Header list of 2b8g.pdb file
Complete list - 9 20 Bytes
HEADER BIOSYNTHETIC PROTEIN 06-OCT-05 2B8G
TITLE SOLUTION STRUCTURE OF BACILLUS SUBTILIS BLAP BIOTINYLATED-FORM (ENERGY
TITLE 2 MINIMIZED MEAN STRUCTURE)
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 2B8G 1 REMARK LINK
REVDAT 2 24-FEB-09 2B8G 1 VERSN
REVDAT 1 06-JUN-06 2B8G 0
JRNL AUTH G.CUI,B.XIA,C.JIN
JRNL TITL SOLUTION STRUCTURE OF BACILLUS SUBTILIS BLAP
JRNL TITL 2 BIOTINYLATED-FORM (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 4560 RESTRAINTS. 4160 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 117 DIHEDRAL ANGLE RESTRAINTS,30 DISTANCE
REMARK 3 RESTRAINTS FROM HYDROGEN BONDS, 253 CHARITY RESTRAINTS
REMARK 4
REMARK 4 2B8G 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_1000034805.
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; 2D 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: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERNUCLEAR TECHNIQUES
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 35 7.86 88.68
REMARK 500 LEU A 65 -44.09 -133.35
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 LEU A 31 GLU A 32 135.22
REMARK 500 THR A 72 GLN A 73 124.85
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 0.13 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BTN A 135
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2B8F RELATED DB: PDB
REMARK 900 BACILLUS SUBTILIS BLAP APO FORM
DBREF 2B8G 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
HET BTN A 135 30
HETNAM BTN BIOTIN
FORMUL 2 BTN C10 H16 N2 O3 S
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 66 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 VAL A 28 O ILE A 40
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
LINK NZ LYS A 35 C11 BTN A 135 1555 1555 1.34
SITE 1 AC1 2 TRP A 12 LYS A 35
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