Header list of 1a23.pdb file
Complete list - 16 20 Bytes
HEADER OXIDOREDUCTASE 15-JAN-98 1A23 TITLE SOLUTION NMR STRUCTURE OF REDUCED DSBA FROM ESCHERICHIA COLI, TITLE 2 MINIMIZED AVERAGE STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: DSBA; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI; SOURCE 3 ORGANISM_TAXID: 562; SOURCE 4 STRAIN: THZ2; SOURCE 5 CELLULAR_LOCATION: PERIPLASM; SOURCE 6 GENE: DSBA; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: THZ2; SOURCE 10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: PERIPLASM; SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PDSBA2; SOURCE 13 EXPRESSION_SYSTEM_GENE: DSBA KEYWDS THIOL-DISULFIDE OXIDOREDUCTASE, INTRODUCTION OF DISULFIDE BONDS, KEYWDS 2 PROTEIN FOLDING, REDOX-ACTIVE CENTER, OXIDOREDUCTASE EXPDTA SOLUTION NMR AUTHOR H.J.SCHIRRA,C.RENNER,M.CZISCH,M.HUBER-WUNDERLICH,T.A.HOLAK, AUTHOR 2 R.GLOCKSHUBER REVDAT 3 16-FEB-22 1A23 1 REMARK REVDAT 2 24-FEB-09 1A23 1 VERSN REVDAT 1 16-SEP-98 1A23 0 JRNL AUTH H.J.SCHIRRA,C.RENNER,M.CZISCH,M.HUBER-WUNDERLICH,T.A.HOLAK, JRNL AUTH 2 R.GLOCKSHUBER JRNL TITL STRUCTURE OF REDUCED DSBA FROM ESCHERICHIA COLI IN SOLUTION. JRNL REF BIOCHEMISTRY V. 37 6263 1998 JRNL REFN ISSN 0006-2960 JRNL PMID 9572841 JRNL DOI 10.1021/BI980136Y REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR 3.851 REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1A23 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_1000170297. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 300 REMARK 210 PH : 3.7 REMARK 210 IONIC STRENGTH : 20MM REMARK 210 PRESSURE : 1013 HPA REMARK 210 SAMPLE CONTENTS : 20 MM SODIUM PHOSPHATE IN H2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-NOESY-HSQC; 13C-NOESY-HSQC; REMARK 210 15N-HSQC; 13C-HSQC; HNCA; HNCO; REMARK 210 CBCA(CO)NH; HN(CA)CO; HNHA; REMARK 210 HBHA(CBCACO)NH; TOCSY; HCCH-TOCSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : AMX600; DRX600; DMX750 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CCNMR REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 80 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : ENERGY MINIMIZED MEAN STRUCTURE REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED WITH TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY AND MULTIDIMENSIONAL NMR EXPERIMENTS ON 13C/15N REMARK 210 LABELED DSBA 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: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O THR A 89 H PHE A 93 1.44 REMARK 500 H LEU A 23 O PHE A 154 1.59 REMARK 500 H SER A 104 OD2 ASP A 107 1.59 REMARK 500 H VAL A 155 O TYR A 159 1.60 REMARK 500 REMARK 500 REMARK: NULL 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 TYR A 3 105.44 80.48 REMARK 500 ASP A 5 90.93 52.90 REMARK 500 ALA A 19 158.61 -45.36 REMARK 500 VAL A 22 80.38 -153.21 REMARK 500 PHE A 28 53.07 -91.66 REMARK 500 PHE A 29 7.25 -150.97 REMARK 500 CYS A 33 -63.62 -29.57 REMARK 500 GLU A 38 -40.82 -132.58 REMARK 500 VAL A 39 -70.00 -106.63 REMARK 500 HIS A 41 18.84 59.11 REMARK 500 PHE A 63 57.24 -140.73 REMARK 500 MET A 64 54.61 -151.50 REMARK 500 ASP A 67 -80.22 -87.49 REMARK 500 LYS A 98 47.41 -152.48 REMARK 500 THR A 99 -48.60 -179.33 REMARK 500 ARG A 103 25.78 -141.98 REMARK 500 GLN A 146 -43.65 86.40 REMARK 500 LEU A 147 137.95 65.35 REMARK 500 ARG A 148 26.15 -159.59 REMARK 500 LYS A 158 -32.69 -159.19 REMARK 500 THR A 168 -87.54 -95.14 REMARK 500 SER A 169 26.52 -163.47 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 103 0.30 SIDE CHAIN REMARK 500 ARG A 109 0.14 SIDE CHAIN REMARK 500 ARG A 148 0.32 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1A24 RELATED DB: PDB DBREF 1A23 A 1 189 UNP P24991 DSBA_ECOLI 20 208 SEQRES 1 A 189 ALA GLN TYR GLU ASP GLY LYS GLN TYR THR THR LEU GLU SEQRES 2 A 189 LYS PRO VAL ALA GLY ALA PRO GLN VAL LEU GLU PHE PHE SEQRES 3 A 189 SER PHE PHE CYS PRO HIS CYS TYR GLN PHE GLU GLU VAL SEQRES 4 A 189 LEU HIS ILE SER ASP ASN VAL LYS LYS LYS LEU PRO GLU SEQRES 5 A 189 GLY VAL LYS MET THR LYS TYR HIS VAL ASN PHE MET GLY SEQRES 6 A 189 GLY ASP LEU GLY LYS ASP LEU THR GLN ALA TRP ALA VAL SEQRES 7 A 189 ALA MET ALA LEU GLY VAL GLU ASP LYS VAL THR VAL PRO SEQRES 8 A 189 LEU PHE GLU GLY VAL GLN LYS THR GLN THR ILE ARG SER SEQRES 9 A 189 ALA SER ASP ILE ARG ASP VAL PHE ILE ASN ALA GLY ILE SEQRES 10 A 189 LYS GLY GLU GLU TYR ASP ALA ALA TRP ASN SER PHE VAL SEQRES 11 A 189 VAL LYS SER LEU VAL ALA GLN GLN GLU LYS ALA ALA ALA SEQRES 12 A 189 ASP VAL GLN LEU ARG GLY VAL PRO ALA MET PHE VAL ASN SEQRES 13 A 189 GLY LYS TYR GLN LEU ASN PRO GLN GLY MET ASP THR SER SEQRES 14 A 189 ASN MET ASP VAL PHE VAL GLN GLN TYR ALA ASP THR VAL SEQRES 15 A 189 LYS TYR LEU SER GLU LYS LYS HELIX 1 1 PRO A 31 GLU A 37 1 7 HELIX 2 1' ILE A 42 LYS A 48 1 7 HELIX 3 2 LEU A 68 LEU A 82 1 15 HELIX 4 3 GLU A 85 GLN A 97 1 13 HELIX 5 4 ALA A 105 ALA A 115 1 11 HELIX 6 5 GLY A 119 ASN A 127 1 9 HELIX 7 6 VAL A 130 ASP A 144 1 15 HELIX 8 7 MET A 171 GLU A 187 1 17 SHEET 1 A 5 TYR A 9 THR A 11 0 SHEET 2 A 5 TYR A 159 LEU A 161 -1 N GLN A 160 O THR A 10 SHEET 3 A 5 ALA A 152 VAL A 155 -1 N VAL A 155 O TYR A 159 SHEET 4 A 5 VAL A 22 PHE A 25 -1 N LEU A 23 O PHE A 154 SHEET 5 A 5 MET A 56 TYR A 59 1 N THR A 57 O VAL A 22 CISPEP 1 VAL A 150 PRO A 151 0 -0.68 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 - 16 20 Bytes