Header list of 2b8f.pdb file
Complete list - 9 20 Bytes
HEADER BIOSYNTHETIC PROTEIN 06-OCT-05 2B8F TITLE SOLUTION STRUCTURE OF BACILLUS SUBTILIS BLAP APO FORM (ENERGY TITLE 2 MINIMIZED MEAN STRUCTURE) CAVEAT 2B8F CHIRALITY ERROR AT CA CENTER OF THR A 72 COMPND MOL_ID: 1; COMPND 2 MOLECULE: BIOTIN/LIPOYL ATTACHMENT PROTEIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS; SOURCE 3 ORGANISM_TAXID: 1423; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS; SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-21A(+) KEYWDS BACILLUS SUBTILIS, SINGLE-DOMAIN BIOTIN CARBOXYL CARRIER PROTEIN, KEYWDS 2 SOLUTION STRUCTURE, BIOSYNTHETIC PROTEIN EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR G.CUI,B.XIA,C.JIN REVDAT 3 09-MAR-22 2B8F 1 REMARK REVDAT 2 24-FEB-09 2B8F 1 VERSN REVDAT 1 06-JUN-06 2B8F 0 JRNL AUTH G.CUI,B.XIA,C.JIN JRNL TITL SOLUTION STRUCTURE OF BACILLUS SUBTILIS BLAP APO FORM JRNL TITL 2 (ENERGY MINIMIZED MEAN STRUCTURE) JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.5, AMBER 7.0 REMARK 3 AUTHORS : BRUKER (XWINNMR), DAVID CASE (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 4125 RESTRAINTS. 3731 ARE REMARK 3 NOE-DERIVED REMARK 3 DISTANCE CONSTRAINTS, 109 DIHEDRAL ANGLE RESTRAINTS,28 DISTANCE REMARK 3 RESTRAINTS FROM HYDROGEN BONDS, 257 CHARITY RESTRAINTS REMARK 4 REMARK 4 2B8F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-OCT-05. REMARK 100 THE DEPOSITION ID IS D_1000034804. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 150 MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.2MM S-BCCP, U-15N, 13C; 50MM REMARK 210 PHOSPHATE BUFFER NA; 90% H2O, 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 2.1, NMRVIEW 5, CYANA REMARK 210 1.0.6 REMARK 210 METHOD USED : SMULATED ANNEALING MOLECULAR REMARK 210 DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL 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 VAL A 28 -31.15 -138.69 REMARK 500 ASN A 70 12.78 -151.19 REMARK 500 SER A 71 42.68 -77.38 REMARK 500 THR A 72 28.24 82.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS REMARK 500 REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES. REMARK 500 MODEL OMEGA REMARK 500 THR A 72 GLN A 73 64.81 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 44 0.09 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2B8G RELATED DB: PDB REMARK 900 BACILLUS SUBTILIS BLAP BIOTINYLATED-FORM DBREF 2B8F A 2 73 UNP Q9R9I3 Q9R9I3_BACSU 2 73 SEQRES 1 A 72 THR VAL SER ILE GLN MET ALA GLY ASN LEU TRP LYS VAL SEQRES 2 A 72 HIS VAL LYS ALA GLY ASP GLN ILE GLU LYS GLY GLN GLU SEQRES 3 A 72 VAL ALA ILE LEU GLU SER MET LYS MET GLU ILE PRO ILE SEQRES 4 A 72 VAL ALA ASP ARG SER GLY ILE VAL LYS GLU VAL LYS LYS SEQRES 5 A 72 LYS GLU GLY ASP PHE VAL ASN GLU GLY ASP VAL LEU LEU SEQRES 6 A 72 GLU LEU SER ASN SER THR GLN SHEET 1 A 4 VAL A 3 SER A 4 0 SHEET 2 A 4 VAL A 64 LEU A 68 -1 O LEU A 65 N VAL A 3 SHEET 3 A 4 GLY A 46 VAL A 51 -1 N GLU A 50 O GLU A 67 SHEET 4 A 4 GLN A 21 ILE A 22 -1 N ILE A 22 O GLY A 46 SHEET 1 B 4 MET A 36 VAL A 41 0 SHEET 2 B 4 GLU A 27 SER A 33 -1 N LEU A 31 O ILE A 38 SHEET 3 B 4 GLY A 9 VAL A 14 -1 N ASN A 10 O GLU A 32 SHEET 4 B 4 PHE A 58 VAL A 59 -1 O VAL A 59 N GLY A 9 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 - 9 20 Bytes