data_4714 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structural analysis of WW domains and design of a WW prototype ; _BMRB_accession_number 4714 _BMRB_flat_file_name bmr4714.str _Entry_type original _Submission_date 2000-04-11 _Accession_date 2000-04-17 _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 Macias Maria J . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 221 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-06-15 original author . stop_ _Original_release_date 2000-06-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural analysis of WW domains and design of a WW prototype' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 20264516 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Macias Maria J. . 2 Gervais V. . . 3 Civera C. . . 4 Oschkinat H. . . stop_ _Journal_abbreviation 'Nat. Struct. Biol.' _Journal_name_full 'Nature Structural Biology' _Journal_volume 7 _Journal_issue 5 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 375 _Page_last 379 _Year 2000 _Details . loop_ _Keyword 'WW domain' 'protein design' 'signal transduction' stop_ save_ ################################## # Molecular system description # ################################## save_system_FMPWW28 _Saveframe_category molecular_system _Mol_system_name 'Formin binding WW domain' _Abbreviation_common FMPWW28 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Formin binding 28 WW domain' $FMPWW28 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_FMPWW28 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Formin binding WW domain' _Abbreviation_common FMPWW28 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 40 _Mol_residue_sequence ; GSMGATAVSEWTEYKTADGK TYYYNNRTLESTWEKPQELK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 SER 3 0 MET 4 1 GLY 5 2 ALA 6 3 THR 7 4 ALA 8 5 VAL 9 6 SER 10 7 GLU 11 8 TRP 12 9 THR 13 10 GLU 14 11 TYR 15 12 LYS 16 13 THR 17 14 ALA 18 15 ASP 19 16 GLY 20 17 LYS 21 18 THR 22 19 TYR 23 20 TYR 24 21 TYR 25 22 ASN 26 23 ASN 27 24 ARG 28 25 THR 29 26 LEU 30 27 GLU 31 28 SER 32 29 THR 33 30 TRP 34 31 GLU 35 32 LYS 36 33 PRO 37 34 GLN 38 35 GLU 39 36 LEU 40 37 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-03 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 11007 FBP28WW2 92.50 37 100.00 100.00 1.28e-16 BMRB 11008 FBP28WW2 92.50 37 100.00 100.00 1.28e-16 BMRB 15453 FBP28WW2 92.50 37 100.00 100.00 1.28e-16 BMRB 25309 entity 92.50 37 97.30 97.30 1.49e-15 BMRB 25310 entity 92.50 37 97.30 97.30 1.06e-15 BMRB 25311 entity 92.50 37 97.30 100.00 7.26e-16 BMRB 25678 entity 92.50 37 97.30 97.30 2.13e-15 BMRB 25679 entity 92.50 37 97.30 97.30 2.15e-15 BMRB 25680 entity 92.50 37 97.30 97.30 1.93e-15 BMRB 25681 entity 92.50 37 97.30 97.30 1.66e-15 BMRB 25682 entity 92.50 37 97.30 97.30 7.99e-16 BMRB 25683 entity 92.50 37 97.30 97.30 1.41e-15 PDB 1E0L "Fbp28ww Domain From Mus Musculus" 92.50 37 100.00 100.00 1.28e-16 PDB 2JUP "Fbp28ww2 Domain In Complex With The Pplipppp Peptide" 92.50 37 100.00 100.00 1.28e-16 PDB 2MW9 "Nmr Structure Of Fbp28 Ww2 Y438r Mutant" 92.50 37 97.30 97.30 1.49e-15 PDB 2MWA "Nmr Structure Of Fbp28 Ww2 Mutant Y446l" 92.50 37 97.30 97.30 1.06e-15 PDB 2MWB "Fbp28 Ww2 Mutant W457f" 92.50 37 97.30 100.00 7.26e-16 PDB 2N4R "Nmr Structure Of Fbp28 Ww Domain L453d Mutant" 92.50 37 97.30 97.30 2.13e-15 PDB 2N4S "Nmr Structure Of Fbp28 Ww Domain L453e Mutant" 92.50 37 97.30 97.30 2.15e-15 PDB 2N4T "Nmr Structure Of Fbp28 Ww Domain L453w Mutant" 92.50 37 97.30 97.30 1.93e-15 PDB 2N4U "Nmr Structure Of Fbp28 Ww Domain E454y Mutant" 92.50 37 97.30 97.30 1.66e-15 PDB 2N4V "Nmr Structure Of Fbp28 Ww Domain T456d Mutant" 92.50 37 97.30 97.30 7.99e-16 PDB 2N4W "Nmr Structure Of Fbp28 Ww Domain T456y Mutant" 92.50 37 97.30 97.30 1.41e-15 PDB 2NNT "General Structural Motifs Of Amyloid Protofilaments" 100.00 40 97.50 100.00 8.22e-19 PDB 2RLY "Fbp28ww2 Domain In Complex With Ptppplpp Peptide" 92.50 37 100.00 100.00 1.28e-16 PDB 2RM0 "Fbp28ww2 Domain In Complex With A Ppplipppp Peptide" 92.50 37 100.00 100.00 1.28e-16 GB AAC52477 "FBP 28, partial [Mus musculus]" 65.00 26 100.00 100.00 9.34e-09 GB EGW05321 "Transcription elongation regulator 1 [Cricetulus griseus]" 92.50 414 100.00 100.00 2.14e-16 GB EHB12574 "Transcription elongation regulator 1-like protein [Heterocephalus glaber]" 85.00 967 100.00 100.00 5.98e-14 GB ELW66441 "Transcription elongation regulator 1, partial [Tupaia chinensis]" 85.00 1001 100.00 100.00 5.91e-14 GB EMP40899 "Transcription elongation regulator 1 [Chelonia mydas]" 85.00 945 97.06 100.00 1.55e-13 REF XP_004697122 "PREDICTED: transcription elongation regulator 1 [Echinops telfairi]" 85.00 1004 100.00 100.00 6.34e-14 REF XP_006977759 "PREDICTED: transcription elongation regulator 1 [Peromyscus maniculatus bairdii]" 92.50 1057 100.00 100.00 7.97e-16 REF XP_007653449 "PREDICTED: uncharacterized protein LOC100076344 [Ornithorhynchus anatinus]" 85.00 774 100.00 100.00 2.20e-14 REF XP_008253407 "PREDICTED: transcription elongation regulator 1 isoform X9 [Oryctolagus cuniculus]" 85.00 770 100.00 100.00 5.91e-14 REF XP_008926141 "PREDICTED: transcription elongation regulator 1 [Manacus vitellinus]" 85.00 814 100.00 100.00 5.46e-14 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $FMPWW28 'house mouse' 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $FMPWW28 'recombinant technology' E.coli . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $FMPWW28 . mM 1 3 . stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version 2.6 _Details . save_ save_xeasy _Saveframe_category software _Name xeasy _Version 1.3.13 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label . save_ save_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond_set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 n/a temperature 285 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis TSP H 1 'methyl protons' ppm 0.00 internal direct spherical internal parallel_to_Bo stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Formin binding 28 WW domain' _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 . 5 ALA H H 8.080 0.02 1 2 . 5 ALA HA H 4.100 0.02 1 3 . 5 ALA HB H 1.150 0.02 1 4 . 6 THR H H 8.170 0.02 1 5 . 6 THR HA H 4.050 0.02 1 6 . 6 THR HB H 3.940 0.02 1 7 . 6 THR HG2 H 0.970 0.02 1 8 . 7 ALA H H 8.170 0.02 1 9 . 7 ALA HA H 4.100 0.02 1 10 . 7 ALA HB H 1.150 0.02 1 11 . 8 VAL H H 8.050 0.02 1 12 . 8 VAL HA H 3.840 0.02 1 13 . 8 VAL HB H 1.820 0.02 1 14 . 8 VAL HG1 H 0.700 0.02 1 15 . 8 VAL HG2 H 0.700 0.02 1 16 . 9 SER H H 8.220 0.02 1 17 . 9 SER HA H 4.250 0.02 1 18 . 9 SER HB2 H 3.770 0.02 2 19 . 9 SER HB3 H 3.640 0.02 2 20 . 10 GLU H H 8.630 0.02 1 21 . 10 GLU HA H 3.940 0.02 1 22 . 10 GLU HB2 H 1.640 0.02 2 23 . 10 GLU HB3 H 1.560 0.02 2 24 . 10 GLU HG2 H 1.740 0.02 1 25 . 10 GLU HG3 H 1.740 0.02 1 26 . 11 TRP H H 8.040 0.02 1 27 . 11 TRP HA H 5.100 0.02 1 28 . 11 TRP HB2 H 2.860 0.02 2 29 . 11 TRP HB3 H 2.670 0.02 2 30 . 11 TRP HD1 H 6.950 0.02 1 31 . 11 TRP HE3 H 7.090 0.02 1 32 . 11 TRP HZ3 H 6.720 0.02 1 33 . 11 TRP HZ2 H 7.260 0.02 1 34 . 11 TRP HH2 H 6.850 0.02 1 35 . 12 THR H H 9.260 0.02 1 36 . 12 THR HA H 4.290 0.02 1 37 . 12 THR HB H 3.640 0.02 1 38 . 12 THR HG2 H 0.640 0.02 1 39 . 13 GLU H H 8.350 0.02 1 40 . 13 GLU HA H 4.150 0.02 1 41 . 13 GLU HB2 H 1.570 0.02 1 42 . 13 GLU HB3 H 1.570 0.02 1 43 . 13 GLU HG2 H 1.570 0.02 1 44 . 13 GLU HG3 H 1.570 0.02 1 45 . 14 TYR H H 8.410 0.02 1 46 . 14 TYR HA H 4.330 0.02 1 47 . 14 TYR HB2 H 2.260 0.02 1 48 . 14 TYR HB3 H 0.940 0.02 2 49 . 14 TYR HD1 H 6.580 0.02 1 50 . 14 TYR HE1 H 6.330 0.02 1 51 . 14 TYR HE2 H 6.330 0.02 1 52 . 14 TYR HD2 H 6.580 0.02 1 53 . 15 LYS H H 8.000 0.02 1 54 . 15 LYS HA H 5.230 0.02 1 55 . 15 LYS HB2 H 1.450 0.02 2 56 . 15 LYS HB3 H 1.380 0.02 2 57 . 15 LYS HG2 H 1.290 0.02 1 58 . 15 LYS HG3 H 1.290 0.02 1 59 . 15 LYS HD2 H 1.110 0.02 1 60 . 15 LYS HD3 H 1.110 0.02 1 61 . 15 LYS HE2 H 2.630 0.02 1 62 . 15 LYS HE3 H 2.630 0.02 1 63 . 16 THR H H 9.090 0.02 1 64 . 16 THR HA H 4.580 0.02 1 65 . 16 THR HB H 4.420 0.02 1 66 . 16 THR HG2 H 1.300 0.02 1 67 . 17 ALA H H 9.040 0.02 1 68 . 17 ALA HA H 3.920 0.02 1 69 . 17 ALA HB H 1.250 0.02 1 70 . 18 ASP H H 7.840 0.02 1 71 . 18 ASP HA H 3.920 0.02 1 72 . 18 ASP HB2 H 2.600 0.02 2 73 . 18 ASP HB3 H 2.420 0.02 2 74 . 19 GLY H H 7.790 0.02 1 75 . 19 GLY HA2 H 3.950 0.02 1 76 . 19 GLY HA3 H 3.390 0.02 1 77 . 20 LYS H H 7.710 0.02 1 78 . 20 LYS HA H 4.320 0.02 1 79 . 20 LYS HB2 H 1.750 0.02 2 80 . 20 LYS HB3 H 1.280 0.02 2 81 . 20 LYS HG2 H 1.100 0.02 1 82 . 20 LYS HG3 H 1.100 0.02 1 83 . 20 LYS HD2 H 1.100 0.02 1 84 . 20 LYS HD3 H 1.100 0.02 1 85 . 20 LYS HE2 H 2.490 0.02 1 86 . 20 LYS HE3 H 2.490 0.02 1 87 . 21 THR H H 8.540 0.02 1 88 . 21 THR HA H 4.740 0.02 1 89 . 21 THR HB H 3.670 0.02 1 90 . 21 THR HG2 H 0.640 0.02 1 91 . 22 TYR H H 8.530 0.02 1 92 . 22 TYR HA H 4.450 0.02 1 93 . 22 TYR HB2 H 2.060 0.02 2 94 . 22 TYR HB3 H 2.000 0.02 2 95 . 22 TYR HD1 H 6.490 0.02 1 96 . 22 TYR HE1 H 6.110 0.02 1 97 . 22 TYR HE2 H 6.110 0.02 1 98 . 22 TYR HD2 H 6.490 0.02 1 99 . 23 TYR H H 8.670 0.02 1 100 . 23 TYR HA H 4.930 0.02 1 101 . 23 TYR HB2 H 2.430 0.02 1 102 . 23 TYR HB3 H 2.430 0.02 1 103 . 23 TYR HD1 H 6.440 0.02 1 104 . 23 TYR HE1 H 6.390 0.02 1 105 . 23 TYR HE2 H 6.390 0.02 1 106 . 23 TYR HD2 H 6.440 0.02 1 107 . 24 TYR H H 9.190 0.02 1 108 . 24 TYR HA H 5.390 0.02 1 109 . 24 TYR HB2 H 2.690 0.02 1 110 . 24 TYR HB3 H 2.690 0.02 1 111 . 24 TYR HD1 H 6.770 0.02 1 112 . 24 TYR HE1 H 6.380 0.02 1 113 . 24 TYR HE2 H 6.380 0.02 1 114 . 24 TYR HD2 H 6.770 0.02 1 115 . 25 ASN H H 8.060 0.02 1 116 . 25 ASN HA H 4.070 0.02 1 117 . 25 ASN HB2 H 2.150 0.02 1 118 . 25 ASN HD21 H 7.260 0.02 2 119 . 25 ASN HD22 H 7.000 0.02 2 120 . 26 ASN H H 8.300 0.02 1 121 . 26 ASN HA H 3.910 0.02 1 122 . 26 ASN HB2 H 2.510 0.02 1 123 . 26 ASN HB3 H 2.510 0.02 1 124 . 26 ASN HD21 H 7.140 0.02 2 125 . 26 ASN HD22 H 6.980 0.02 2 126 . 27 ARG H H 8.350 0.02 1 127 . 27 ARG HA H 4.050 0.02 1 128 . 27 ARG HB2 H 1.680 0.02 2 129 . 27 ARG HB3 H 1.360 0.02 2 130 . 27 ARG HG2 H 1.220 0.02 2 131 . 27 ARG HG3 H 1.010 0.02 2 132 . 27 ARG HD2 H 3.730 0.02 2 133 . 27 ARG HD3 H 3.010 0.02 2 134 . 27 ARG HE H 7.800 0.02 1 135 . 28 THR H H 7.760 0.02 1 136 . 28 THR HA H 3.940 0.02 1 137 . 28 THR HB H 3.740 0.02 1 138 . 28 THR HG2 H 0.690 0.02 1 139 . 29 LEU H H 7.650 0.02 1 140 . 29 LEU HA H 3.530 0.02 1 141 . 29 LEU HB2 H 1.460 0.02 2 142 . 29 LEU HB3 H 1.040 0.02 2 143 . 29 LEU HG H 1.850 0.02 1 144 . 29 LEU HD1 H 0.600 0.02 2 145 . 29 LEU HD2 H 0.510 0.02 2 146 . 30 GLU H H 6.940 0.02 1 147 . 30 GLU HA H 4.060 0.02 1 148 . 30 GLU HB2 H 1.660 0.02 2 149 . 30 GLU HB3 H 1.510 0.02 2 150 . 30 GLU HG2 H 2.000 0.02 2 151 . 30 GLU HG3 H 1.860 0.02 2 152 . 31 SER H H 8.260 0.02 1 153 . 31 SER HA H 5.790 0.02 1 154 . 31 SER HB2 H 3.440 0.02 1 155 . 31 SER HB3 H 3.440 0.02 1 156 . 32 THR H H 9.170 0.02 1 157 . 32 THR HA H 4.580 0.02 1 158 . 32 THR HB H 4.030 0.02 1 159 . 32 THR HG2 H 0.940 0.02 1 160 . 33 TRP H H 8.280 0.02 1 161 . 33 TRP HA H 4.760 0.02 1 162 . 33 TRP HB2 H 3.390 0.02 1 163 . 33 TRP HB3 H 3.390 0.02 1 164 . 33 TRP HD1 H 7.140 0.02 1 165 . 33 TRP HE3 H 7.820 0.02 1 166 . 33 TRP HZ3 H 6.660 0.02 1 167 . 33 TRP HZ2 H 7.050 0.02 1 168 . 33 TRP HH2 H 6.800 0.02 1 169 . 34 GLU H H 7.960 0.02 1 170 . 34 GLU HA H 4.140 0.02 1 171 . 34 GLU HB2 H 1.540 0.02 2 172 . 34 GLU HB3 H 1.460 0.02 2 173 . 34 GLU HG2 H 1.830 0.02 1 174 . 34 GLU HG3 H 1.830 0.02 1 175 . 35 LYS H H 8.210 0.02 1 176 . 35 LYS HA H 2.440 0.02 1 177 . 35 LYS HB2 H 1.130 0.02 1 178 . 35 LYS HB3 H 1.130 0.02 1 179 . 35 LYS HG2 H 0.790 0.02 1 180 . 35 LYS HG3 H 0.790 0.02 1 181 . 35 LYS HD2 H 1.130 0.02 1 182 . 35 LYS HD3 H 1.130 0.02 1 183 . 35 LYS HE2 H 2.400 0.02 1 184 . 35 LYS HE3 H 2.400 0.02 1 185 . 35 LYS HZ H 8.843 0.02 1 186 . 36 PRO HA H 3.660 0.02 1 187 . 36 PRO HB2 H 1.130 0.02 1 188 . 36 PRO HB3 H 1.130 0.02 1 189 . 36 PRO HD2 H 2.390 0.02 2 190 . 36 PRO HD3 H 1.850 0.02 2 191 . 37 GLN H H 8.350 0.02 1 192 . 37 GLN HA H 3.520 0.02 1 193 . 37 GLN HB2 H 1.700 0.02 2 194 . 37 GLN HB3 H 1.760 0.02 2 195 . 37 GLN HG2 H 2.110 0.02 1 196 . 37 GLN HG3 H 2.110 0.02 1 197 . 37 GLN HE21 H 7.390 0.02 2 198 . 37 GLN HE22 H 6.700 0.02 2 199 . 38 GLU H H 8.900 0.02 1 200 . 38 GLU HA H 3.880 0.02 1 201 . 38 GLU HB2 H 1.760 0.02 2 202 . 38 GLU HB3 H 1.730 0.02 2 203 . 38 GLU HG2 H 2.050 0.02 1 204 . 38 GLU HG3 H 2.050 0.02 1 205 . 39 LEU H H 7.330 0.02 1 206 . 39 LEU HA H 4.170 0.02 1 207 . 39 LEU HB2 H 1.100 0.02 2 208 . 39 LEU HB3 H 1.010 0.02 2 209 . 39 LEU HG H 1.340 0.02 1 210 . 39 LEU HD1 H 0.620 0.02 2 211 . 39 LEU HD2 H 0.510 0.02 2 212 . 40 LYS H H 7.410 0.02 1 213 . 40 LYS HA H 3.710 0.02 1 214 . 40 LYS HB2 H 1.580 0.02 2 215 . 40 LYS HB3 H 1.460 0.02 2 216 . 40 LYS HG2 H 1.340 0.02 2 217 . 40 LYS HG3 H 1.200 0.02 2 218 . 40 LYS HD2 H 1.130 0.02 2 219 . 40 LYS HD3 H 0.970 0.02 2 220 . 40 LYS HE2 H 2.560 0.02 1 221 . 40 LYS HE3 H 2.560 0.02 1 stop_ save_