91 ILE H H 8.847 . 1
416 . 91 ILE CA C 61.274 . 1
417 . 91 ILE CB C 41.393 . 1
418 . 91 ILE C C 173.835 . 1
419 . 92 MET N N 121.489 . 1
420 . 92 MET H H 7.974 . 1
421 . 92 MET CA C 51.931 . 1
422 . 92 MET CB C 30.106 . 1
423 . 92 MET C C 174.090 . 1
424 . 93 VAL N N 125.298 . 1
425 . 93 VAL H H 9.324 . 1
426 . 93 VAL CA C 62.091 . 1
427 . 93 VAL CB C 31.443 . 1
428 . 93 VAL C C 177.226 . 1
429 . 94 ILE N N 118.482 . 1
430 . 94 ILE H H 8.554 . 1
431 . 94 ILE CA C 60.996 . 1
432 . 94 ILE CB C 37.667 . 1
433 . 94 ILE C C 173.579 . 1
434 . 95 GLY N N 102.691 . 1
435 . 95 GLY H H 6.056 . 1
436 . 95 GLY CA C 41.349 . 1
437 . 95 GLY C C 174.578 . 1
438 . 96 GLY N N 112.501 . 1
439 . 96 GLY H H 7.700 . 1
440 . 96 GLY CA C 46.522 . 1
441 . 96 GLY C C 173.927 . 1
442 . 97 GLY N N 108.472 . 1
443 . 97 GLY H H 7.425 . 1
444 . 97 GLY CA C 49.396 . 1
445 . 97 GLY C C 175.414 . 1
446 . 98 ARG N N 123.629 . 1
447 . 98 ARG H H 9.877 . 1
448 . 98 ARG CA C 58.360 . 1
449 . 98 ARG CB C 29.664 . 1
450 . 98 ARG C C 180.944 . 1
451 . 99 VAL N N 122.974 . 1
452 . 99 VAL H H 7.497 . 1
453 . 99 VAL CA C 68.544 . 1
454 . 99 VAL CB C 31.531 . 1
455 . 99 VAL C C 178.899 . 1
456 . 100 TYR N N 120.179 . 1
457 . 100 TYR H H 9.621 . 1
458 . 100 TYR CA C 60.157 . 1
459 . 100 TYR CB C 37.954 . 1
460 . 100 TYR C C 178.365 . 1
461 . 101 GLU N N 115.906 . 1
462 . 101 GLU H H 8.182 . 1
463 . 101 GLU CA C 59.932 . 1
464 . 101 GLU CB C 29.680 . 1
465 . 101 GLU C C 178.620 . 1
466 . 102 GLN N N 114.072 . 1
467 . 102 GLN H H 7.301 . 1
468 . 102 GLN CA C 57.887 . 1
469 . 102 GLN CB C 32.714 . 1
470 . 102 GLN C C 177.459 . 1
471 . 103 PHE N N 113.616 . 1
472 . 103 PHE H H 8.190 . 1
473 . 103 PHE CA C 60.481 . 1
474 . 103 PHE CB C 41.531 . 1
475 . 103 PHE C C 177.180 . 1
476 . 104 LEU N N 123.339 . 1
477 . 104 LEU H H 8.538 . 1
478 . 104 LEU CA C 60.925 . 1
479 . 104 LEU CB C 38.250 . 1
480 . 105 PRO CA C 65.342 . 1
481 . 105 PRO CB C 31.212 . 1
482 . 105 PRO C C 177.482 . 1
483 . 106 LYS N N 112.927 . 1
484 . 106 LYS H H 7.439 . 1
485 . 106 LYS CA C 55.572 . 1
486 . 106 LYS CB C 34.595 . 1
487 . 106 LYS C C 176.065 . 1
488 . 107 ALA N N 122.651 . 1
489 . 107 ALA H H 8.008 . 1
490 . 107 ALA CA C 52.493 . 1
491 . 107 ALA CB C 20.935 . 1
492 . 108 GLN N N 118.294 . 1
493 . 108 GLN H H 9.323 . 1
494 . 108 GLN CA C 55.580 . 1
495 . 108 GLN CB C 31.524 . 1
496 . 108 GLN C C 175.484 . 1
497 . 109 LYS N N 120.843 . 1
498 . 109 LYS H H 7.822 . 1
499 . 109 LYS CA C 56.015 . 1
500 . 109 LYS CB C 36.898 . 1
501 . 109 LYS C C 174.137 . 1
502 . 110 LEU N N 121.616 . 1
503 . 110 LEU H H 9.015 . 1
504 . 110 LEU CA C 52.973 . 1
505 . 110 LEU CB C 44.462 . 1
506 . 110 LEU C C 174.764 . 1
507 . 111 TYR N N 122.037 . 1
508 . 111 TYR H H 9.408 . 1
509 . 111 TYR CA C 56.299 . 1
510 . 111 TYR CB C 38.435 . 1
511 . 111 TYR C C 174.206 . 1
512 . 112 LEU N N 122.458 . 1
513 . 112 LEU H H 9.734 . 1
514 . 112 LEU CA C 52.718 . 1
515 . 112 LEU CB C 45.119 . 1
516 . 112 LEU C C 175.670 . 1
517 . 113 THR N N 117.736 . 1
518 . 113 THR H H 8.083 . 1
519 . 113 THR CA C 60.162 . 1
520 . 113 THR CB C 68.818 . 1
521 . 113 THR C C 173.416 . 1
522 . 114 HIS N N 126.104 . 1
523 . 114 HIS H H 9.292 . 1
524 . 114 HIS CA C 55.089 . 1
525 . 114 HIS CB C 30.900 . 1
526 . 114 HIS C C 175.833 . 1
527 . 115 ILE N N 127.126 . 1
528 . 115 ILE H H 9.135 . 1
529 . 115 ILE CA C 60.741 . 1
530 . 115 ILE CB C 39.220 . 1
531 . 115 ILE C C 176.832 . 1
532 . 116 ASP N N 129.899 . 1
533 . 116 ASP H H 8.415 . 1
534 . 116 ASP CA C 53.509 . 1
535 . 116 ASP CB C 38.500 . 1
536 . 116 ASP C C 173.927 . 1
537 . 117 ALA N N 124.188 . 1
538 . 117 ALA H H 7.801 . 1
539 . 117 ALA CA C 51.049 . 1
540 . 117 ALA CB C 20.298 . 1
541 . 117 ALA C C 174.578 . 1
542 . 118 GLU N N 123.420 . 1
543 . 118 GLU H H 8.629 . 1
544 . 118 GLU CA C 55.278 . 1
545 . 118 GLU CB C 29.178 . 1
546 . 118 GLU C C 175.321 . 1
547 . 119 VAL N N 119.754 . 1
548 . 119 VAL H H 8.278 . 1
549 . 119 VAL CA C 58.730 . 1
550 . 119 VAL CB C 35.321 . 1
551 . 119 VAL C C 174.787 . 1
552 . 120 GLU N N 124.162 . 1
553 . 120 GLU H H 8.474 . 1
554 . 120 GLU CA C 56.408 . 1
555 . 120 GLU CB C 30.245 . 1
556 . 120 GLU C C 175.995 . 1
557 . 121 GLY N N 107.202 . 1
558 . 121 GLY H H 8.594 . 1
559 . 121 GLY CA C 45.973 . 1
560 . 121 GLY C C 172.882 . 1
561 . 122 ASP N N 116.551 . 1
562 . 122 ASP H H 8.885 . 1
563 . 122 ASP CA C 52.187 . 1
564 . 122 ASP CB C 42.339 . 1
565 . 122 ASP C C 176.320 . 1
566 . 123 THR N N 115.610 . 1
567 . 123 THR H H 7.541 . 1
568 . 123 THR CA C 62.798 . 1
569 . 123 THR CB C 72.991 . 1
570 . 123 THR C C 172.859 . 1
571 . 124 HIS N N 126.951 . 1
572 . 124 HIS H H 9.615 . 1
573 . 124 HIS CA C 56.550 . 1
574 . 124 HIS CB C 33.613 . 1
575 . 124 HIS C C 174.044 . 1
576 . 125 PHE N N 124.958 . 1
577 . 125 PHE H H 9.357 . 1
578 . 125 PHE CA C 57.077 . 1
579 . 125 PHE CB C 41.787 . 1
580 . 126 PRO CA C 62.511 . 1
581 . 126 PRO CB C 31.988 . 1
582 . 126 PRO C C 173.951 . 1
583 . 127 ASP N N 117.656 . 1
584 . 127 ASP H H 8.230 . 1
585 . 127 ASP CA C 54.293 . 1
586 . 127 ASP CB C 40.603 . 1
587 . 127 ASP C C 173.463 . 1
588 . 128 TYR N N 119.752 . 1
589 . 128 TYR H H 7.564 . 1
590 . 128 TYR CA C 55.365 . 1
591 . 128 TYR CB C 39.202 . 1
592 . 128 TYR C C 173.602 . 1
593 . 129 GLU N N 123.652 . 1
594 . 129 GLU H H 8.913 . 1
595 . 129 GLU CA C 53.124 . 1
596 . 129 GLU CB C 29.721 . 1
597 . 130 PRO CA C 65.984 . 1
598 . 130 PRO CB C 32.205 . 1
599 . 130 PRO C C 178.504 . 1
600 . 131 ASP N N 114.886 . 1
601 . 131 ASP H H 9.228 . 1
602 . 131 ASP CA C 56.561 . 1
603 . 131 ASP CB C 39.958 . 1
604 . 131 ASP C C 176.111 . 1
605 . 132 ASP N N 117.958 . 1
606 . 132 ASP H H 8.256 . 1
607 . 132 ASP CA C 55.010 . 1
608 . 132 ASP CB C 41.316 . 1
609 . 132 ASP C C 175.159 . 1
610 . 133 TRP N N 119.886 . 1
611 . 133 TRP H H 7.841 . 1
612 . 133 TRP CA C 56.052 . 1
613 . 133 TRP CB C 34.125 . 1
614 . 133 TRP C C 173.951 . 1
615 . 134 GLU N N 122.976 . 1
616 . 134 GLU H H 9.636 . 1
617 . 134 GLU CA C 54.295 . 1
618 . 134 GLU CB C 32.498 . 1
619 . 134 GLU C C 175.809 . 1
620 . 135 SER N N 121.612 . 1
621 . 135 SER H H 9.164 . 1
622 . 135 SER CA C 58.652 . 1
623 . 135 SER CB C 62.312 . 1
624 . 135 SER C C 176.274 . 1
625 . 136 VAL N N 122.018 . 1
626 . 136 VAL H H 9.083 . 1
627 . 136 VAL CA C 60.947 . 1
628 . 136 VAL CB C 32.472 . 1
629 . 136 VAL C C 175.902 . 1
630 . 137 PHE N N 123.857 . 1
631 . 137 PHE H H 7.942 . 1
632 . 137 PHE CA C 58.406 . 1
633 . 137 PHE CB C 42.875 . 1
634 . 137 PHE C C 173.706 . 1
635 . 138 SER N N 119.592 . 1
636 . 138 SER H H 7.680 . 1
637 . 138 SER CA C 57.104 . 1
638 . 138 SER CB C 64.241 . 1
639 . 138 SER C C 173.254 . 1
640 . 139 GLU N N 126.127 . 1
641 . 139 GLU H H 8.778 . 1
642 . 139 GLU CA C 56.060 . 1
643 . 139 GLU CB C 34.866 . 1
644 . 139 GLU C C 173.927 . 1
645 . 140 PHE N N 128.944 . 1
646 . 140 PHE H H 8.776 . 1
647 . 140 PHE CA C 58.690 . 1
648 . 140 PHE CB C 40.361 . 1
649 . 140 PHE C C 174.555 . 1
650 . 141 HIS N N 123.125 . 1
651 . 141 HIS H H 8.203 . 1
652 . 141 HIS CA C 54.280 . 1
653 . 141 HIS CB C 31.790 . 1
654 . 141 HIS C C 172.301 . 1
655 . 142 ASP N N 120.304 . 1
656 . 142 ASP H H 8.168 . 1
657 . 142 ASP CA C 53.300 . 1
658 . 142 ASP CB C 42.445 . 1
659 . 142 ASP C C 175.786 . 1
660 . 143 ALA N N 122.135 . 1
661 . 143 ALA H H 8.221 . 1
662 . 143 ALA CA C 53.023 . 1
663 . 143 ALA CB C 19.125 . 1
664 . 143 ALA C C 177.203 . 1
665 . 144 ASP N N 121.209 . 1
666 . 144 ASP H H 9.149 . 1
667 . 144 ASP CA C 53.013 . 1
668 . 144 ASP CB C 41.862 . 1
669 . 144 ASP C C 177.250 . 1
670 . 145 ALA N N 117.949 . 1
671 . 145 ALA H H 8.285 . 1
672 . 145 ALA CA C 55.011 . 1
673 . 145 ALA CB C 18.189 . 1
674 . 145 ALA C C 178.829 . 1
675 . 146 GLN N N 113.097 . 1
676 . 146 GLN H H 7.969 . 1
677 . 146 GLN CA C 56.569 . 1
678 . 146 GLN CB C 30.929 . 1
679 . 146 GLN C C 175.112 . 1
680 . 147 ASN N N 119.624 . 1
681 . 147 ASN H H 8.257 . 1
682 . 147 ASN CA C 52.376 . 1
683 . 147 ASN CB C 41.089 . 1
684 . 147 ASN C C 173.625 . 1
685 . 148 SER N N 117.007 . 1
686 . 148 SER H H 9.016 . 1
687 . 148 SER CA C 60.746 . 1
688 . 148 SER CB C 63.312 . 1
689 . 148 SER C C 172.534 . 1
690 . 149 HIS N N 117.355 . 1
691 . 149 HIS H H 6.926 . 1
692 . 149 HIS CA C 53.735 . 1
693 . 149 HIS CB C 33.815 . 1
694 . 149 HIS C C 173.858 . 1
695 . 150 SER N N 113.840 . 1
696 . 150 SER H H 8.728 . 1
697 . 150 SER CA C 58.416 . 1
698 . 150 SER CB C 64.348 . 1
699 . 150 SER C C 173.161 . 1
700 . 151 TYR N N 114.698 . 1
701 . 151 TYR H H 7.650 . 1
702 . 151 TYR CA C 54.796 . 1
703 . 151 TYR CB C 39.211 . 1
704 . 151 TYR C C 172.232 . 1
705 . 152 CYS N N 118.531 . 1
706 . 152 CYS H H 8.318 . 1
707 . 152 CYS CA C 55.246 . 1
708 . 152 CYS CB C 30.113 . 1
709 . 152 CYS C C 174.113 . 1
710 . 153 PHE N N 128.452 . 1
711 . 153 PHE H H 8.390 . 1
712 . 153 PHE CA C 55.579 . 1
713 . 153 PHE CB C 40.112 . 1
714 . 153 PHE C C 175.066 . 1
715 . 154 GLU N N 124.254 . 1
716 . 154 GLU H H 9.866 . 1
717 . 154 GLU CA C 54.515 . 1
718 . 154 GLU CB C 35.075 . 1
719 . 154 GLU C C 174.601 . 1
720 . 155 ILE N N 123.751 . 1
721 . 155 ILE H H 8.700 . 1
722 . 155 ILE CA C 60.162 . 1
723 . 155 ILE CB C 40.260 . 1
724 . 155 ILE C C 175.159 . 1
725 . 156 LEU N N 125.884 . 1
726 . 156 LEU H H 9.325 . 1
727 . 156 LEU CA C 53.291 . 1
728 . 156 LEU CB C 45.662 . 1
729 . 156 LEU C C 175.902 . 1
730 . 157 GLU N N 119.589 . 1
731 . 157 GLU H H 9.380 . 1
732 . 157 GLU CA C 54.483 . 1
733 . 157 GLU CB C 33.570 . 1
734 . 157 GLU C C 176.251 . 1
735 . 158 ARG N N 127.120 . 1
736 . 158 ARG H H 8.323 . 1
737 . 158 ARG CA C 57.378 . 1
738 . 158 ARG CB C 30.711 . 1
739 . 158 ARG C C 176.460 . 1
740 . 159 ARG N N 131.571 . 1
741 . 159 ARG H H 8.040 . 1
742 . 159 ARG CA C 58.741 . 1
743 . 159 ARG CB C 30.970 . 1
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