HEADER TRANSFERASE 07-DEC-00 1HNH
TITLE CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III + DEGRADED FORM OF
TITLE 2 ACETYL-COA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE III, BETA-
COMPND 5 KETOACYL-ACP SYNTHASE III;
COMPND 6 EC: 2.3.1.41;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FABH, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.QIU,C.A.JANSON,W.W.SMITH,M.HEAD,J.LONSDALE,A.K.KONSTANTINIDIS
REVDAT 4 13-JUL-11 1HNH 1 VERSN
REVDAT 3 24-FEB-09 1HNH 1 VERSN
REVDAT 2 21-MAR-01 1HNH 1 JRNL
REVDAT 1 27-DEC-00 1HNH 0
JRNL AUTH X.QIU,C.A.JANSON,W.W.SMITH,M.HEAD,J.LONSDALE,
JRNL AUTH 2 A.K.KONSTANTINIDIS
JRNL TITL REFINED STRUCTURES OF BETA-KETOACYL-ACYL CARRIER PROTEIN
JRNL TITL 2 SYNTHASE III.
JRNL REF J.MOL.BIOL. V. 307 341 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11243824
JRNL DOI 10.1006/JMBI.2000.4457
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH X.QIU,C.A.JANSON,A.K.KONSTANTINIDIS,S.NWAGWU,C.SILVERMAN,
REMARK 1 AUTH 2 W.W.SMITH,S.K.KHANDEKAR,J.LONSDALE,S.S.ABDEL-MEGUID
REMARK 1 TITL CRYSTAL STRUCTURE OF BETA-KETOACYL-ACYL CARRIER PROTEIN
REMARK 1 TITL 2 SYNTHASE III. A KEY CONDENSING ENZYME IN BACTERIAL FATTY
REMARK 1 TITL 3 ACID BIOSYNTHESIS
REMARK 1 REF J.BIOL.CHEM. V. 274 36465 1999
REMARK 1 REFN ISSN 0021-9258
REMARK 1 DOI 10.1074/JBC.274.51.36465
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 33450
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : 5%
REMARK 3 R VALUE (WORKING SET) : 0.221
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1600
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2334
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 236
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.013
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE ACETYL-COA WAS DEGRADED TO
REMARK 3 COA. CYSTEINE 112 IS ACETYLATED AND IS LABELLED AS SCY.
REMARK 4
REMARK 4 1HNH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-DEC-00.
REMARK 100 THE RCSB ID CODE IS RCSB012464.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-APR-99
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : CUSTOM-MADE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 203786
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.0
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEK4000, PH 7, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.40000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 36.22500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 36.22500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 25.70000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 36.22500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 36.22500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 77.10000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 36.22500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.22500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 25.70000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 36.22500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.22500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 77.10000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 51.40000
REMARK 290
REMARK 290 REMARK: NULL
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4700 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
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 350 BIOMT1 2 0.000000 -1.000000 0.000000 72.45000
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 72.45000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 51.40000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 627 LIES ON A SPECIAL POSITION.
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 VAL A 197 CG1 CG2
REMARK 470 LYS A 214 CG CD CE NZ
REMARK 470 ARG A 249 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 257 CG CD CE NZ
REMARK 470 LYS A 294 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 HOH A 444 O HOH A 569 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 628 O HOH A 628 8665 2.07
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 LEU A 75 140.88 -170.84
REMARK 500 SER A 82 35.09 -148.17
REMARK 500 ALA A 110 31.80 -150.42
REMARK 500 ALA A 111 -124.41 44.12
REMARK 500 VAL A 141 57.98 -119.03
REMARK 500 PRO A 148 -0.95 -58.99
REMARK 500 PRO A 199 -8.68 -57.11
REMARK 500 ALA A 246 -66.05 -103.11
REMARK 500 SER A 276 -125.80 55.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 521 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH A 588 DISTANCE = 5.58 ANGSTROMS
REMARK 525 HOH A 603 DISTANCE = 6.00 ANGSTROMS
REMARK 525 HOH A 606 DISTANCE = 5.12 ANGSTROMS
REMARK 525 HOH A 610 DISTANCE = 5.64 ANGSTROMS
REMARK 525 HOH A 623 DISTANCE = 5.15 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE COA A 350
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HN9 RELATED DB: PDB
REMARK 900 BETA-KETOACYL-ACP SYNTHASE III
REMARK 900 RELATED ID: 1HND RELATED DB: PDB
REMARK 900 BETA-KETOACYL-ACP SYNTHASE III + COA
REMARK 900 RELATED ID: 1HNJ RELATED DB: PDB
REMARK 900 BETA-KETOACYL-ACP SYNTHASE III + MALONYL-COA
REMARK 900 RELATED ID: 1HNK RELATED DB: PDB
REMARK 900 BETA-KETOACYL-ACP SYNTHASE III IN APO TETRAGONAL FORM
DBREF 1HNH A 1 317 UNP P0A6R0 FABH_ECOLI 1 317
SEQADV 1HNH MSE A 1 UNP P0A6R0 MET 1 MODIFIED RESIDUE
SEQADV 1HNH MSE A 25 UNP P0A6R0 MET 25 MODIFIED RESIDUE
SEQADV 1HNH MSE A 54 UNP P0A6R0 MET 54 MODIFIED RESIDUE
SEQADV 1HNH MSE A 65 UNP P0A6R0 MET 65 MODIFIED RESIDUE
SEQADV 1HNH MSE A 97 UNP P0A6R0 MET 97 MODIFIED RESIDUE
SEQADV 1HNH SCY A 112 UNP P0A6R0 CYS 112 MODIFIED RESIDUE
SEQADV 1HNH MSE A 207 UNP P0A6R0 MET 207 MODIFIED RESIDUE
SEQADV 1HNH MSE A 260 UNP P0A6R0 MET 260 MODIFIED RESIDUE
SEQADV 1HNH MSE A 262 UNP P0A6R0 MET 262 MODIFIED RESIDUE
SEQRES 1 A 317 MSE TYR THR LYS ILE ILE GLY THR GLY SER TYR LEU PRO
SEQRES 2 A 317 GLU GLN VAL ARG THR ASN ALA ASP LEU GLU LYS MSE VAL
SEQRES 3 A 317 ASP THR SER ASP GLU TRP ILE VAL THR ARG THR GLY ILE
SEQRES 4 A 317 ARG GLU ARG HIS ILE ALA ALA PRO ASN GLU THR VAL SER
SEQRES 5 A 317 THR MSE GLY PHE GLU ALA ALA THR ARG ALA ILE GLU MSE
SEQRES 6 A 317 ALA GLY ILE GLU LYS ASP GLN ILE GLY LEU ILE VAL VAL
SEQRES 7 A 317 ALA THR THR SER ALA THR HIS ALA PHE PRO SER ALA ALA
SEQRES 8 A 317 CYS GLN ILE GLN SER MSE LEU GLY ILE LYS GLY CYS PRO
SEQRES 9 A 317 ALA PHE ASP VAL ALA ALA ALA SCY ALA GLY PHE THR TYR
SEQRES 10 A 317 ALA LEU SER VAL ALA ASP GLN TYR VAL LYS SER GLY ALA
SEQRES 11 A 317 VAL LYS TYR ALA LEU VAL VAL GLY SER ASP VAL LEU ALA
SEQRES 12 A 317 ARG THR CYS ASP PRO THR ASP ARG GLY THR ILE ILE ILE
SEQRES 13 A 317 PHE GLY ASP GLY ALA GLY ALA ALA VAL LEU ALA ALA SER
SEQRES 14 A 317 GLU GLU PRO GLY ILE ILE SER THR HIS LEU HIS ALA ASP
SEQRES 15 A 317 GLY SER TYR GLY GLU LEU LEU THR LEU PRO ASN ALA ASP
SEQRES 16 A 317 ARG VAL ASN PRO GLU ASN SER ILE HIS LEU THR MSE ALA
SEQRES 17 A 317 GLY ASN GLU VAL PHE LYS VAL ALA VAL THR GLU LEU ALA
SEQRES 18 A 317 HIS ILE VAL ASP GLU THR LEU ALA ALA ASN ASN LEU ASP
SEQRES 19 A 317 ARG SER GLN LEU ASP TRP LEU VAL PRO HIS GLN ALA ASN
SEQRES 20 A 317 LEU ARG ILE ILE SER ALA THR ALA LYS LYS LEU GLY MSE
SEQRES 21 A 317 SER MSE ASP ASN VAL VAL VAL THR LEU ASP ARG HIS GLY
SEQRES 22 A 317 ASN THR SER ALA ALA SER VAL PRO CYS ALA LEU ASP GLU
SEQRES 23 A 317 ALA VAL ARG ASP GLY ARG ILE LYS PRO GLY GLN LEU VAL
SEQRES 24 A 317 LEU LEU GLU ALA PHE GLY GLY GLY PHE THR TRP GLY SER
SEQRES 25 A 317 ALA LEU VAL ARG PHE
MODRES 1HNH MSE A 1 MET SELENOMETHIONINE
MODRES 1HNH MSE A 25 MET SELENOMETHIONINE
MODRES 1HNH MSE A 54 MET SELENOMETHIONINE
MODRES 1HNH MSE A 65 MET SELENOMETHIONINE
MODRES 1HNH MSE A 97 MET SELENOMETHIONINE
MODRES 1HNH SCY A 112 CYS S-ACETYL-CYSTEINE
MODRES 1HNH MSE A 207 MET SELENOMETHIONINE
MODRES 1HNH MSE A 260 MET SELENOMETHIONINE
MODRES 1HNH MSE A 262 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 25 8
HET MSE A 54 8
HET MSE A 65 8
HET MSE A 97 8
HET SCY A 112 9
HET MSE A 207 8
HET MSE A 260 8
HET MSE A 262 8
HET COA A 350 48
HETNAM MSE SELENOMETHIONINE
HETNAM SCY S-ACETYL-CYSTEINE
HETNAM COA COENZYME A
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 1 SCY C5 H9 N O3 S
FORMUL 2 COA C21 H36 N7 O16 P3 S
FORMUL 3 HOH *236(H2 O)
HELIX 1 1 ASN A 19 LYS A 24 1 6
HELIX 2 2 SER A 29 GLY A 38 1 10
HELIX 3 3 THR A 50 GLY A 67 1 18
HELIX 4 4 GLU A 69 ILE A 73 5 5
HELIX 5 5 SER A 89 GLY A 99 1 11
HELIX 6 6 ALA A 113 SER A 128 1 16
HELIX 7 7 ASP A 150 ILE A 155 1 6
HELIX 8 8 GLY A 183 GLU A 187 5 5
HELIX 9 9 ALA A 208 ASN A 231 1 24
HELIX 10 10 ASP A 234 LEU A 238 5 5
HELIX 11 11 ASN A 247 GLY A 259 1 13
HELIX 12 12 SER A 261 ASN A 264 5 4
HELIX 13 13 THR A 268 GLY A 273 1 6
HELIX 14 14 THR A 275 ALA A 277 5 3
HELIX 15 15 ALA A 278 ASP A 290 1 13
SHEET 1 A 5 TYR A 2 TYR A 11 0
SHEET 2 A 5 ASP A 159 SER A 169 -1 O ALA A 161 N TYR A 11
SHEET 3 A 5 TYR A 133 VAL A 141 -1 O ALA A 134 N LEU A 166
SHEET 4 A 5 LEU A 75 ALA A 79 1 O LEU A 75 N LEU A 135
SHEET 5 A 5 ALA A 105 VAL A 108 1 O PHE A 106 N VAL A 78
SHEET 1 B 2 GLN A 15 THR A 18 0
SHEET 2 B 2 GLU A 41 ILE A 44 -1 O ARG A 42 N ARG A 17
SHEET 1 C 4 ILE A 174 ALA A 181 0
SHEET 2 C 4 THR A 309 ARG A 316 -1 O TRP A 310 N HIS A 180
SHEET 3 C 4 LEU A 298 GLY A 305 -1 O VAL A 299 N VAL A 315
SHEET 4 C 4 TRP A 240 VAL A 242 1 O TRP A 240 N LEU A 300
SHEET 1 D 2 LEU A 189 THR A 190 0
SHEET 2 D 2 THR A 206 MSE A 207 -1 N THR A 206 O THR A 190
LINK C MSE A 1 N TYR A 2 1555 1555 1.33
LINK C LYS A 24 N MSE A 25 1555 1555 1.32
LINK C MSE A 25 N VAL A 26 1555 1555 1.33
LINK C THR A 53 N MSE A 54 1555 1555 1.33
LINK C MSE A 54 N GLY A 55 1555 1555 1.34
LINK C GLU A 64 N MSE A 65 1555 1555 1.34
LINK C MSE A 65 N ALA A 66 1555 1555 1.33
LINK C SER A 96 N MSE A 97 1555 1555 1.33
LINK C MSE A 97 N LEU A 98 1555 1555 1.33
LINK C ALA A 111 N SCY A 112 1555 1555 1.33
LINK C SCY A 112 N ALA A 113 1555 1555 1.34
LINK C THR A 206 N MSE A 207 1555 1555 1.33
LINK C MSE A 207 N ALA A 208 1555 1555 1.32
LINK C GLY A 259 N MSE A 260 1555 1555 1.33
LINK C MSE A 260 N SER A 261 1555 1555 1.33
LINK C SER A 261 N MSE A 262 1555 1555 1.33
LINK C MSE A 262 N ASP A 263 1555 1555 1.34
CISPEP 1 PHE A 87 PRO A 88 0 0.82
CISPEP 2 PRO A 172 GLY A 173 0 -14.88
CISPEP 3 GLY A 307 PHE A 308 0 -11.36
SITE 1 AC1 24 THR A 28 TRP A 32 ARG A 36 THR A 37
SITE 2 AC1 24 PRO A 47 SCY A 112 ARG A 151 ILE A 155
SITE 3 AC1 24 MSE A 207 GLY A 209 ASN A 210 VAL A 212
SITE 4 AC1 24 PHE A 213 HIS A 244 ASN A 247 ASN A 274
SITE 5 AC1 24 HOH A 442 HOH A 528 HOH A 542 HOH A 543
SITE 6 AC1 24 HOH A 585 HOH A 590 HOH A 605 HOH A 634
CRYST1 72.450 72.450 102.800 90.00 90.00 90.00 P 41 21 2 8
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 0.013803 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013803 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009728 0.00000
HETATM 1 N MSE A 1 16.717 50.410 20.420 1.00 28.35 N
HETATM 2 CA MSE A 1 16.743 49.469 19.255 1.00 28.72 C
HETATM 3 C MSE A 1 16.725 48.057 19.821 1.00 27.44 C
HETATM 4 O MSE A 1 17.149 47.828 20.967 1.00 28.25 O
HETATM 5 CB MSE A 1 18.036 49.661 18.462 1.00 29.28 C
HETATM 6 CG MSE A 1 18.131 48.843 17.188 1.00 34.62 C
HETATM 7 SE MSE A 1 17.419 49.797 15.803 1.00 39.72 SE
HETATM 8 CE MSE A 1 18.585 51.145 15.765 1.00 35.77 C
(ATOM LINES ARE NOT SHOWN.)
END
