Header list of 1yub.pdb file
Complete list - 2 20 Bytes
HEADER METHYLTRANSFERASE 04-MAR-97 1YUB TITLE SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS TITLE 2 MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, TITLE 3 MINIMIZED AVERAGE STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: RRNA METHYLTRANSFERASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ERMAM; COMPND 5 EC: 2.1.1.48; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE; SOURCE 3 ORGANISM_TAXID: 1313; SOURCE 4 STRAIN: 5728, A CLINICAL ISOLATE FROM ABBOTT CULTURE COLLECTION; SOURCE 5 CELL_LINE: BL21; SOURCE 6 GENE: ERM; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-24(+); SOURCE 11 EXPRESSION_SYSTEM_GENE: ERM KEYWDS METHYLTRANSFERASE, ERM, ERMAM, MLS ANTIBIOTICS, RRNA EXPDTA SOLUTION NMR AUTHOR L.YU,A.M.PETROS,A.SCHNUCHEL,P.ZHONG,J.M.SEVERIN,K.WALTER,T.F.HOLZMAN, AUTHOR 2 S.W.FESIK REVDAT 3 02-MAR-22 1YUB 1 REMARK REVDAT 2 24-FEB-09 1YUB 1 VERSN REVDAT 1 04-MAR-98 1YUB 0 JRNL AUTH L.YU,A.M.PETROS,A.SCHNUCHEL,P.ZHONG,J.M.SEVERIN,K.WALTER, JRNL AUTH 2 T.F.HOLZMAN,S.W.FESIK JRNL TITL SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT JRNL TITL 2 CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC JRNL TITL 3 RESISTANCE. JRNL REF NAT.STRUCT.BIOL. V. 4 483 1997 JRNL REFN ISSN 1072-8368 JRNL PMID 9187657 JRNL DOI 10.1038/NSB0697-483 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH L.YU,A.M.PETROS,A.SCHNUCHEL,P.ZHONG,J.M.SEVERIN,K.WALTER, REMARK 1 AUTH 2 T.F.HOLZMAN,S.W.FESIK REMARK 1 TITL ERRATUM. SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE REMARK 1 TITL 2 (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN REMARK 1 TITL 3 ANTIBIOTIC RESISTANCE REMARK 1 REF NAT.STRUCT.BIOL. V. 4 592 1997 REMARK 1 REFN ISSN 1072-8368 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.1 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE TOTAL NUMBER OF DISTANCE RESTRAINTS REMARK 3 USED WAS 3259. THE TOTAL NUMBER OF TORSIONAL RESTRAINTS USED WAS REMARK 3 63. REMARK 4 REMARK 4 1YUB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000177444. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.5 REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE, 100 MM REMARK 210 NACL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D; 3D; 4D NMR REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX500; AMX600; DRX800 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR 3.1 REMARK 210 METHOD USED : DG/SA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 17 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY AND LEAST REMARK 210 RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: NULL REMARK 215 REMARK 215 NMR STUDY REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON REMARK 215 THESE RECORDS ARE MEANINGLESS. REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LYS A 3 -148.79 40.56 REMARK 500 ASN A 4 62.99 175.11 REMARK 500 LYS A 6 50.43 -115.45 REMARK 500 TYR A 7 -157.04 -125.86 REMARK 500 THR A 13 43.29 24.93 REMARK 500 ASN A 26 96.32 46.43 REMARK 500 LYS A 28 -74.44 -92.00 REMARK 500 GLU A 29 -35.37 169.85 REMARK 500 THR A 32 172.81 -43.58 REMARK 500 THR A 38 -150.32 -115.88 REMARK 500 HIS A 42 67.12 -179.35 REMARK 500 LEU A 43 -174.36 170.01 REMARK 500 THR A 44 -74.30 79.37 REMARK 500 LEU A 59 156.58 58.20 REMARK 500 LEU A 63 -71.28 81.09 REMARK 500 SER A 67 88.57 -54.27 REMARK 500 SER A 68 96.42 39.49 REMARK 500 LEU A 71 33.92 -81.47 REMARK 500 LEU A 73 65.89 35.69 REMARK 500 ASN A 74 31.68 -152.58 REMARK 500 THR A 75 -129.28 -114.53 REMARK 500 ARG A 76 79.64 -107.68 REMARK 500 GLN A 82 -154.97 78.55 REMARK 500 ASP A 83 139.94 -31.88 REMARK 500 ILE A 84 -108.31 -140.50 REMARK 500 LEU A 85 -83.84 45.88 REMARK 500 PHE A 89 97.68 -39.04 REMARK 500 PRO A 90 -159.76 -85.42 REMARK 500 LYS A 92 146.28 76.17 REMARK 500 GLN A 93 -168.77 80.27 REMARK 500 TYR A 103 4.24 81.02 REMARK 500 LEU A 105 133.30 169.95 REMARK 500 SER A 106 -40.60 179.78 REMARK 500 GLU A 116 -6.59 -141.48 REMARK 500 SER A 120 -47.93 83.45 REMARK 500 GLU A 128 -84.38 164.07 REMARK 500 THR A 134 -63.24 -93.66 REMARK 500 THR A 140 -5.52 71.03 REMARK 500 LEU A 154 -66.89 -121.53 REMARK 500 ALA A 159 43.11 81.41 REMARK 500 PRO A 166 -171.15 -48.89 REMARK 500 LYS A 167 -43.02 -156.09 REMARK 500 ARG A 177 101.54 -56.57 REMARK 500 HIS A 178 -166.71 -107.04 REMARK 500 THR A 179 -82.50 -57.44 REMARK 500 THR A 180 128.37 -178.95 REMARK 500 ASP A 184 -34.27 -39.82 REMARK 500 VAL A 198 -68.75 -100.72 REMARK 500 ASN A 199 -72.48 -43.95 REMARK 500 ARG A 200 35.61 171.44 REMARK 500 REMARK 500 THIS ENTRY HAS 56 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 76 0.30 SIDE CHAIN REMARK 500 ARG A 94 0.11 SIDE CHAIN REMARK 500 ARG A 118 0.28 SIDE CHAIN REMARK 500 ARG A 133 0.32 SIDE CHAIN REMARK 500 ARG A 139 0.15 SIDE CHAIN REMARK 500 ARG A 177 0.30 SIDE CHAIN REMARK 500 ARG A 200 0.20 SIDE CHAIN REMARK 500 ARG A 203 0.20 SIDE CHAIN REMARK 500 ARG A 244 0.27 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1YUB A 1 245 UNP P21236 ERM_STRPN 1 245 SEQRES 1 A 245 MET ASN LYS ASN ILE LYS TYR SER GLN ASN PHE LEU THR SEQRES 2 A 245 SER GLU LYS VAL LEU ASN GLN ILE ILE LYS GLN LEU ASN SEQRES 3 A 245 LEU LYS GLU THR ASP THR VAL TYR GLU ILE GLY THR GLY SEQRES 4 A 245 LYS GLY HIS LEU THR THR LYS LEU ALA LYS ILE SER LYS SEQRES 5 A 245 GLN VAL THR SER ILE GLU LEU ASP SER HIS LEU PHE ASN SEQRES 6 A 245 LEU SER SER GLU LYS LEU LYS LEU ASN THR ARG VAL THR SEQRES 7 A 245 LEU ILE HIS GLN ASP ILE LEU GLN PHE GLN PHE PRO ASN SEQRES 8 A 245 LYS GLN ARG TYR LYS ILE VAL GLY ASN ILE PRO TYR HIS SEQRES 9 A 245 LEU SER THR GLN ILE ILE LYS LYS VAL VAL PHE GLU SER SEQRES 10 A 245 ARG ALA SER ASP ILE TYR LEU ILE VAL GLU GLU GLY PHE SEQRES 11 A 245 TYR LYS ARG THR LEU ASP ILE HIS ARG THR LEU GLY LEU SEQRES 12 A 245 LEU LEU HIS THR GLN VAL SER ILE GLN GLN LEU LEU LYS SEQRES 13 A 245 LEU PRO ALA GLU CYS PHE HIS PRO LYS PRO LYS VAL ASN SEQRES 14 A 245 SER VAL LEU ILE LYS LEU THR ARG HIS THR THR ASP VAL SEQRES 15 A 245 PRO ASP LYS TYR TRP LYS LEU TYR THR TYR PHE VAL SER SEQRES 16 A 245 LYS TRP VAL ASN ARG GLU TYR ARG GLN LEU PHE THR LYS SEQRES 17 A 245 ASN GLN PHE HIS GLN ALA MET LYS HIS ALA LYS VAL ASN SEQRES 18 A 245 ASN LEU SER THR ILE THR TYR GLU GLN VAL LEU SER ILE SEQRES 19 A 245 PHE ASN SER TYR LEU LEU PHE ASN GLY ARG LYS HELIX 1 H1 LYS A 16 LEU A 25 1 10 HELIX 2 H2 LEU A 43 ILE A 50 1 8 HELIX 3 H3 HIS A 62 ASN A 65 1 4 HELIX 4 H4 LEU A 85 GLN A 88 1 4 HELIX 5 H5 SER A 106 GLU A 116 1 11 HELIX 6 H6 GLY A 129 ASP A 136 1 8 HELIX 7 H7 THR A 140 HIS A 146 1 7 HELIX 8 H8 TYR A 186 ASN A 199 1 14 HELIX 9 H9 TYR A 202 LEU A 205 1 4 HELIX 10 H10 GLN A 210 ALA A 218 1 9 HELIX 11 H11 TYR A 228 PHE A 241 1 14 SHEET 1 SH1 7 ARG A 76 ILE A 80 0 SHEET 2 SH1 7 GLN A 53 ILE A 57 1 N SER A 56 O THR A 78 SHEET 3 SH1 7 THR A 32 ILE A 36 1 N VAL A 33 O GLN A 53 SHEET 4 SH1 7 TYR A 95 ASN A 100 1 N VAL A 98 O TYR A 34 SHEET 5 SH1 7 SER A 120 GLU A 127 1 N TYR A 123 O ILE A 97 SHEET 6 SH1 7 SER A 170 ARG A 177 -1 N ILE A 173 O LEU A 124 SHEET 7 SH1 7 VAL A 149 LYS A 156 -1 N GLN A 152 O LYS A 174 SHEET 1 SH2 2 PHE A 11 THR A 13 0 SHEET 2 SH2 2 CYS A 161 HIS A 163 -1 O HIS A 163 N PHE A 11 CISPEP 1 HIS A 163 PRO A 164 0 -0.16 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000
Complete list - 2 20 Bytes