data_5757 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 13C, 15N solid state NMR chemical shift assignments for the microcrystallin Crh domain swapped dimer ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bockmann Anja . . 2 Lange Adam . . 3 Galinier Anne . . 4 Luca Sorin . . 5 Giraud Nicolas . . 6 Juy Michel . . 7 Heise Henrike . . 8 Montserret Roland . . 9 Penin Francois . . 10 Baldus Marc . . stop_ _BMRB_accession_number 5757 _BMRB_flat_file_name bmr5757.str _Entry_type new _Submission_date 2003-03-27 _Accession_date 2003-03-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Chemical shifts for the monomeric (BMRB-4972) and dimeric forms of Crh show important differences due to conformational changes induced by the N-terminal 3D domain swap observed in the dimeric form ; loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 2 stop_ loop_ _Data_type _Data_type_count '15N chemical shifts' 90 '13C chemical shifts' 360 stop_ loop_ _Related_BMRB_accession_number _Relationship 4972 "Crh monomer in solution state" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bockmann Anja . . 2 Lange Adam . . 3 Galinier Anne . . 4 Luca Sorin . . 5 Giraud Nicolas . . 6 Juy Michel . . 7 Heise Henrike . . 8 Montserret Roland . . 9 Penin Francois . . 10 Baldus Marc . . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_volume 27 _Journal_issue 4 _Page_first 323 _Page_last 339 _Year 2003 loop_ _Keyword "Assignments" "catabolite repression histidine-containing phosphocarrier protein (Crh)" "MAS" "protein dynamics" "protein structure" "solid state NMR spectroscopy" stop_ save_ ################################## # Molecular system description # ################################## save_system_Crh _Saveframe_category molecular_system _Mol_system_name "Crh dimer" _Abbreviation_common Crh _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "Crh subunit 1" $Crh "Crh subunit 2" $Crh stop_ _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 "Crh subunit 1" 1 "Crh subunit 2" stop_ loop_ _Biological_function "phospho-carrier protein" stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1MU4 ? ; The system reported in the PDB data base corresponds to the Crh domain swapped dimer structure solved by a single crystal X-ray study. The system reported here corresponds to microcrystalline PEG precipitated Crh. TALOS dihedral angle predictions strongly indicate that the microcrystallin protein is equally in the dimeric domain swapped form observed for the diffracting crystals ; PDB 1K1C . ; The system reported in the PDB data base corresponds to the Crh monomer structure as determined by liquid state NMR methods.The system reported here corresponds to microcrystalline PEG precipitated Crh. TALOS dihedral angle predictions strongly indicate that the microcrystallin protein is in the dimeric domain swapped form observed for diffracting crystals (PDB 1mu4) ; stop_ save_ ######################## # Monomeric polymers # ######################## save_Crh _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "catabolite repression HPr" _Name_variant . _Abbreviation_common Crh _Molecular_mass 10391 _Mol_thiol_state 'not present' _Details ; Crh has been shown to exist in a slow monomer-dimer equilibrium in solution. The structure of the monomeric form could be solved by liquid state NMR spectroscopy. We recently solved the domain swapped dimer structure by X-ray crystallograpy. The microcrystall in solid Crh dimer serves us as model molecule for the development of solid state NMR methods ; ############################## # Polymer residue sequence # ############################## _Residue_count 93 _Mol_residue_sequence ; MVQQKVEVRLKTGLQARPAA LFVQEANRFTSDVFLEKDGK KVNAKSIMGLMSLAVSTGTE VTLIAQGEDEQEALEKLAAY VQEEVLQHHHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 VAL 3 GLN 4 GLN 5 LYS 6 VAL 7 GLU 8 VAL 9 ARG 10 LEU 11 LYS 12 THR 13 GLY 14 LEU 15 GLN 16 ALA 17 ARG 18 PRO 19 ALA 20 ALA 21 LEU 22 PHE 23 VAL 24 GLN 25 GLU 26 ALA 27 ASN 28 ARG 29 PHE 30 THR 31 SER 32 ASP 33 VAL 34 PHE 35 LEU 36 GLU 37 LYS 38 ASP 39 GLY 40 LYS 41 LYS 42 VAL 43 ASN 44 ALA 45 LYS 46 SER 47 ILE 48 MET 49 GLY 50 LEU 51 MET 52 SER 53 LEU 54 ALA 55 VAL 56 SER 57 THR 58 GLY 59 THR 60 GLU 61 VAL 62 THR 63 LEU 64 ILE 65 ALA 66 GLN 67 GLY 68 GLU 69 ASP 70 GLU 71 GLN 72 GLU 73 ALA 74 LEU 75 GLU 76 LYS 77 LEU 78 ALA 79 ALA 80 TYR 81 VAL 82 GLN 83 GLU 84 GLU 85 VAL 86 LEU 87 GLN 88 HIS 89 HIS 90 HIS 91 HIS 92 HIS 93 HIS stop_ _Sequence_homology_query_date 2008-06-26 _Sequence_homology_query_revised_last_date 2008-06-26 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 4972 "catabolite repression HPr" 93.55 87 100.00 100.00 3.38e-42 PDB 1K1C "Solution Structure Of Crh, The Bacillus Subtilis Catabolite Repression Hpr" 90.32 84 100.00 100.00 2.17e-40 PDB 1MU4 "Crystal Structure At 1.8 Angstroms Of The Bacillus Subtilis Catabolite Repression Histidine Containing Protein (Crh)" 93.55 87 100.00 100.00 3.38e-42 PDB 2AK7 "Structure Of A Dimeric P-Ser-Crh" 92.47 86 98.84 98.84 5.58e-41 EMBL CAB08060 "hypothetical protein [Bacillus subtilis]" 91.40 85 100.00 100.00 3.80e-41 EMBL CAB15479 "catabolite repression HPr-like protein [Bacillus subtilis subsp. subtilis str. 168]" 91.40 85 100.00 100.00 3.80e-41 REF NP_391354 "catabolite repression HPr-like protein [Bacillus subtilis subsp. subtilis str. 168]" 91.40 85 100.00 100.00 3.80e-41 SWISS-PROT O06976 "HPr-like protein crh (Catabolite repression HPr)" 91.40 85 100.00 100.00 3.80e-41 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Crh "Bacillus subtilis" 1423 Eubacteria . Bacillus subtilis 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 $Crh 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solid _Details ; Microcrystallin solid protein obtained by slow precipitation with PEG ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $Crh . mg 4 20 "[U-98% 13C; U-98% 15N]" stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 2.0 loop_ _Task "data processing" stop_ save_ save_NMRVIEW _Saveframe_category software _Name NMRVIEW _Version 5.0 loop_ _Task assignments stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DSX _Field_strength 500 save_ save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DSX _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 13C-13C proton driven spin diffusion (PDSD) 13C-13C CO selective J-decoupled PDSD 13C-13C RFDR 13C-13C DQ SPC-5 15N-13C NCACO 15N-13C NCOCACB ; save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details ; The actual sample temperature is around 278K, which is not read out probe T. MAS speed is around 10 kHz. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.9 0.2 n/a temperature 278 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 external_to_the_sample direct . external_to_the_sample . . 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 # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "Crh subunit 1" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 VAL N N 116.5 0.1 1 2 2 VAL CA C 58.0 0.1 1 3 2 VAL CB C 35.1 0.1 1 4 2 VAL CG1 C 21.5 0.1 1 5 2 VAL CG2 C 21.5 0.1 1 6 2 VAL C C 174.0 0.1 1 7 3 GLN N N 82.6 0.1 1 8 3 GLN CA C 54.9 0.1 1 9 3 GLN CB C 32.7 0.1 1 10 3 GLN CG C 30.9 0.1 1 11 3 GLN C C 172.2 0.1 1 12 4 GLN N N 125.5 0.1 1 13 4 GLN CA C 55.5 0.1 1 14 4 GLN CB C 32.2 0.1 1 15 4 GLN CG C 33.2 0.1 1 16 4 GLN CD C 180.2 0.1 1 17 4 GLN C C 174.1 0.1 1 18 5 LYS N N 115.2 0.1 1 19 5 LYS CA C 53.5 0.1 1 20 5 LYS CB C 33.2 0.1 1 21 5 LYS CG C 24.5 0.1 1 22 5 LYS CD C 28.8 0.1 1 23 5 LYS CE C 40.1 0.1 1 24 5 LYS C C 174.9 0.1 1 25 6 VAL N N 117.4 0.1 1 26 6 VAL CA C 55.5 0.1 1 27 6 VAL CB C 35.6 0.1 1 28 6 VAL CG1 C 19.8 0.1 2 29 6 VAL CG2 C 22.9 0.1 2 30 6 VAL C C 175.6 0.1 1 31 7 GLU N N 123.3 0.1 1 32 7 GLU CA C 54.5 0.1 1 33 7 GLU CB C 31.3 0.1 1 34 7 GLU CG C 36.8 0.1 1 35 7 GLU CD C 182.9 0.1 1 36 7 GLU C C 175.4 0.1 1 37 8 VAL N N 122.7 0.1 1 38 8 VAL CA C 63.7 0.1 1 39 8 VAL CB C 31.1 0.1 1 40 8 VAL CG1 C 21.6 0.1 2 41 8 VAL CG2 C 22.4 0.1 2 42 8 VAL C C 176.8 0.1 1 43 9 ARG N N 126.8 0.1 1 44 9 ARG CA C 54.1 0.1 1 45 9 ARG CB C 28.0 0.1 1 46 10 LEU N N 116.7 0.1 1 47 10 LEU CA C 52.9 0.1 1 48 10 LEU CB C 43.0 0.1 1 49 10 LEU CG C 25.5 0.1 1 50 10 LEU CD1 C 21.0 0.1 1 51 10 LEU CD2 C 21.0 0.1 1 52 11 LYS N N 118.6 0.1 1 53 11 LYS CA C 58.1 0.1 1 54 11 LYS CB C 33.3 0.1 1 55 11 LYS C C 174.1 0.1 1 56 12 THR N N 109.5 0.1 1 57 12 THR CA C 59.1 0.1 1 58 12 THR CB C 73.4 0.1 1 59 12 THR CG2 C 20.7 0.1 1 60 12 THR C C 173.8 0.1 1 61 13 GLY N N 106.4 0.1 1 62 13 GLY CA C 44.9 0.1 1 63 13 GLY C C 172.1 0.1 1 64 14 LEU N N 120.0 0.1 1 65 14 LEU CA C 56.2 0.1 1 66 14 LEU CB C 43.4 0.1 1 67 14 LEU CG C 26.6 0.1 1 68 14 LEU CD1 C 24.8 0.1 1 69 14 LEU CD2 C 24.8 0.1 1 70 14 LEU C C 177.2 0.1 1 71 15 GLN N N 118.4 0.1 1 72 15 GLN CA C 55.3 0.1 1 73 15 GLN CB C 33.8 0.1 1 74 15 GLN CG C 32.1 0.1 1 75 15 GLN CD C 180.1 0.1 1 76 15 GLN C C 174.1 0.1 1 77 16 ALA N N 118.2 0.1 1 78 16 ALA CA C 54.9 0.1 1 79 16 ALA CB C 16.9 0.1 1 80 16 ALA C C 179.1 0.1 1 81 17 ARG N N 121.4 0.1 1 82 17 ARG CA C 61.4 0.1 1 83 17 ARG CB C 27.2 0.1 1 84 17 ARG C C 177.5 0.1 1 85 18 PRO N N 133.6 0.1 1 86 18 PRO CA C 65.1 0.1 1 87 18 PRO CB C 31.6 0.1 1 88 18 PRO CG C 28.2 0.1 1 89 18 PRO CD C 49.2 0.1 1 90 18 PRO C C 180.0 0.1 1 91 19 ALA N N 119.8 0.1 1 92 19 ALA CA C 55.5 0.1 1 93 19 ALA CB C 18.3 0.1 1 94 20 ALA N N 121.5 0.1 1 95 20 ALA CA C 54.8 0.1 1 96 20 ALA CB C 18.3 0.1 1 97 21 LEU N N 119.6 0.1 1 98 21 LEU CA C 56.9 0.1 1 99 21 LEU CB C 40.6 0.1 1 100 21 LEU CG C 26.9 0.1 1 101 21 LEU CD1 C 20.8 0.1 1 102 21 LEU CD2 C 20.8 0.1 1 103 21 LEU C C 178.6 0.1 1 104 22 PHE N N 122.6 0.1 1 105 22 PHE CA C 61.1 0.1 1 106 22 PHE CB C 38.4 0.1 1 107 22 PHE CG C 138.9 0.1 1 108 22 PHE CD1 C 131.6 0.1 1 109 22 PHE CD2 C 131.6 0.1 1 110 22 PHE C C 177.6 0.1 1 111 23 VAL N N 120.2 0.1 1 112 23 VAL CA C 66.6 0.1 1 113 23 VAL CB C 31.5 0.1 1 114 23 VAL CG1 C 22.0 0.1 2 115 23 VAL CG2 C 23.3 0.1 2 116 23 VAL C C 177.0 0.1 1 117 24 GLN N N 118.2 0.1 1 118 24 GLN CA C 58.7 0.1 1 119 24 GLN CB C 29.0 0.1 1 120 24 GLN CG C 34.2 0.1 1 121 24 GLN CD C 180.1 0.1 1 122 25 GLU N N 117.9 0.1 1 123 25 GLU CA C 57.8 0.1 1 124 25 GLU CB C 28.6 0.1 1 125 25 GLU CG C 34.4 0.1 1 126 25 GLU CD C 182.7 0.1 1 127 26 ALA N N 118.2 0.1 1 128 26 ALA CA C 54.6 0.1 1 129 26 ALA CB C 17.8 0.1 1 130 27 ASN N N 113.9 0.1 1 131 27 ASN CA C 53.8 0.1 1 132 27 ASN CB C 38.4 0.1 1 133 27 ASN CG C 176.1 0.1 1 134 27 ASN ND2 N 110.3 0.1 1 135 28 ARG N N 117.9 0.1 1 136 28 ARG CA C 57.2 0.1 1 137 28 ARG CB C 28.9 0.1 1 138 28 ARG CG C 27.4 0.1 1 139 28 ARG CD C 42.8 0.1 1 140 29 PHE N N 118.5 0.1 1 141 29 PHE CA C 56.8 0.1 1 142 29 PHE CB C 39.6 0.1 1 143 29 PHE CG C 140.5 0.1 1 144 29 PHE CD1 C 131.5 0.1 1 145 29 PHE CD2 C 131.5 0.1 1 146 29 PHE C C 175.8 0.1 1 147 30 THR N N 119.8 0.1 1 148 30 THR CA C 63.8 0.1 1 149 30 THR CB C 68.7 0.1 1 150 30 THR CG2 C 21.9 0.1 1 151 30 THR C C 177.7 0.1 1 152 31 SER N N 121.6 0.1 1 153 31 SER CA C 61.6 0.1 1 154 31 SER CB C 64.9 0.1 1 155 31 SER C C 173.7 0.1 1 156 32 ASP N N 121.5 0.1 1 157 32 ASP CA C 54.2 0.1 1 158 32 ASP CB C 42.2 0.1 1 159 32 ASP CG C 180.2 0.1 1 160 32 ASP C C 175.5 0.1 1 161 33 VAL N N 120.8 0.1 1 162 33 VAL CA C 59.6 0.1 1 163 33 VAL CB C 35.2 0.1 1 164 33 VAL CG1 C 22.2 0.1 2 165 33 VAL CG2 C 20.0 0.1 2 166 33 VAL C C 173.9 0.1 1 167 34 PHE N N 122.0 0.1 1 168 34 PHE CA C 55.0 0.1 1 169 34 PHE CB C 43.1 0.1 1 170 34 PHE CG C 138.7 0.1 1 171 34 PHE CD1 C 131.6 0.1 1 172 34 PHE CD2 C 131.6 0.1 1 173 34 PHE C C 174.9 0.1 1 174 35 LEU N N 117.7 0.1 1 175 35 LEU CA C 53.2 0.1 1 176 35 LEU CB C 46.3 0.1 1 177 35 LEU CG C 27.6 0.1 1 178 35 LEU CD1 C 24.2 0.1 2 179 35 LEU CD2 C 25.4 0.1 2 180 35 LEU C C 175.6 0.1 1 181 36 GLU N N 122.9 0.1 1 182 36 GLU CA C 53.8 0.1 1 183 36 GLU CB C 34.3 0.1 1 184 36 GLU CG C 36.3 0.1 1 185 36 GLU CD C 182.0 0.1 1 186 36 GLU C C 174.7 0.1 1 187 37 LYS N N 123.8 0.1 1 188 37 LYS CA C 55.8 0.1 1 189 37 LYS CB C 36.1 0.1 1 190 37 LYS CG C 25.0 0.1 1 191 37 LYS CD C 28.9 0.1 1 192 37 LYS CE C 42.1 0.1 1 193 38 ASP N N 129.9 0.1 1 194 38 ASP CA C 55.4 0.1 1 195 38 ASP CB C 39.6 0.1 1 196 38 ASP CG C 180.9 0.1 1 197 38 ASP C C 175.5 0.1 1 198 39 GLY N N 105.0 0.1 1 199 39 GLY CA C 45.0 0.1 1 200 39 GLY C C 173.8 0.1 1 201 40 LYS N N 122.6 0.1 1 202 40 LYS CA C 54.0 0.1 1 203 40 LYS CB C 33.3 0.1 1 204 40 LYS CG C 25.0 0.1 1 205 40 LYS CD C 28.9 0.1 1 206 40 LYS CE C 42.1 0.1 1 207 41 LYS N N 126.0 0.1 1 208 41 LYS CA C 54.1 0.1 1 209 41 LYS CB C 35.4 0.1 1 210 41 LYS CG C 25.2 0.1 1 211 41 LYS CD C 28.9 0.1 1 212 41 LYS CE C 40.7 0.1 1 213 42 VAL N N 118.8 0.1 1 214 42 VAL CA C 57.9 0.1 1 215 42 VAL CB C 35.0 0.1 1 216 42 VAL CG1 C 18.4 0.1 2 217 42 VAL CG2 C 21.6 0.1 2 218 43 ASN N N 121.4 0.1 1 219 43 ASN CA C 53.0 0.1 1 220 43 ASN CB C 38.1 0.1 1 221 43 ASN CG C 176.7 0.1 1 222 43 ASN C C 174.9 0.1 1 223 43 ASN ND2 N 111.0 0.1 1 224 44 ALA N N 128.4 0.1 1 225 44 ALA CA C 51.8 0.1 1 226 44 ALA CB C 18.9 0.1 1 227 44 ALA C C 173.8 0.1 1 228 45 LYS N N 110.2 0.1 1 229 45 LYS CA C 55.6 0.1 1 230 45 LYS CB C 31.5 0.1 1 231 45 LYS CG C 27.4 0.1 1 232 45 LYS CD C 29.5 0.1 1 233 45 LYS CE C 42.8 0.1 1 234 45 LYS C C 175.5 0.1 1 235 46 SER N N 114.9 0.1 1 236 46 SER CA C 54.2 0.1 1 237 46 SER CB C 64.6 0.1 1 238 46 SER C C 174.4 0.1 1 239 47 ILE N N 131.0 0.1 1 240 47 ILE CA C 66.4 0.1 1 241 47 ILE CB C 37.7 0.1 1 242 47 ILE CG1 C 30.4 0.1 1 243 47 ILE CG2 C 17.8 0.1 1 244 47 ILE CD1 C 14.1 0.1 1 245 47 ILE C C 178.0 0.1 1 246 48 MET N N 117.7 0.1 1 247 48 MET CA C 58.3 0.1 1 248 48 MET CB C 32.3 0.1 1 249 48 MET CG C 32.2 0.1 1 250 48 MET CE C 15.9 0.1 1 251 49 GLY N N 107.9 0.1 1 252 49 GLY CA C 46.9 0.1 1 253 49 GLY C C 176.9 0.1 1 254 50 LEU N N 124.8 0.1 1 255 50 LEU CA C 58.2 0.1 1 256 50 LEU CB C 43.3 0.1 1 257 50 LEU C C 179.7 0.1 1 258 51 MET N N 114.3 0.1 1 259 51 MET CA C 59.1 0.1 1 260 51 MET CB C 33.6 0.1 1 261 51 MET CG C 33.5 0.1 1 262 51 MET CE C 15.8 0.1 1 263 52 SER N N 112.3 0.1 1 264 52 SER CA C 59.8 0.1 1 265 52 SER CB C 63.8 0.1 1 266 52 SER C C 175.2 0.1 1 267 53 LEU N N 122.0 0.1 1 268 53 LEU CA C 54.2 0.1 1 269 53 LEU CB C 42.8 0.1 1 270 53 LEU CG C 26.1 0.1 1 271 53 LEU CD1 C 22.4 0.1 1 272 53 LEU CD2 C 22.4 0.1 1 273 54 ALA N N 131.2 0.1 1 274 54 ALA CA C 51.8 0.1 1 275 54 ALA CB C 17.1 0.1 1 276 54 ALA C C 176.8 0.1 1 277 55 VAL N N 121.2 0.1 1 278 55 VAL CA C 60.2 0.1 1 279 55 VAL CB C 37.1 0.1 1 280 55 VAL CG1 C 20.0 0.1 2 281 55 VAL CG2 C 22.9 0.1 2 282 55 VAL C C 180.9 0.1 1 283 56 SER N N 118.0 0.1 1 284 56 SER CA C 56.7 0.1 1 285 56 SER CB C 65.9 0.1 1 286 56 SER C C 173.5 0.1 1 287 57 THR N N 122.4 0.1 1 288 57 THR CA C 65.8 0.1 1 289 57 THR CB C 68.4 0.1 1 290 57 THR CG2 C 22.4 0.1 1 291 57 THR C C 175.8 0.1 1 292 58 GLY N N 117.1 0.1 1 293 58 GLY CA C 44.4 0.1 1 294 58 GLY C C 173.9 0.1 1 295 59 THR N N 117.2 0.1 1 296 59 THR CA C 63.0 0.1 1 297 59 THR CB C 68.8 0.1 1 298 59 THR CG2 C 22.4 0.1 1 299 59 THR C C 172.4 0.1 1 300 60 GLU N N 121.8 0.1 1 301 60 GLU CA C 54.3 0.1 1 302 60 GLU CB C 32.7 0.1 1 303 60 GLU CG C 36.3 0.1 1 304 60 GLU CD C 183.2 0.1 1 305 61 VAL N N 118.9 0.1 1 306 61 VAL CA C 58.4 0.1 1 307 61 VAL CB C 34.8 0.1 1 308 61 VAL CG1 C 22.9 0.1 2 309 61 VAL CG2 C 19.8 0.1 2 310 62 THR N N 117.2 0.1 1 311 62 THR CA C 62.6 0.1 1 312 62 THR CB C 69.1 0.1 1 313 62 THR CG2 C 22.5 0.1 1 314 62 THR C C 172.6 0.1 1 315 63 LEU N N 131.0 0.1 1 316 63 LEU CA C 53.8 0.1 1 317 63 LEU CB C 45.0 0.1 1 318 63 LEU CG C 27.6 0.1 1 319 63 LEU CD1 C 24.2 0.1 1 320 63 LEU CD2 C 24.2 0.1 1 321 64 ILE N N 125.8 0.1 1 322 64 ILE CA C 59.8 0.1 1 323 64 ILE CB C 42.6 0.1 1 324 64 ILE CG1 C 28.0 0.1 1 325 64 ILE CG2 C 17.8 0.1 1 326 64 ILE CD1 C 15.0 0.1 1 327 64 ILE C C 173.9 0.1 1 328 65 ALA N N 126.4 0.1 1 329 65 ALA CA C 50.0 0.1 1 330 65 ALA CB C 23.0 0.1 1 331 65 ALA C C 175.9 0.1 1 332 66 GLN N N 120.1 0.1 1 333 66 GLN CA C 53.7 0.1 1 334 66 GLN CB C 32.1 0.1 1 335 66 GLN CG C 33.4 0.1 1 336 66 GLN CD C 179.1 0.1 1 337 66 GLN C C 174.2 0.1 1 338 67 GLY N N 119.5 0.1 1 339 67 GLY CA C 45.2 0.1 1 340 67 GLY C C 174.9 0.1 1 341 68 GLU N N 118.7 0.1 1 342 68 GLU CA C 59.2 0.1 1 343 68 GLU CB C 29.9 0.1 1 344 68 GLU CG C 36.2 0.1 1 345 68 GLU CD C 183.3 0.1 1 346 69 ASP N N 114.8 0.1 1 347 69 ASP CA C 51.1 0.1 1 348 69 ASP CB C 39.4 0.1 1 349 69 ASP CG C 179.6 0.1 1 350 69 ASP C C 176.2 0.1 1 351 70 GLU N N 116.3 0.1 1 352 70 GLU CA C 57.4 0.1 1 353 70 GLU CB C 27.2 0.1 1 354 70 GLU CG C 36.9 0.1 1 355 70 GLU CD C 184.5 0.1 1 356 70 GLU C C 175.1 0.1 1 357 71 GLN N N 121.4 0.1 1 358 71 GLN CA C 59.5 0.1 1 359 71 GLN CB C 27.7 0.1 1 360 71 GLN CG C 33.8 0.1 1 361 71 GLN CD C 179.7 0.1 1 362 72 GLU N N 117.1 0.1 1 363 72 GLU CA C 59.3 0.1 1 364 72 GLU CB C 26.8 0.1 1 365 72 GLU CG C 34.2 0.1 1 366 72 GLU CD C 183.2 0.1 1 367 73 ALA N N 122.4 0.1 1 368 73 ALA CA C 53.5 0.1 1 369 73 ALA CB C 17.9 0.1 1 370 73 ALA C C 178.7 0.1 1 371 74 LEU N N 116.5 0.1 1 372 74 LEU CA C 58.0 0.1 1 373 74 LEU CB C 42.1 0.1 1 374 74 LEU CG C 26.0 0.1 1 375 74 LEU CD1 C 24.3 0.1 1 376 74 LEU CD2 C 24.3 0.1 1 377 75 GLU N N 116.9 0.1 1 378 75 GLU CA C 58.9 0.1 1 379 75 GLU CB C 29.4 0.1 1 380 75 GLU CG C 36.2 0.1 1 381 75 GLU CD C 182.6 0.1 1 382 75 GLU C C 176.2 0.1 1 383 76 LYS N N 118.9 0.1 1 384 76 LYS CA C 59.0 0.1 1 385 76 LYS CB C 32.2 0.1 1 386 76 LYS CG C 24.8 0.1 1 387 76 LYS CD C 28.6 0.1 1 388 76 LYS CE C 42.1 0.1 1 389 77 LEU N N 119.3 0.1 1 390 77 LEU CA C 57.5 0.1 1 391 77 LEU CB C 40.9 0.1 1 392 77 LEU CG C 26.8 0.1 1 393 77 LEU CD1 C 22.5 0.1 1 394 77 LEU CD2 C 22.5 0.1 1 395 77 LEU C C 179.1 0.1 1 396 78 ALA N N 121.1 0.1 1 397 78 ALA CA C 55.1 0.1 1 398 78 ALA CB C 18.2 0.1 1 399 78 ALA C C 181.5 0.1 1 400 79 ALA N N 120.1 0.1 1 401 79 ALA CA C 55.6 0.1 1 402 79 ALA CB C 18.7 0.1 1 403 79 ALA C C 180.9 0.1 1 404 80 TYR N N 116.8 0.1 1 405 80 TYR CA C 61.3 0.1 1 406 80 TYR CB C 38.0 0.1 1 407 80 TYR CG C 129.7 0.1 1 408 80 TYR CD1 C 132.8 0.1 1 409 80 TYR CD2 C 132.8 0.1 1 410 80 TYR CE1 C 118.2 0.1 1 411 80 TYR CE2 C 118.2 0.1 1 412 80 TYR CZ C 157.3 0.1 1 413 80 TYR C C 176.8 0.1 1 414 81 VAL N N 117.8 0.1 1 415 81 VAL CA C 64.6 0.1 1 416 81 VAL CB C 32.2 0.1 1 417 81 VAL CG1 C 22.1 0.1 2 418 81 VAL CG2 C 23.5 0.1 2 419 81 VAL C C 174.6 0.1 1 420 82 GLN N N 113.4 0.1 1 421 82 GLN CA C 55.7 0.1 1 422 82 GLN CB C 29.9 0.1 1 423 82 GLN CG C 35.1 0.1 1 424 82 GLN CD C 179.0 0.1 1 425 83 GLU N N 114.9 0.1 1 426 83 GLU CA C 55.7 0.1 1 427 83 GLU CB C 30.0 0.1 1 428 83 GLU CG C 36.2 0.1 1 429 83 GLU CD C 181.7 0.1 1 430 84 GLU N N 114.9 0.1 1 431 84 GLU CA C 55.3 0.1 1 432 84 GLU CB C 29.8 0.1 1 433 84 GLU CG C 36.2 0.1 1 434 84 GLU CD C 181.7 0.1 1 435 85 VAL N N 93.4 0.1 1 436 85 VAL CA C 60.6 0.1 1 437 85 VAL CB C 32.7 0.1 1 438 85 VAL CG2 C 19.3 0.1 2 439 85 VAL CG1 C 21.3 0.1 2 440 85 VAL C C 171.1 0.1 1 stop_ save_ save_shift_set_2 _Saveframe_category assigned_chemical_shifts _Details ; Peak doubling has been observed for a limited number of signals, indicating conformational or dynamic disorder. The minor signals are reported in this list. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "Crh subunit 1" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 10 LEU CA C 53.1 0.1 1 2 10 LEU CB C 42.6 0.1 1 3 12 THR N N 111.0 0.1 1 4 18 PRO C C 178.8 0.1 1 5 38 ASP CB C 40.0 0.1 1 6 38 ASP CG C 181.7 0.1 1 7 49 GLY N N 109.5 0.1 1 8 52 SER N N 113.1 0.1 1 9 54 ALA C C 175.7 0.1 1 10 67 GLY N N 117.1 0.1 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _PubMed_ID 11361074 save_ save_ref_2 _Saveframe_category citation _PubMed_ID 11916384 save_ save_ref_3 _Saveframe_category citation _PubMed_ID . _Citation_full ; Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue HPr Juy, M., Penin, F., Favier, A., Galinier, A., Montserret, R., Haser, R., Deutscher, J. and Bockmann, A. (2003) submitted ; save_