HEADER TRANSCRIPTION 11-FEB-11 3QP6
TITLE CRYSTAL STRUCTURE OF CVIR (CHROMOBACTERIUM VIOLACEUM 12472) BOUND TO
TITLE 2 C6-HSL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CVIR TRANSCRIPTIONAL REGULATOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TRANSCRIPTIONAL ACTIVATOR, LUXR/UHPA FAMILY OF REGULATORS;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CHROMOBACTERIUM VIOLACEUM;
SOURCE 3 ORGANISM_TAXID: 536;
SOURCE 4 STRAIN: 12472;
SOURCE 5 GENE: CVIR;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET23B
KEYWDS QUORUM SENSING, AGONIST, ANTAGONIST, LUXR, ACYLATED HOMOSERINE
KEYWDS 2 LACTONE, TRANSCRIPTION FACTOR, DNA BINDING PROTEIN, LIGAND BINDING
KEYWDS 3 DOMAIN, SIGNAL RECEPTOR, N-HEXANOYL-L-HOMOSERINE LACTONE,
KEYWDS 4 TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.CHEN,L.SWEM,D.SWEM,D.STAUFF,C.O'LOUGHLIN,P.JEFFREY,B.BASSLER,
AUTHOR 2 F.HUGHSON
REVDAT 4 13-SEP-23 3QP6 1 REMARK
REVDAT 3 17-JUL-19 3QP6 1 REMARK
REVDAT 2 04-MAY-11 3QP6 1 JRNL
REVDAT 1 30-MAR-11 3QP6 0
JRNL AUTH G.CHEN,L.R.SWEM,D.L.SWEM,D.L.STAUFF,C.T.O'LOUGHLIN,
JRNL AUTH 2 P.D.JEFFREY,B.L.BASSLER,F.M.HUGHSON
JRNL TITL A STRATEGY FOR ANTAGONIZING QUORUM SENSING.
JRNL REF MOL.CELL V. 42 199 2011
JRNL REFN ISSN 1097-2765
JRNL PMID 21504831
JRNL DOI 10.1016/J.MOLCEL.2011.04.003
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.5_2
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.54
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 20466
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.183
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 1048
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 26.5380 - 3.8215 1.00 2913 149 0.1706 0.1983
REMARK 3 2 3.8215 - 3.0346 1.00 2796 148 0.1791 0.2264
REMARK 3 3 3.0346 - 2.6514 1.00 2769 150 0.1960 0.2180
REMARK 3 4 2.6514 - 2.4092 1.00 2755 147 0.1843 0.2398
REMARK 3 5 2.4092 - 2.2366 1.00 2738 150 0.1850 0.2310
REMARK 3 6 2.2366 - 2.1048 1.00 2736 155 0.1799 0.2398
REMARK 3 7 2.1048 - 1.9994 1.00 2711 149 0.1932 0.2689
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.32
REMARK 3 B_SOL : 27.12
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.800
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) : 1.75470
REMARK 3 B22 (A**2) : -4.73730
REMARK 3 B33 (A**2) : 2.98260
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 2085
REMARK 3 ANGLE : 1.061 2826
REMARK 3 CHIRALITY : 0.069 311
REMARK 3 PLANARITY : 0.004 371
REMARK 3 DIHEDRAL : 17.635 777
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QP6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063927.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 298
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0401
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20522
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1270
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.20
REMARK 200 R MERGE FOR SHELL (I) : 0.31900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.656
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3QP7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.04
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM IMIDAZOLE, 10% W/V PEG5000 MME,
REMARK 280 PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 296K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
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 66.06250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 66.06250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 25.12400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 44.56000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 25.12400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 44.56000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 66.06250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 25.12400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 44.56000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 66.06250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 25.12400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 44.56000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
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
REMARK 350 TOTAL BURIED SURFACE AREA: 6570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 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 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 66.06250
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 276 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 278 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 282 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 286 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 VAL A 2
REMARK 465 THR A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 PRO A 6
REMARK 465 GLY A 265
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 OE1 GLN A 106 O HOH A 271 2.12
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 PRO A 52 1.01 -67.31
REMARK 500 SER A 79 23.92 -150.01
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 HL6 A 266
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3QP1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CVIR LIGAND-BINDING DOMAIN BOUND TO C6-HSL
REMARK 900 RELATED ID: 3QP2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CVIR LIGAND-BINDING DOMAIN BOUND TO C8-HSL
REMARK 900 RELATED ID: 3QP4 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CVIR LIGAND-BINDING DOMAIN BOUND TO C10-HSL
REMARK 900 RELATED ID: 3QP5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CVIR BOUND TO ANTAGONIST CHLOROLACTONE (CL)
REMARK 900 RELATED ID: 3QP7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF SEMET CVIR (CHROMOBACTERIUM VIOLACEUM 12472)
REMARK 900 BOUND TO C6-HSL
REMARK 900 RELATED ID: 3QP8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF CVIR (CHROMOBACTERIUM VIOLACEUM 12472) BOUND
REMARK 900 TO C10-HSL
DBREF 3QP6 A 1 265 UNP Q7NQP7 Q7NQP7_CHRVO 1 265
SEQRES 1 A 265 MET VAL THR SER LYS PRO ILE ASN ALA ARG PRO LEU PRO
SEQRES 2 A 265 ALA GLY LEU THR ALA SER GLN GLN TRP THR LEU LEU GLU
SEQRES 3 A 265 TRP ILE HIS MET ALA GLY HIS ILE GLU THR GLU GLY GLU
SEQRES 4 A 265 LEU LYS ALA PHE LEU ASP ASN ILE LEU SER GLN ALA PRO
SEQRES 5 A 265 SER ASP ARG ILE ILE LEU VAL LEU GLY ARG LEU ASN ASN
SEQRES 6 A 265 GLN ASN GLN ILE GLN ARG MET GLU LYS VAL LEU ASN VAL
SEQRES 7 A 265 SER TYR PRO SER ASP TRP LEU ASN GLN TYR SER GLN GLU
SEQRES 8 A 265 ASN PHE ALA GLN HIS ASP PRO ILE MET ARG ILE HIS LEU
SEQRES 9 A 265 GLY GLN GLY PRO VAL ILE TRP GLU GLU ARG PHE SER ARG
SEQRES 10 A 265 ALA LYS GLY SER GLU GLU LYS ARG PHE ILE ALA GLU ALA
SEQRES 11 A 265 SER SER ASN GLY MET GLY SER GLY ILE THR PHE SER ALA
SEQRES 12 A 265 ALA SER ASP ARG ASN ASN VAL GLY SER ILE LEU SER ILE
SEQRES 13 A 265 GLY GLY LYS GLU PRO GLY ARG ASN ALA ALA LEU VAL ALA
SEQRES 14 A 265 MET LEU ASN CYS LEU THR PRO HIS LEU HIS GLN ALA ALA
SEQRES 15 A 265 VAL ARG ILE ALA ASN LEU PRO PRO ALA SER PRO SER ASN
SEQRES 16 A 265 MET PRO LEU SER GLN ARG GLU TYR ASP ILE PHE HIS TRP
SEQRES 17 A 265 MET SER ARG GLY LYS THR ASN TRP GLU ILE ALA THR ILE
SEQRES 18 A 265 LEU ASN ILE SER GLU ARG THR VAL LYS PHE HIS VAL ALA
SEQRES 19 A 265 ASN VAL ILE ARG LYS LEU ASN ALA ASN ASN ARG THR HIS
SEQRES 20 A 265 ALA ILE VAL LEU GLY MET HIS LEU ALA MET THR PRO ARG
SEQRES 21 A 265 GLU LEU VAL ASN GLY
HET HL6 A 266 14
HETNAM HL6 N-[(3S)-2-OXOTETRAHYDROFURAN-3-YL]HEXANAMIDE
HETSYN HL6 N-HEXANOYL-L-HOMOSERINE LACTONE
FORMUL 2 HL6 C10 H17 N O3
FORMUL 3 HOH *241(H2 O)
HELIX 1 1 THR A 17 GLY A 32 1 16
HELIX 2 2 THR A 36 LEU A 48 1 13
HELIX 3 3 PRO A 81 GLU A 91 1 11
HELIX 4 4 ASN A 92 HIS A 96 5 5
HELIX 5 5 ASP A 97 ILE A 102 5 6
HELIX 6 6 TRP A 111 SER A 116 1 6
HELIX 7 7 GLY A 120 ASN A 133 1 14
HELIX 8 8 ASN A 164 ASN A 187 1 24
HELIX 9 9 SER A 199 ARG A 211 1 13
HELIX 10 10 THR A 214 ASN A 223 1 10
HELIX 11 11 SER A 225 LEU A 240 1 16
HELIX 12 12 ASN A 244 GLY A 252 1 9
HELIX 13 13 GLY A 252 THR A 258 1 7
SHEET 1 A 5 ILE A 69 ASN A 77 0
SHEET 2 A 5 ARG A 55 LEU A 63 -1 N LEU A 60 O GLU A 73
SHEET 3 A 5 VAL A 150 GLY A 157 -1 O GLY A 157 N ARG A 55
SHEET 4 A 5 GLY A 138 ALA A 144 -1 N PHE A 141 O LEU A 154
SHEET 5 A 5 VAL A 109 ILE A 110 -1 N VAL A 109 O THR A 140
CISPEP 1 GLN A 50 ALA A 51 0 2.19
SITE 1 AC1 9 TYR A 80 TRP A 84 ASP A 97 ILE A 99
SITE 2 AC1 9 TRP A 111 PHE A 126 MET A 135 ILE A 153
SITE 3 AC1 9 SER A 155
CRYST1 50.248 89.120 132.125 90.00 90.00 90.00 C 2 2 21 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 0.019901 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011221 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007569 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
