HEADER TRANSFERASE 12-AUG-07 2JU2
TITLE MINIMIZED MEAN SOLUTION STRUCTURE OF THE ACYL CARRIER PROTEIN DOMAIN
TITLE 2 FROM MODULE 2 OF 6-DEOXYERYTHRONOLIDE B SYNTHASE (DEBS)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ERYTHRONOLIDE SYNTHASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ACYL CARRIER PROTEIN DOMAIN;
COMPND 5 SYNONYM: ORF 1, 6-DEOXYERYTHRONOLIDE B SYNTHASE I, DEBS 1;
COMPND 6 EC: 2.3.1.94;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROPOLYSPORA ERYTHRAEA;
SOURCE 3 ORGANISM_TAXID: 1836;
SOURCE 4 GENE: ERYA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28(A);
SOURCE 10 OTHER_DETAILS: STOP CODON AT THE C-TERMINUS, BEFORE THE C-TERMINAL
SOURCE 11 HIS-TAG PRESENT IN THE EXPRESSION VECTOR PLASMID
KEYWDS CARRIER PROTEIN DOMAIN, MODULAR POLYKETIDE SYNTHASE, ALPHA-HELICAL
KEYWDS 2 BUNDLE, ACYLTRANSFERASE, ANTIBIOTIC BIOSYNTHESIS, MULTIFUNCTIONAL
KEYWDS 3 ENZYME, NADP, PHOSPHOPANTETHEINE, TRANSFERASE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR V.Y.ALEKSEYEV,C.W.LIU,J.D.PUGLISI,C.KHOSLA
REVDAT 3 16-MAR-22 2JU2 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2JU2 1 VERSN
REVDAT 1 02-OCT-07 2JU2 0
JRNL AUTH V.Y.ALEKSEYEV,C.W.LIU,D.E.CANE,J.D.PUGLISI,C.KHOSLA
JRNL TITL SOLUTION STRUCTURE AND PROPOSED DOMAIN DOMAIN RECOGNITION
JRNL TITL 2 INTERFACE OF AN ACYL CARRIER PROTEIN DOMAIN FROM A MODULAR
JRNL TITL 3 POLYKETIDE SYNTHASE.
JRNL REF PROTEIN SCI. V. 16 2093 2007
JRNL REFN ISSN 0961-8368
JRNL PMID 17893358
JRNL DOI 10.1110/PS.073011407
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5
REMARK 3 AUTHORS : GUNTERT, P. ET AL. (DYANA), GUNTERT, P. ET AL.
REMARK 3 (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STANDARD SIMULATED ANNEALING
REMARK 3 PROTOCOL INCLUDED AS PART OF DYANA SOFTWARE WAS USED TO
REMARK 3 CALCULATE A TOTAL OF 50 STRUCTURES, OF WHICH 30 STRUCTURES WITH
REMARK 3 THE LOWEST TARGET FUNCTION VALUES WERE CHOSEN FOR THE SOLUTION
REMARK 3 STRUCTURE ENSEMBLE. THE HELICAL REGIONS OF THESE 30 STRUCTURES
REMARK 3 WERE SUPERIMPOSED AND THE MEAN STRUCTURE WAS OBTAINED USING
REMARK 3 MOLMOL SOFTWARE, THEN SUBJECTED TO THE STANDARD VARIABLE TARGET
REMARK 3 FUNCTION MINIMIZATION IMPLEMENTED IN DYANA. THE RESULTING
REMARK 3 MINIMIZED MEAN STRUCTURE IS DEPOSITED HERE. THE ENSEMBLE OF 30
REMARK 3 STRUCTURES IS DEPOSITED IN THE PDB ENTRY 2JU1.
REMARK 4
REMARK 4 2JU2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000100290.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : 30
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8-1 MM [U-13C; U-15N] ACYL
REMARK 210 CARRIER PROTEIN, 0.05 % SODIUM
REMARK 210 AZIDE, 30 MM SODIUM PHOSPHATE,
REMARK 210 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D 1H-15N NOESY; 3D 1H-13C/15N
REMARK 210 NOESY; 3D HCCH-TOCSY; 3D HNHA;
REMARK 210 2D 1H-15N HSQC; 3D HNCACB; 3D
REMARK 210 C(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 LEU A 60 H LEU A 64 1.52
REMARK 500 O ARG A 14 H THR A 18 1.53
REMARK 500 O LEU A 24 H SER A 28 1.53
REMARK 500 O THR A 27 H THR A 31 1.53
REMARK 500 O THR A 75 H ASP A 79 1.54
REMARK 500 O ALA A 43 H SER A 84 1.56
REMARK 500 O LEU A 76 H HIS A 80 1.56
REMARK 500 O GLY A 88 H ALA A 92 1.57
REMARK 500 O LEU A 5 H LEU A 9 1.59
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 HIS A 3 -65.32 71.74
REMARK 500 MET A 4 38.75 -88.41
REMARK 500 ALA A 10 34.68 -85.40
REMARK 500 LEU A 12 86.21 30.60
REMARK 500 ALA A 15 -70.26 -42.35
REMARK 500 ASP A 36 55.10 -114.92
REMARK 500 ALA A 40 41.13 -93.13
REMARK 500 ASP A 53 -60.86 -137.64
REMARK 500 SER A 54 -61.48 -144.72
REMARK 500 LEU A 60 -76.25 -55.26
REMARK 500 THR A 68 -73.31 -112.55
REMARK 500 LEU A 72 160.59 -44.83
REMARK 500 SER A 84 -39.69 -36.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2JU1 RELATED DB: PDB
REMARK 900 ENSEMBLE OF 30 STRUCTURES OF THE ACYL CARRIER PROTEIN DOMAIN FROM
REMARK 900 MODULE 2 OF THE 6-DEOXYERYTHRONOLIDE B SYNTHASE (DEBS)
DBREF 2JU2 A 5 95 UNP Q03131 ERYA1_SACER 3318 3408
SEQADV 2JU2 GLY A 1 UNP Q03131 EXPRESSION TAG
SEQADV 2JU2 SER A 2 UNP Q03131 EXPRESSION TAG
SEQADV 2JU2 HIS A 3 UNP Q03131 EXPRESSION TAG
SEQADV 2JU2 MET A 4 UNP Q03131 EXPRESSION TAG
SEQRES 1 A 95 GLY SER HIS MET LEU ARG ASP ARG LEU ALA GLY LEU PRO
SEQRES 2 A 95 ARG ALA GLU ARG THR ALA GLU LEU VAL ARG LEU VAL ARG
SEQRES 3 A 95 THR SER THR ALA THR VAL LEU GLY HIS ASP ASP PRO LYS
SEQRES 4 A 95 ALA VAL ARG ALA THR THR PRO PHE LYS GLU LEU GLY PHE
SEQRES 5 A 95 ASP SER LEU ALA ALA VAL ARG LEU ARG ASN LEU LEU ASN
SEQRES 6 A 95 ALA ALA THR GLY LEU ARG LEU PRO SER THR LEU VAL PHE
SEQRES 7 A 95 ASP HIS PRO ASN ALA SER ALA VAL ALA GLY PHE LEU ASP
SEQRES 8 A 95 ALA GLU LEU GLY
HELIX 1 1 MET A 4 ALA A 10 1 7
HELIX 2 2 PRO A 13 GLY A 34 1 22
HELIX 3 3 ASP A 37 VAL A 41 5 5
HELIX 4 4 PRO A 46 PHE A 52 1 7
HELIX 5 5 SER A 54 GLY A 69 1 16
HELIX 6 6 THR A 75 HIS A 80 1 6
HELIX 7 7 ASN A 82 GLY A 95 1 14
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
(ATOM LINES ARE NOT SHOWN.)
END
