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HEADER HYDROLASE 17-FEB-23 8CLQ
TITLE ZEARALENONE LACTONASE OF STREPTOMYCES COELICOFLAVUS MUTANT H286Y IN
TITLE 2 COMPLEX WITH HYDROLYZED ZEARALENONE
CAVEAT 8CLQ ZGR A 500 HAS WRONG CHIRALITY AT ATOM C10 ZGR B 500 HAS
CAVEAT 2 8CLQ WRONG CHIRALITY AT ATOM C10 ZGR C 500 HAS WRONG CHIRALITY
CAVEAT 3 8CLQ AT ATOM C10 ZGR D 500 HAS WRONG CHIRALITY AT ATOM C10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROLASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOFLAVUS;
SOURCE 3 ORGANISM_TAXID: 285562;
SOURCE 4 GENE: SMCF_1294;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ZEARALENONE, MYCOTOXIN, LACTONASE, CARBOXYLESTERASE, ESTERASE,
KEYWDS 2 HYDROLASE, BIODEGRADATION, STREPTOMYCES COELICOFLAVUS
EXPDTA X-RAY DIFFRACTION
AUTHOR D.PUEHRINGER,G.MLYNEK
REVDAT 1 28-FEB-24 8CLQ 0
JRNL AUTH S.FRUHAUF,D.PUEHRINGER,M.THAMHESL,P.FAJTL,E.KUNZ-VEKIRO,
JRNL AUTH 2 A.HOEBARTNER-GUSSL,J.PANHOELZL,K.PREM,V.KLINGENBRUNNER,
JRNL AUTH 3 G.SCHATZMAYR,G.ADAM,J.DAMBORSKY,K.DJINOVIC-CARUGO,Z.PROKOP,
JRNL AUTH 4 W.D.MOLL
JRNL TITL BACTERIAL LACTONASES ZENA WITH NONCANONICAL STRUCTURAL
JRNL TITL 2 FEATURES HYDROLYSE THE MYCOTOXIN ZEARALENONE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.53 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.20.1-4489
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) : 1.53
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.77
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 171289
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.150
REMARK 3 FREE R VALUE TEST SET COUNT : 1970
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 46.7700 - 3.6900 1.00 12847 152 0.1579 0.1627
REMARK 3 2 3.6900 - 2.9300 1.00 12464 146 0.1488 0.1836
REMARK 3 3 2.9300 - 2.5600 1.00 12393 140 0.1622 0.1970
REMARK 3 4 2.5600 - 2.3200 1.00 12315 146 0.1714 0.2143
REMARK 3 5 2.3200 - 2.1600 1.00 12295 141 0.1832 0.2031
REMARK 3 6 2.1600 - 2.0300 1.00 12253 140 0.2034 0.2097
REMARK 3 7 2.0300 - 1.9300 1.00 12232 147 0.2278 0.2683
REMARK 3 8 1.9300 - 1.8400 1.00 12255 137 0.2712 0.2818
REMARK 3 9 1.8400 - 1.7700 1.00 12193 148 0.3073 0.3091
REMARK 3 10 1.7700 - 1.7100 1.00 12140 147 0.3311 0.3395
REMARK 3 11 1.7100 - 1.6600 1.00 12194 137 0.3565 0.3847
REMARK 3 12 1.6600 - 1.6100 0.99 11976 141 0.3757 0.3718
REMARK 3 13 1.6100 - 1.5700 0.96 11743 129 0.3953 0.3992
REMARK 3 14 1.5700 - 1.5300 0.82 10019 119 0.4095 0.4084
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.280
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.130
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 21.44
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 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 : 0.004 9863
REMARK 3 ANGLE : 0.736 13450
REMARK 3 CHIRALITY : 0.044 1403
REMARK 3 PLANARITY : 0.006 1780
REMARK 3 DIHEDRAL : 9.260 1381
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 8CLQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-FEB-23.
REMARK 100 THE DEPOSITION ID IS D_1292126825.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 174008
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.530
REMARK 200 RESOLUTION RANGE LOW (A) : 46.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.20450
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 7.0100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 4.24400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 0.370
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MG FORMATE DIHYDRATE 10.09% PEG
REMARK 280 3350 (PH 6.9), VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 32.90450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 67.41100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.93350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 67.41100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.90450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.93350
REMARK 290 SMTRY3 4 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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 39960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 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 PRO A 5
REMARK 465 ALA A 6
REMARK 465 LEU A 7
REMARK 465 ARG A 8
REMARK 465 ASP A 9
REMARK 465 GLY A 76
REMARK 465 HIS A 310
REMARK 465 HIS A 311
REMARK 465 HIS A 312
REMARK 465 HIS A 313
REMARK 465 HIS A 314
REMARK 465 HIS A 315
REMARK 465 MET B 1
REMARK 465 HIS B 311
REMARK 465 HIS B 312
REMARK 465 HIS B 313
REMARK 465 HIS B 314
REMARK 465 HIS B 315
REMARK 465 MET C 1
REMARK 465 VAL C 2
REMARK 465 ALA C 308
REMARK 465 PRO C 309
REMARK 465 HIS C 310
REMARK 465 HIS C 311
REMARK 465 HIS C 312
REMARK 465 HIS C 313
REMARK 465 HIS C 314
REMARK 465 HIS C 315
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 THR D 3
REMARK 465 SER D 4
REMARK 465 PRO D 309
REMARK 465 HIS D 310
REMARK 465 HIS D 311
REMARK 465 HIS D 312
REMARK 465 HIS D 313
REMARK 465 HIS D 314
REMARK 465 HIS D 315
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 SER A 112 -113.52 58.84
REMARK 500 PHE A 141 -47.53 75.10
REMARK 500 HIS A 242 -149.12 -94.54
REMARK 500 MET A 287 63.31 -102.23
REMARK 500 ASP B 9 74.38 -110.47
REMARK 500 THR B 48 -3.31 72.80
REMARK 500 SER B 112 -118.12 59.29
REMARK 500 PHE B 141 -46.09 70.42
REMARK 500 HIS B 242 -148.31 -93.39
REMARK 500 SER C 112 -118.29 55.52
REMARK 500 PHE C 141 -47.80 70.55
REMARK 500 HIS C 242 -148.36 -95.70
REMARK 500 MET C 287 59.17 -99.65
REMARK 500 THR D 48 -2.18 78.08
REMARK 500 SER D 112 -114.08 55.27
REMARK 500 PHE D 141 -48.13 70.34
REMARK 500 VAL D 174 -60.73 -94.70
REMARK 500 HIS D 242 -148.96 -97.21
REMARK 500 MET D 287 66.82 -100.70
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8CLQ A 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
DBREF 8CLQ B 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
DBREF 8CLQ C 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
DBREF 8CLQ D 1 309 UNP H1Q8U7 H1Q8U7_9ACTN 1 309
SEQADV 8CLQ TYR A 286 UNP H1Q8U7 HIS 286 ENGINEERED MUTATION
SEQADV 8CLQ HIS A 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS A 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS A 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS A 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS A 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS A 315 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ TYR B 286 UNP H1Q8U7 HIS 286 ENGINEERED MUTATION
SEQADV 8CLQ HIS B 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS B 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS B 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS B 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS B 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS B 315 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ TYR C 286 UNP H1Q8U7 HIS 286 ENGINEERED MUTATION
SEQADV 8CLQ HIS C 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS C 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS C 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS C 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS C 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS C 315 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ TYR D 286 UNP H1Q8U7 HIS 286 ENGINEERED MUTATION
SEQADV 8CLQ HIS D 310 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS D 311 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS D 312 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS D 313 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS D 314 UNP H1Q8U7 EXPRESSION TAG
SEQADV 8CLQ HIS D 315 UNP H1Q8U7 EXPRESSION TAG
SEQRES 1 A 315 MET VAL THR SER PRO ALA LEU ARG ASP VAL HIS VAL PRO
SEQRES 2 A 315 HIS ALA TYR PRO GLU GLN GLN VAL ASP LEU GLY GLU ILE
SEQRES 3 A 315 THR MET ASN TYR ALA GLU ALA GLY ASP PRO ASP ARG PRO
SEQRES 4 A 315 ALA VAL LEU LEU ILE PRO GLU GLN THR GLY SER TRP TRP
SEQRES 5 A 315 SER TYR GLU GLU ALA MET GLY LEU LEU SER GLU HIS PHE
SEQRES 6 A 315 HIS VAL TYR ALA VAL ASP LEU ARG GLY GLN GLY ARG SER
SEQRES 7 A 315 SER TRP THR PRO LYS ARG TYR SER LEU ASP ASN PHE GLY
SEQRES 8 A 315 ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL VAL LYS ARG
SEQRES 9 A 315 PRO VAL VAL VAL ALA GLY ASN SER SER GLY GLY VAL LEU
SEQRES 10 A 315 ALA ALA TRP LEU SER ALA TYR SER MET PRO GLY GLN LEU
SEQRES 11 A 315 ARG GLY VAL LEU CYS GLU ASP PRO PRO PHE PHE ALA SER
SEQRES 12 A 315 GLU LEU VAL PRO ALA HIS GLY HIS SER VAL ARG GLN GLY
SEQRES 13 A 315 ALA GLY PRO VAL PHE GLU LEU PHE ARG THR TYR LEU GLY
SEQRES 14 A 315 ASP GLN TRP SER VAL GLY ASP TRP GLU GLY PHE CYS ARG
SEQRES 15 A 315 ALA ALA GLY ALA SER ALA SER PRO MET ALA ARG SER PHE
SEQRES 16 A 315 VAL ALA ASP GLY ILE PRO GLN HIS LEU GLN GLU TYR ASP
SEQRES 17 A 315 PRO GLU TRP ALA ARG VAL PHE TYR GLU GLY THR VAL GLY
SEQRES 18 A 315 LEU SER CYS PRO HIS GLU ARG MET LEU GLY GLN VAL LYS
SEQRES 19 A 315 THR PRO VAL LEU LEU THR HIS HIS MET ARG GLY ILE ASP
SEQRES 20 A 315 PRO GLU THR GLY ASN LEU LEU GLY ALA LEU SER ASP GLU
SEQRES 21 A 315 GLN ALA LEU ARG ALA ARG ARG LEU MET ASP SER ALA GLY
SEQRES 22 A 315 VAL THR VAL ASP TYR GLU SER VAL PRO ASP ALA SER TYR
SEQRES 23 A 315 MET MET HIS GLN SER ALA PRO ALA ARG TYR VAL GLU ILE
SEQRES 24 A 315 PHE THR ARG TRP ALA ALA ALA LEU ALA PRO HIS HIS HIS
SEQRES 25 A 315 HIS HIS HIS
SEQRES 1 B 315 MET VAL THR SER PRO ALA LEU ARG ASP VAL HIS VAL PRO
SEQRES 2 B 315 HIS ALA TYR PRO GLU GLN GLN VAL ASP LEU GLY GLU ILE
SEQRES 3 B 315 THR MET ASN TYR ALA GLU ALA GLY ASP PRO ASP ARG PRO
SEQRES 4 B 315 ALA VAL LEU LEU ILE PRO GLU GLN THR GLY SER TRP TRP
SEQRES 5 B 315 SER TYR GLU GLU ALA MET GLY LEU LEU SER GLU HIS PHE
SEQRES 6 B 315 HIS VAL TYR ALA VAL ASP LEU ARG GLY GLN GLY ARG SER
SEQRES 7 B 315 SER TRP THR PRO LYS ARG TYR SER LEU ASP ASN PHE GLY
SEQRES 8 B 315 ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL VAL LYS ARG
SEQRES 9 B 315 PRO VAL VAL VAL ALA GLY ASN SER SER GLY GLY VAL LEU
SEQRES 10 B 315 ALA ALA TRP LEU SER ALA TYR SER MET PRO GLY GLN LEU
SEQRES 11 B 315 ARG GLY VAL LEU CYS GLU ASP PRO PRO PHE PHE ALA SER
SEQRES 12 B 315 GLU LEU VAL PRO ALA HIS GLY HIS SER VAL ARG GLN GLY
SEQRES 13 B 315 ALA GLY PRO VAL PHE GLU LEU PHE ARG THR TYR LEU GLY
SEQRES 14 B 315 ASP GLN TRP SER VAL GLY ASP TRP GLU GLY PHE CYS ARG
SEQRES 15 B 315 ALA ALA GLY ALA SER ALA SER PRO MET ALA ARG SER PHE
SEQRES 16 B 315 VAL ALA ASP GLY ILE PRO GLN HIS LEU GLN GLU TYR ASP
SEQRES 17 B 315 PRO GLU TRP ALA ARG VAL PHE TYR GLU GLY THR VAL GLY
SEQRES 18 B 315 LEU SER CYS PRO HIS GLU ARG MET LEU GLY GLN VAL LYS
SEQRES 19 B 315 THR PRO VAL LEU LEU THR HIS HIS MET ARG GLY ILE ASP
SEQRES 20 B 315 PRO GLU THR GLY ASN LEU LEU GLY ALA LEU SER ASP GLU
SEQRES 21 B 315 GLN ALA LEU ARG ALA ARG ARG LEU MET ASP SER ALA GLY
SEQRES 22 B 315 VAL THR VAL ASP TYR GLU SER VAL PRO ASP ALA SER TYR
SEQRES 23 B 315 MET MET HIS GLN SER ALA PRO ALA ARG TYR VAL GLU ILE
SEQRES 24 B 315 PHE THR ARG TRP ALA ALA ALA LEU ALA PRO HIS HIS HIS
SEQRES 25 B 315 HIS HIS HIS
SEQRES 1 C 315 MET VAL THR SER PRO ALA LEU ARG ASP VAL HIS VAL PRO
SEQRES 2 C 315 HIS ALA TYR PRO GLU GLN GLN VAL ASP LEU GLY GLU ILE
SEQRES 3 C 315 THR MET ASN TYR ALA GLU ALA GLY ASP PRO ASP ARG PRO
SEQRES 4 C 315 ALA VAL LEU LEU ILE PRO GLU GLN THR GLY SER TRP TRP
SEQRES 5 C 315 SER TYR GLU GLU ALA MET GLY LEU LEU SER GLU HIS PHE
SEQRES 6 C 315 HIS VAL TYR ALA VAL ASP LEU ARG GLY GLN GLY ARG SER
SEQRES 7 C 315 SER TRP THR PRO LYS ARG TYR SER LEU ASP ASN PHE GLY
SEQRES 8 C 315 ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL VAL LYS ARG
SEQRES 9 C 315 PRO VAL VAL VAL ALA GLY ASN SER SER GLY GLY VAL LEU
SEQRES 10 C 315 ALA ALA TRP LEU SER ALA TYR SER MET PRO GLY GLN LEU
SEQRES 11 C 315 ARG GLY VAL LEU CYS GLU ASP PRO PRO PHE PHE ALA SER
SEQRES 12 C 315 GLU LEU VAL PRO ALA HIS GLY HIS SER VAL ARG GLN GLY
SEQRES 13 C 315 ALA GLY PRO VAL PHE GLU LEU PHE ARG THR TYR LEU GLY
SEQRES 14 C 315 ASP GLN TRP SER VAL GLY ASP TRP GLU GLY PHE CYS ARG
SEQRES 15 C 315 ALA ALA GLY ALA SER ALA SER PRO MET ALA ARG SER PHE
SEQRES 16 C 315 VAL ALA ASP GLY ILE PRO GLN HIS LEU GLN GLU TYR ASP
SEQRES 17 C 315 PRO GLU TRP ALA ARG VAL PHE TYR GLU GLY THR VAL GLY
SEQRES 18 C 315 LEU SER CYS PRO HIS GLU ARG MET LEU GLY GLN VAL LYS
SEQRES 19 C 315 THR PRO VAL LEU LEU THR HIS HIS MET ARG GLY ILE ASP
SEQRES 20 C 315 PRO GLU THR GLY ASN LEU LEU GLY ALA LEU SER ASP GLU
SEQRES 21 C 315 GLN ALA LEU ARG ALA ARG ARG LEU MET ASP SER ALA GLY
SEQRES 22 C 315 VAL THR VAL ASP TYR GLU SER VAL PRO ASP ALA SER TYR
SEQRES 23 C 315 MET MET HIS GLN SER ALA PRO ALA ARG TYR VAL GLU ILE
SEQRES 24 C 315 PHE THR ARG TRP ALA ALA ALA LEU ALA PRO HIS HIS HIS
SEQRES 25 C 315 HIS HIS HIS
SEQRES 1 D 315 MET VAL THR SER PRO ALA LEU ARG ASP VAL HIS VAL PRO
SEQRES 2 D 315 HIS ALA TYR PRO GLU GLN GLN VAL ASP LEU GLY GLU ILE
SEQRES 3 D 315 THR MET ASN TYR ALA GLU ALA GLY ASP PRO ASP ARG PRO
SEQRES 4 D 315 ALA VAL LEU LEU ILE PRO GLU GLN THR GLY SER TRP TRP
SEQRES 5 D 315 SER TYR GLU GLU ALA MET GLY LEU LEU SER GLU HIS PHE
SEQRES 6 D 315 HIS VAL TYR ALA VAL ASP LEU ARG GLY GLN GLY ARG SER
SEQRES 7 D 315 SER TRP THR PRO LYS ARG TYR SER LEU ASP ASN PHE GLY
SEQRES 8 D 315 ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL VAL LYS ARG
SEQRES 9 D 315 PRO VAL VAL VAL ALA GLY ASN SER SER GLY GLY VAL LEU
SEQRES 10 D 315 ALA ALA TRP LEU SER ALA TYR SER MET PRO GLY GLN LEU
SEQRES 11 D 315 ARG GLY VAL LEU CYS GLU ASP PRO PRO PHE PHE ALA SER
SEQRES 12 D 315 GLU LEU VAL PRO ALA HIS GLY HIS SER VAL ARG GLN GLY
SEQRES 13 D 315 ALA GLY PRO VAL PHE GLU LEU PHE ARG THR TYR LEU GLY
SEQRES 14 D 315 ASP GLN TRP SER VAL GLY ASP TRP GLU GLY PHE CYS ARG
SEQRES 15 D 315 ALA ALA GLY ALA SER ALA SER PRO MET ALA ARG SER PHE
SEQRES 16 D 315 VAL ALA ASP GLY ILE PRO GLN HIS LEU GLN GLU TYR ASP
SEQRES 17 D 315 PRO GLU TRP ALA ARG VAL PHE TYR GLU GLY THR VAL GLY
SEQRES 18 D 315 LEU SER CYS PRO HIS GLU ARG MET LEU GLY GLN VAL LYS
SEQRES 19 D 315 THR PRO VAL LEU LEU THR HIS HIS MET ARG GLY ILE ASP
SEQRES 20 D 315 PRO GLU THR GLY ASN LEU LEU GLY ALA LEU SER ASP GLU
SEQRES 21 D 315 GLN ALA LEU ARG ALA ARG ARG LEU MET ASP SER ALA GLY
SEQRES 22 D 315 VAL THR VAL ASP TYR GLU SER VAL PRO ASP ALA SER TYR
SEQRES 23 D 315 MET MET HIS GLN SER ALA PRO ALA ARG TYR VAL GLU ILE
SEQRES 24 D 315 PHE THR ARG TRP ALA ALA ALA LEU ALA PRO HIS HIS HIS
SEQRES 25 D 315 HIS HIS HIS
HET ZGR A 500 47
HET ZGR B 500 47
HET ZGR C 500 47
HET ZGR D 500 47
HETNAM ZGR 2,4-DIHYDROXY-6-[(1E,10S)-10-HYDROXY-6-OXOUNDEC-1-EN-1-
HETNAM 2 ZGR YL]BENZOIC ACID
FORMUL 5 ZGR 4(C18 H24 O6)
FORMUL 9 HOH *629(H2 O)
HELIX 1 AA1 SER A 50 SER A 53 5 4
HELIX 2 AA2 TYR A 54 SER A 62 1 9
HELIX 3 AA3 SER A 86 VAL A 101 1 16
HELIX 4 AA4 SER A 112 SER A 125 1 14
HELIX 5 AA5 SER A 152 GLY A 156 5 5
HELIX 6 AA6 ALA A 157 LEU A 168 1 12
HELIX 7 AA7 GLY A 169 SER A 173 5 5
HELIX 8 AA8 ASP A 176 ALA A 186 1 11
HELIX 9 AA9 SER A 189 PHE A 195 1 7
HELIX 10 AB1 PRO A 201 GLU A 206 1 6
HELIX 11 AB2 PRO A 209 GLU A 217 1 9
HELIX 12 AB3 PRO A 225 GLY A 231 1 7
HELIX 13 AB4 SER A 258 ALA A 272 1 15
HELIX 14 AB5 MET A 287 ALA A 292 1 6
HELIX 15 AB6 ALA A 292 ALA A 306 1 15
HELIX 16 AB7 SER B 4 ARG B 8 5 5
HELIX 17 AB8 SER B 50 SER B 53 5 4
HELIX 18 AB9 TYR B 54 SER B 62 1 9
HELIX 19 AC1 SER B 86 VAL B 101 1 16
HELIX 20 AC2 SER B 112 SER B 125 1 14
HELIX 21 AC3 SER B 152 GLY B 156 5 5
HELIX 22 AC4 ALA B 157 LEU B 168 1 12
HELIX 23 AC5 GLY B 169 SER B 173 5 5
HELIX 24 AC6 ASP B 176 ALA B 186 1 11
HELIX 25 AC7 SER B 189 SER B 194 1 6
HELIX 26 AC8 PRO B 201 GLU B 206 1 6
HELIX 27 AC9 PRO B 209 GLU B 217 1 9
HELIX 28 AD1 PRO B 225 GLY B 231 1 7
HELIX 29 AD2 SER B 258 ALA B 272 1 15
HELIX 30 AD3 MET B 287 ALA B 292 1 6
HELIX 31 AD4 ALA B 292 LEU B 307 1 16
HELIX 32 AD5 SER C 4 ARG C 8 5 5
HELIX 33 AD6 SER C 50 SER C 53 5 4
HELIX 34 AD7 TYR C 54 SER C 62 1 9
HELIX 35 AD8 SER C 86 VAL C 101 1 16
HELIX 36 AD9 SER C 112 SER C 125 1 14
HELIX 37 AE1 SER C 152 GLY C 156 5 5
HELIX 38 AE2 ALA C 157 LEU C 168 1 12
HELIX 39 AE3 GLY C 169 SER C 173 5 5
HELIX 40 AE4 ASP C 176 ALA C 186 1 11
HELIX 41 AE5 SER C 189 SER C 194 1 6
HELIX 42 AE6 PRO C 201 GLU C 206 1 6
HELIX 43 AE7 PRO C 209 GLU C 217 1 9
HELIX 44 AE8 PRO C 225 GLY C 231 1 7
HELIX 45 AE9 SER C 258 ALA C 272 1 15
HELIX 46 AF1 MET C 287 ALA C 292 1 6
HELIX 47 AF2 ALA C 292 ALA C 306 1 15
HELIX 48 AF3 SER D 50 SER D 53 5 4
HELIX 49 AF4 TYR D 54 SER D 62 1 9
HELIX 50 AF5 SER D 86 VAL D 101 1 16
HELIX 51 AF6 SER D 112 SER D 125 1 14
HELIX 52 AF7 SER D 152 GLY D 156 5 5
HELIX 53 AF8 ALA D 157 LEU D 168 1 12
HELIX 54 AF9 GLY D 169 SER D 173 5 5
HELIX 55 AG1 ASP D 176 ALA D 186 1 11
HELIX 56 AG2 SER D 189 SER D 194 1 6
HELIX 57 AG3 PRO D 201 GLU D 206 1 6
HELIX 58 AG4 PRO D 209 GLU D 217 1 9
HELIX 59 AG5 PRO D 225 GLY D 231 1 7
HELIX 60 AG6 SER D 258 ALA D 272 1 15
HELIX 61 AG7 MET D 287 ALA D 292 1 6
HELIX 62 AG8 ALA D 292 ALA D 306 1 15
SHEET 1 AA1 8 GLU A 18 ASP A 22 0
SHEET 2 AA1 8 THR A 27 ALA A 33 -1 O TYR A 30 N GLN A 19
SHEET 3 AA1 8 HIS A 66 VAL A 70 -1 O VAL A 67 N ALA A 33
SHEET 4 AA1 8 ALA A 40 ILE A 44 1 N VAL A 41 O HIS A 66
SHEET 5 AA1 8 VAL A 106 ASN A 111 1 O ALA A 109 N LEU A 42
SHEET 6 AA1 8 LEU A 130 GLU A 136 1 O LEU A 134 N VAL A 108
SHEET 7 AA1 8 VAL A 237 HIS A 241 1 O LEU A 238 N CYS A 135
SHEET 8 AA1 8 VAL A 276 SER A 280 1 O ASP A 277 N LEU A 239
SHEET 1 AA2 2 ARG A 244 ILE A 246 0
SHEET 2 AA2 2 LEU A 253 GLY A 255 -1 O LEU A 254 N GLY A 245
SHEET 1 AA3 8 GLU B 18 ASP B 22 0
SHEET 2 AA3 8 THR B 27 ALA B 33 -1 O TYR B 30 N GLN B 19
SHEET 3 AA3 8 HIS B 66 VAL B 70 -1 O VAL B 67 N ALA B 33
SHEET 4 AA3 8 ALA B 40 ILE B 44 1 N LEU B 43 O TYR B 68
SHEET 5 AA3 8 VAL B 106 ASN B 111 1 O ALA B 109 N LEU B 42
SHEET 6 AA3 8 LEU B 130 GLU B 136 1 O LEU B 134 N VAL B 108
SHEET 7 AA3 8 VAL B 237 HIS B 241 1 O LEU B 238 N CYS B 135
SHEET 8 AA3 8 VAL B 276 SER B 280 1 O ASP B 277 N VAL B 237
SHEET 1 AA4 2 ARG B 244 ILE B 246 0
SHEET 2 AA4 2 LEU B 253 GLY B 255 -1 O LEU B 254 N GLY B 245
SHEET 1 AA5 8 GLU C 18 ASP C 22 0
SHEET 2 AA5 8 THR C 27 ALA C 33 -1 O TYR C 30 N GLN C 19
SHEET 3 AA5 8 HIS C 66 VAL C 70 -1 O VAL C 67 N ALA C 33
SHEET 4 AA5 8 ALA C 40 ILE C 44 1 N LEU C 43 O TYR C 68
SHEET 5 AA5 8 VAL C 106 ASN C 111 1 O ALA C 109 N LEU C 42
SHEET 6 AA5 8 LEU C 130 GLU C 136 1 O GLU C 136 N GLY C 110
SHEET 7 AA5 8 VAL C 237 HIS C 241 1 O LEU C 238 N CYS C 135
SHEET 8 AA5 8 VAL C 276 SER C 280 1 O ASP C 277 N VAL C 237
SHEET 1 AA6 2 ARG C 244 ILE C 246 0
SHEET 2 AA6 2 LEU C 253 GLY C 255 -1 O LEU C 254 N GLY C 245
SHEET 1 AA7 8 GLU D 18 ASP D 22 0
SHEET 2 AA7 8 THR D 27 ALA D 33 -1 O TYR D 30 N GLN D 19
SHEET 3 AA7 8 HIS D 66 VAL D 70 -1 O VAL D 67 N ALA D 33
SHEET 4 AA7 8 ALA D 40 ILE D 44 1 N VAL D 41 O HIS D 66
SHEET 5 AA7 8 VAL D 106 ASN D 111 1 O ALA D 109 N ILE D 44
SHEET 6 AA7 8 LEU D 130 GLU D 136 1 O LEU D 134 N VAL D 108
SHEET 7 AA7 8 VAL D 237 HIS D 241 1 O LEU D 238 N CYS D 135
SHEET 8 AA7 8 VAL D 276 SER D 280 1 O ASP D 277 N LEU D 239
SHEET 1 AA8 2 ARG D 244 ILE D 246 0
SHEET 2 AA8 2 LEU D 253 GLY D 255 -1 O LEU D 254 N GLY D 245
CRYST1 65.809 129.867 134.822 90.00 90.00 90.00 P 21 21 21 16
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 0.015195 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007700 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007417 0.00000
TER 4549 PRO A 309
TER 9240 HIS B 310
TER 13897 LEU C 307
TER 18547 ALA D 308
MASTER 291 0 4 62 40 0 0 610182 4 188 100
END |