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HEADER HYDROLASE 17-FEB-23 8CLV
TITLE ZEARALENONE LACTONASE OF RHODOCOCCUS ERYTHROPOLIS IN COMPLEX WITH
TITLE 2 HYDROLYZED ZEARALENONE
CAVEAT 8CLV ZGR A 400 HAS WRONG CHIRALITY AT ATOM C10 ZGR B 400 HAS
CAVEAT 2 8CLV WRONG CHIRALITY AT ATOM C10 ZGR C 400 HAS WRONG CHIRALITY
CAVEAT 3 8CLV AT ATOM C10 ZGR D 400 HAS WRONG CHIRALITY AT ATOM C10
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZEARALENONE LACTONASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS ERYTHROPOLIS;
SOURCE 3 ORGANISM_TAXID: 1833;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ZEARALENONE, MYCOTOXIN, LACTONASE, CARBOXYLESTERASE, ESTERASE,
KEYWDS 2 HYDROLASE, BIODEGRADATION, RHODOCOCCUS ERYTHROPOLIS, HYDROLYZED
KEYWDS 3 ZEARALENONE, HZEN
EXPDTA X-RAY DIFFRACTION
AUTHOR D.PUEHRINGER
REVDAT 1 28-FEB-24 8CLV 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. 2.54 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) : 2.54
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.05
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 3 NUMBER OF REFLECTIONS : 44325
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.510
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 47.0500 - 6.1200 0.87 3001 142 0.1747 0.1965
REMARK 3 2 6.1200 - 4.8600 0.90 2992 141 0.1684 0.1856
REMARK 3 3 4.8600 - 4.2400 0.91 3007 142 0.1480 0.1724
REMARK 3 4 4.2400 - 3.8600 0.92 3035 143 0.1669 0.1801
REMARK 3 5 3.8600 - 3.5800 0.92 3023 143 0.1916 0.2181
REMARK 3 6 3.5800 - 3.3700 0.93 3057 145 0.2202 0.2802
REMARK 3 7 3.3700 - 3.2000 0.94 3034 143 0.2425 0.3028
REMARK 3 8 3.2000 - 3.0600 0.93 3044 143 0.2647 0.3111
REMARK 3 9 3.0600 - 2.9400 0.94 3052 144 0.2843 0.3499
REMARK 3 10 2.9400 - 2.8400 0.94 3046 145 0.2808 0.3285
REMARK 3 11 2.8400 - 2.7500 0.93 3012 142 0.3116 0.3659
REMARK 3 12 2.7500 - 2.6700 0.93 3011 143 0.3359 0.3951
REMARK 3 13 2.6700 - 2.6000 0.93 3014 142 0.3411 0.4104
REMARK 3 14 2.6000 - 2.5400 0.93 2998 141 0.3478 0.3627
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) : 0.420
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.85
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 : 0.003 9828
REMARK 3 ANGLE : 0.582 13408
REMARK 3 CHIRALITY : 0.040 1420
REMARK 3 PLANARITY : 0.005 1768
REMARK 3 DIHEDRAL : 9.373 1336
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 8CLV 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_1292126828.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-MAY-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 4M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44439
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.540
REMARK 200 RESOLUTION RANGE LOW (A) : 47.050
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 10.50
REMARK 200 R MERGE (I) : 0.21970
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.6300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.54
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.80
REMARK 200 R MERGE FOR SHELL (I) : 1.98400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.370
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 (%): 50.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NACL, 0.1 M BIS-TRIS 5.5 PH, 25%
REMARK 280 W/V PEG 3350, PH 5.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 295.15K
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 68.06500
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 68.06500
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 61.69000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 86.04500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 61.69000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 86.04500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.06500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 61.69000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 86.04500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.06500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 61.69000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 86.04500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 APPLY THE FOLLOWING TO CHAINS: A, B
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ALA A 2
REMARK 465 GLU A 3
REMARK 465 GLU A 4
REMARK 465 GLY A 5
REMARK 465 THR A 6
REMARK 465 ARG A 7
REMARK 465 SER A 8
REMARK 465 GLU A 9
REMARK 465 ALA A 10
REMARK 465 ALA A 11
REMARK 465 ASP A 12
REMARK 465 ALA A 13
REMARK 465 ALA A 14
REMARK 465 THR A 15
REMARK 465 GLN A 16
REMARK 465 ALA A 17
REMARK 465 ARG A 18
REMARK 465 GLN A 19
REMARK 465 LEU A 20
REMARK 465 PRO A 21
REMARK 465 ASP A 22
REMARK 465 SER A 23
REMARK 465 ARG A 24
REMARK 465 ASN A 327
REMARK 465 ASP A 328
REMARK 465 HIS A 329
REMARK 465 HIS A 330
REMARK 465 HIS A 331
REMARK 465 HIS A 332
REMARK 465 HIS A 333
REMARK 465 HIS A 334
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 GLU B 3
REMARK 465 GLU B 4
REMARK 465 GLY B 5
REMARK 465 THR B 6
REMARK 465 ARG B 7
REMARK 465 SER B 8
REMARK 465 GLU B 9
REMARK 465 ALA B 10
REMARK 465 ALA B 11
REMARK 465 ASP B 12
REMARK 465 ALA B 13
REMARK 465 ALA B 14
REMARK 465 THR B 15
REMARK 465 GLN B 16
REMARK 465 ALA B 17
REMARK 465 ARG B 18
REMARK 465 GLN B 19
REMARK 465 LEU B 20
REMARK 465 PRO B 21
REMARK 465 ASP B 22
REMARK 465 SER B 23
REMARK 465 ARG B 24
REMARK 465 ASN B 327
REMARK 465 ASP B 328
REMARK 465 HIS B 329
REMARK 465 HIS B 330
REMARK 465 HIS B 331
REMARK 465 HIS B 332
REMARK 465 HIS B 333
REMARK 465 HIS B 334
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 GLU C 3
REMARK 465 GLU C 4
REMARK 465 GLY C 5
REMARK 465 THR C 6
REMARK 465 ARG C 7
REMARK 465 SER C 8
REMARK 465 GLU C 9
REMARK 465 ALA C 10
REMARK 465 ALA C 11
REMARK 465 ASP C 12
REMARK 465 ALA C 13
REMARK 465 ALA C 14
REMARK 465 THR C 15
REMARK 465 GLN C 16
REMARK 465 ALA C 17
REMARK 465 ARG C 18
REMARK 465 GLN C 19
REMARK 465 LEU C 20
REMARK 465 PRO C 21
REMARK 465 ASP C 22
REMARK 465 SER C 23
REMARK 465 ARG C 24
REMARK 465 ASN C 327
REMARK 465 ASP C 328
REMARK 465 HIS C 329
REMARK 465 HIS C 330
REMARK 465 HIS C 331
REMARK 465 HIS C 332
REMARK 465 HIS C 333
REMARK 465 HIS C 334
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 GLU D 3
REMARK 465 GLU D 4
REMARK 465 GLY D 5
REMARK 465 THR D 6
REMARK 465 ARG D 7
REMARK 465 SER D 8
REMARK 465 GLU D 9
REMARK 465 ALA D 10
REMARK 465 ALA D 11
REMARK 465 ASP D 12
REMARK 465 ALA D 13
REMARK 465 ALA D 14
REMARK 465 THR D 15
REMARK 465 GLN D 16
REMARK 465 ALA D 17
REMARK 465 ARG D 18
REMARK 465 GLN D 19
REMARK 465 LEU D 20
REMARK 465 PRO D 21
REMARK 465 ASP D 22
REMARK 465 SER D 23
REMARK 465 ARG D 24
REMARK 465 ASN D 327
REMARK 465 ASP D 328
REMARK 465 HIS D 329
REMARK 465 HIS D 330
REMARK 465 HIS D 331
REMARK 465 HIS D 332
REMARK 465 HIS D 333
REMARK 465 HIS D 334
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 ASP D 87 HG SER D 94 1.58
REMARK 500 OG SER C 128 O13 ZGR C 400 2.11
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 THR A 64 -5.03 76.34
REMARK 500 ARG A 99 -5.41 75.97
REMARK 500 SER A 128 -120.82 67.41
REMARK 500 PHE A 157 -53.50 70.60
REMARK 500 ALA A 172 -100.74 -131.00
REMARK 500 HIS A 259 -153.80 -95.42
REMARK 500 THR B 64 -6.62 80.08
REMARK 500 SER B 128 -111.74 56.53
REMARK 500 PHE B 157 -52.55 73.72
REMARK 500 ALA B 172 -93.57 -136.57
REMARK 500 HIS B 259 -150.73 -91.69
REMARK 500 ASP B 309 58.24 -145.01
REMARK 500 SER C 128 -105.17 58.17
REMARK 500 PHE C 157 -58.97 70.71
REMARK 500 ALA C 172 -103.19 -145.72
REMARK 500 HIS C 259 -153.08 -89.86
REMARK 500 ARG D 89 129.40 -38.70
REMARK 500 SER D 128 -116.94 61.79
REMARK 500 PHE D 157 -53.57 73.79
REMARK 500 ALA D 172 -98.95 -136.42
REMARK 500 HIS D 259 -157.51 -94.68
REMARK 500
REMARK 500 REMARK: NULL
DBREF 8CLV A 1 334 PDB 8CLV 8CLV 1 334
DBREF 8CLV B 1 334 PDB 8CLV 8CLV 1 334
DBREF 8CLV C 1 334 PDB 8CLV 8CLV 1 334
DBREF 8CLV D 1 334 PDB 8CLV 8CLV 1 334
SEQRES 1 A 334 MET ALA GLU GLU GLY THR ARG SER GLU ALA ALA ASP ALA
SEQRES 2 A 334 ALA THR GLN ALA ARG GLN LEU PRO ASP SER ARG ASN ILE
SEQRES 3 A 334 PHE VAL SER HIS ARG PHE PRO GLU ARG GLN VAL ASP LEU
SEQRES 4 A 334 GLY GLU VAL VAL MET ASN PHE ALA GLU ALA GLY SER PRO
SEQRES 5 A 334 ASP ASN PRO ALA LEU LEU LEU LEU PRO GLU GLN THR GLY
SEQRES 6 A 334 SER TRP TRP SER TYR GLU PRO VAL MET GLY LEU LEU ALA
SEQRES 7 A 334 GLU ASN PHE HIS VAL PHE ALA VAL ASP ILE ARG GLY GLN
SEQRES 8 A 334 GLY ARG SER THR TRP THR PRO ARG ARG TYR SER LEU ASP
SEQRES 9 A 334 ASN PHE GLY ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL
SEQRES 10 A 334 ILE LYS ARG PRO VAL VAL VAL ALA GLY ASN SER SER GLY
SEQRES 11 A 334 GLY LEU LEU ALA ALA TRP LEU SER ALA TYR ALA MET PRO
SEQRES 12 A 334 GLY GLN ILE ARG ALA ALA LEU CYS GLU ASP ALA PRO PHE
SEQRES 13 A 334 PHE ALA SER GLU LEU VAL PRO ALA TYR GLY HIS SER VAL
SEQRES 14 A 334 LEU GLN ALA ALA GLY PRO ALA PHE GLU LEU TYR ARG ASP
SEQRES 15 A 334 PHE LEU GLY ASP GLN TRP SER ILE GLY ASP TRP LYS GLY
SEQRES 16 A 334 PHE VAL GLU ALA ALA LYS ALA SER PRO ALA LYS ALA MET
SEQRES 17 A 334 GLN LEU PHE PRO THR PRO ASP GLU ALA PRO GLN ASN LEU
SEQRES 18 A 334 LYS GLU TYR ASP PRO GLU TRP GLY ARG ALA PHE PHE GLU
SEQRES 19 A 334 GLY THR VAL ALA LEU HIS CYS PRO HIS ASP ARG MET LEU
SEQRES 20 A 334 SER GLN VAL LYS THR PRO ILE LEU ILE THR HIS HIS ALA
SEQRES 21 A 334 ARG THR ILE ASP PRO GLU THR GLY GLU LEU LEU GLY ALA
SEQRES 22 A 334 LEU SER ASP LEU GLN ALA GLU HIS ALA GLN ASP ILE ILE
SEQRES 23 A 334 ARG SER ALA GLY VAL ARG VAL ASP TYR GLN SER HIS PRO
SEQRES 24 A 334 ASP ALA LEU HIS MET MET HIS LEU PHE ASP PRO ALA ARG
SEQRES 25 A 334 TYR ALA GLU ILE LEU THR SER TRP SER ALA THR LEU PRO
SEQRES 26 A 334 ALA ASN ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 B 334 MET ALA GLU GLU GLY THR ARG SER GLU ALA ALA ASP ALA
SEQRES 2 B 334 ALA THR GLN ALA ARG GLN LEU PRO ASP SER ARG ASN ILE
SEQRES 3 B 334 PHE VAL SER HIS ARG PHE PRO GLU ARG GLN VAL ASP LEU
SEQRES 4 B 334 GLY GLU VAL VAL MET ASN PHE ALA GLU ALA GLY SER PRO
SEQRES 5 B 334 ASP ASN PRO ALA LEU LEU LEU LEU PRO GLU GLN THR GLY
SEQRES 6 B 334 SER TRP TRP SER TYR GLU PRO VAL MET GLY LEU LEU ALA
SEQRES 7 B 334 GLU ASN PHE HIS VAL PHE ALA VAL ASP ILE ARG GLY GLN
SEQRES 8 B 334 GLY ARG SER THR TRP THR PRO ARG ARG TYR SER LEU ASP
SEQRES 9 B 334 ASN PHE GLY ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL
SEQRES 10 B 334 ILE LYS ARG PRO VAL VAL VAL ALA GLY ASN SER SER GLY
SEQRES 11 B 334 GLY LEU LEU ALA ALA TRP LEU SER ALA TYR ALA MET PRO
SEQRES 12 B 334 GLY GLN ILE ARG ALA ALA LEU CYS GLU ASP ALA PRO PHE
SEQRES 13 B 334 PHE ALA SER GLU LEU VAL PRO ALA TYR GLY HIS SER VAL
SEQRES 14 B 334 LEU GLN ALA ALA GLY PRO ALA PHE GLU LEU TYR ARG ASP
SEQRES 15 B 334 PHE LEU GLY ASP GLN TRP SER ILE GLY ASP TRP LYS GLY
SEQRES 16 B 334 PHE VAL GLU ALA ALA LYS ALA SER PRO ALA LYS ALA MET
SEQRES 17 B 334 GLN LEU PHE PRO THR PRO ASP GLU ALA PRO GLN ASN LEU
SEQRES 18 B 334 LYS GLU TYR ASP PRO GLU TRP GLY ARG ALA PHE PHE GLU
SEQRES 19 B 334 GLY THR VAL ALA LEU HIS CYS PRO HIS ASP ARG MET LEU
SEQRES 20 B 334 SER GLN VAL LYS THR PRO ILE LEU ILE THR HIS HIS ALA
SEQRES 21 B 334 ARG THR ILE ASP PRO GLU THR GLY GLU LEU LEU GLY ALA
SEQRES 22 B 334 LEU SER ASP LEU GLN ALA GLU HIS ALA GLN ASP ILE ILE
SEQRES 23 B 334 ARG SER ALA GLY VAL ARG VAL ASP TYR GLN SER HIS PRO
SEQRES 24 B 334 ASP ALA LEU HIS MET MET HIS LEU PHE ASP PRO ALA ARG
SEQRES 25 B 334 TYR ALA GLU ILE LEU THR SER TRP SER ALA THR LEU PRO
SEQRES 26 B 334 ALA ASN ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 C 334 MET ALA GLU GLU GLY THR ARG SER GLU ALA ALA ASP ALA
SEQRES 2 C 334 ALA THR GLN ALA ARG GLN LEU PRO ASP SER ARG ASN ILE
SEQRES 3 C 334 PHE VAL SER HIS ARG PHE PRO GLU ARG GLN VAL ASP LEU
SEQRES 4 C 334 GLY GLU VAL VAL MET ASN PHE ALA GLU ALA GLY SER PRO
SEQRES 5 C 334 ASP ASN PRO ALA LEU LEU LEU LEU PRO GLU GLN THR GLY
SEQRES 6 C 334 SER TRP TRP SER TYR GLU PRO VAL MET GLY LEU LEU ALA
SEQRES 7 C 334 GLU ASN PHE HIS VAL PHE ALA VAL ASP ILE ARG GLY GLN
SEQRES 8 C 334 GLY ARG SER THR TRP THR PRO ARG ARG TYR SER LEU ASP
SEQRES 9 C 334 ASN PHE GLY ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL
SEQRES 10 C 334 ILE LYS ARG PRO VAL VAL VAL ALA GLY ASN SER SER GLY
SEQRES 11 C 334 GLY LEU LEU ALA ALA TRP LEU SER ALA TYR ALA MET PRO
SEQRES 12 C 334 GLY GLN ILE ARG ALA ALA LEU CYS GLU ASP ALA PRO PHE
SEQRES 13 C 334 PHE ALA SER GLU LEU VAL PRO ALA TYR GLY HIS SER VAL
SEQRES 14 C 334 LEU GLN ALA ALA GLY PRO ALA PHE GLU LEU TYR ARG ASP
SEQRES 15 C 334 PHE LEU GLY ASP GLN TRP SER ILE GLY ASP TRP LYS GLY
SEQRES 16 C 334 PHE VAL GLU ALA ALA LYS ALA SER PRO ALA LYS ALA MET
SEQRES 17 C 334 GLN LEU PHE PRO THR PRO ASP GLU ALA PRO GLN ASN LEU
SEQRES 18 C 334 LYS GLU TYR ASP PRO GLU TRP GLY ARG ALA PHE PHE GLU
SEQRES 19 C 334 GLY THR VAL ALA LEU HIS CYS PRO HIS ASP ARG MET LEU
SEQRES 20 C 334 SER GLN VAL LYS THR PRO ILE LEU ILE THR HIS HIS ALA
SEQRES 21 C 334 ARG THR ILE ASP PRO GLU THR GLY GLU LEU LEU GLY ALA
SEQRES 22 C 334 LEU SER ASP LEU GLN ALA GLU HIS ALA GLN ASP ILE ILE
SEQRES 23 C 334 ARG SER ALA GLY VAL ARG VAL ASP TYR GLN SER HIS PRO
SEQRES 24 C 334 ASP ALA LEU HIS MET MET HIS LEU PHE ASP PRO ALA ARG
SEQRES 25 C 334 TYR ALA GLU ILE LEU THR SER TRP SER ALA THR LEU PRO
SEQRES 26 C 334 ALA ASN ASP HIS HIS HIS HIS HIS HIS
SEQRES 1 D 334 MET ALA GLU GLU GLY THR ARG SER GLU ALA ALA ASP ALA
SEQRES 2 D 334 ALA THR GLN ALA ARG GLN LEU PRO ASP SER ARG ASN ILE
SEQRES 3 D 334 PHE VAL SER HIS ARG PHE PRO GLU ARG GLN VAL ASP LEU
SEQRES 4 D 334 GLY GLU VAL VAL MET ASN PHE ALA GLU ALA GLY SER PRO
SEQRES 5 D 334 ASP ASN PRO ALA LEU LEU LEU LEU PRO GLU GLN THR GLY
SEQRES 6 D 334 SER TRP TRP SER TYR GLU PRO VAL MET GLY LEU LEU ALA
SEQRES 7 D 334 GLU ASN PHE HIS VAL PHE ALA VAL ASP ILE ARG GLY GLN
SEQRES 8 D 334 GLY ARG SER THR TRP THR PRO ARG ARG TYR SER LEU ASP
SEQRES 9 D 334 ASN PHE GLY ASN ASP LEU VAL ARG PHE ILE ALA LEU VAL
SEQRES 10 D 334 ILE LYS ARG PRO VAL VAL VAL ALA GLY ASN SER SER GLY
SEQRES 11 D 334 GLY LEU LEU ALA ALA TRP LEU SER ALA TYR ALA MET PRO
SEQRES 12 D 334 GLY GLN ILE ARG ALA ALA LEU CYS GLU ASP ALA PRO PHE
SEQRES 13 D 334 PHE ALA SER GLU LEU VAL PRO ALA TYR GLY HIS SER VAL
SEQRES 14 D 334 LEU GLN ALA ALA GLY PRO ALA PHE GLU LEU TYR ARG ASP
SEQRES 15 D 334 PHE LEU GLY ASP GLN TRP SER ILE GLY ASP TRP LYS GLY
SEQRES 16 D 334 PHE VAL GLU ALA ALA LYS ALA SER PRO ALA LYS ALA MET
SEQRES 17 D 334 GLN LEU PHE PRO THR PRO ASP GLU ALA PRO GLN ASN LEU
SEQRES 18 D 334 LYS GLU TYR ASP PRO GLU TRP GLY ARG ALA PHE PHE GLU
SEQRES 19 D 334 GLY THR VAL ALA LEU HIS CYS PRO HIS ASP ARG MET LEU
SEQRES 20 D 334 SER GLN VAL LYS THR PRO ILE LEU ILE THR HIS HIS ALA
SEQRES 21 D 334 ARG THR ILE ASP PRO GLU THR GLY GLU LEU LEU GLY ALA
SEQRES 22 D 334 LEU SER ASP LEU GLN ALA GLU HIS ALA GLN ASP ILE ILE
SEQRES 23 D 334 ARG SER ALA GLY VAL ARG VAL ASP TYR GLN SER HIS PRO
SEQRES 24 D 334 ASP ALA LEU HIS MET MET HIS LEU PHE ASP PRO ALA ARG
SEQRES 25 D 334 TYR ALA GLU ILE LEU THR SER TRP SER ALA THR LEU PRO
SEQRES 26 D 334 ALA ASN ASP HIS HIS HIS HIS HIS HIS
HET ZGR A 400 47
HET ZGR B 400 47
HET ZGR C 400 47
HET ZGR D 400 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 *135(H2 O)
HELIX 1 AA1 SER A 66 SER A 69 5 4
HELIX 2 AA2 TYR A 70 ALA A 78 1 9
HELIX 3 AA3 SER A 102 VAL A 117 1 16
HELIX 4 AA4 SER A 128 ALA A 141 1 14
HELIX 5 AA5 SER A 168 ALA A 172 5 5
HELIX 6 AA6 ALA A 173 LEU A 184 1 12
HELIX 7 AA7 GLY A 185 SER A 189 5 5
HELIX 8 AA8 ASP A 192 SER A 203 1 12
HELIX 9 AA9 ALA A 205 PHE A 211 5 7
HELIX 10 AB1 PRO A 218 GLU A 223 1 6
HELIX 11 AB2 PRO A 226 GLU A 234 1 9
HELIX 12 AB3 PRO A 242 GLN A 249 1 8
HELIX 13 AB4 SER A 275 ALA A 289 1 15
HELIX 14 AB5 MET A 304 ASP A 309 1 6
HELIX 15 AB6 ASP A 309 THR A 323 1 15
HELIX 16 AB7 SER B 66 SER B 69 5 4
HELIX 17 AB8 TYR B 70 ALA B 78 1 9
HELIX 18 AB9 SER B 102 VAL B 117 1 16
HELIX 19 AC1 SER B 128 ALA B 141 1 14
HELIX 20 AC2 SER B 168 ALA B 172 5 5
HELIX 21 AC3 ALA B 173 LEU B 184 1 12
HELIX 22 AC4 GLY B 185 SER B 189 5 5
HELIX 23 AC5 ASP B 192 SER B 203 1 12
HELIX 24 AC6 ALA B 205 PHE B 211 5 7
HELIX 25 AC7 PRO B 218 GLU B 223 1 6
HELIX 26 AC8 PRO B 226 GLU B 234 1 9
HELIX 27 AC9 PRO B 242 VAL B 250 1 9
HELIX 28 AD1 SER B 275 ALA B 289 1 15
HELIX 29 AD2 MET B 304 ASP B 309 1 6
HELIX 30 AD3 ASP B 309 THR B 323 1 15
HELIX 31 AD4 SER C 66 SER C 69 5 4
HELIX 32 AD5 TYR C 70 GLU C 79 1 10
HELIX 33 AD6 SER C 102 VAL C 117 1 16
HELIX 34 AD7 SER C 128 ALA C 141 1 14
HELIX 35 AD8 SER C 168 ALA C 172 5 5
HELIX 36 AD9 ALA C 173 LEU C 184 1 12
HELIX 37 AE1 GLY C 185 SER C 189 5 5
HELIX 38 AE2 ASP C 192 SER C 203 1 12
HELIX 39 AE3 ALA C 205 PHE C 211 5 7
HELIX 40 AE4 PRO C 218 GLU C 223 1 6
HELIX 41 AE5 PRO C 226 GLU C 234 1 9
HELIX 42 AE6 PRO C 242 GLN C 249 1 8
HELIX 43 AE7 SER C 275 ALA C 289 1 15
HELIX 44 AE8 MET C 304 ASP C 309 1 6
HELIX 45 AE9 ASP C 309 THR C 323 1 15
HELIX 46 AF1 SER D 66 SER D 69 5 4
HELIX 47 AF2 TYR D 70 GLU D 79 1 10
HELIX 48 AF3 SER D 102 VAL D 117 1 16
HELIX 49 AF4 SER D 128 ALA D 141 1 14
HELIX 50 AF5 SER D 168 ALA D 172 5 5
HELIX 51 AF6 ALA D 173 LEU D 184 1 12
HELIX 52 AF7 GLY D 185 SER D 189 5 5
HELIX 53 AF8 ASP D 192 SER D 203 1 12
HELIX 54 AF9 PRO D 218 GLU D 223 1 6
HELIX 55 AG1 PRO D 226 GLU D 234 1 9
HELIX 56 AG2 PRO D 242 GLN D 249 1 8
HELIX 57 AG3 SER D 275 ALA D 289 1 15
HELIX 58 AG4 MET D 304 ASP D 309 1 6
HELIX 59 AG5 ASP D 309 THR D 323 1 15
SHEET 1 AA1 8 GLU A 34 ASP A 38 0
SHEET 2 AA1 8 VAL A 43 ALA A 49 -1 O PHE A 46 N ARG A 35
SHEET 3 AA1 8 HIS A 82 VAL A 86 -1 O ALA A 85 N ALA A 47
SHEET 4 AA1 8 ALA A 56 LEU A 60 1 N LEU A 57 O HIS A 82
SHEET 5 AA1 8 VAL A 122 ASN A 127 1 O VAL A 123 N LEU A 58
SHEET 6 AA1 8 ILE A 146 GLU A 152 1 O LEU A 150 N VAL A 124
SHEET 7 AA1 8 ILE A 254 HIS A 258 1 O LEU A 255 N CYS A 151
SHEET 8 AA1 8 VAL A 293 SER A 297 1 O ASP A 294 N ILE A 256
SHEET 1 AA2 2 THR A 262 ILE A 263 0
SHEET 2 AA2 2 LEU A 270 LEU A 271 -1 O LEU A 271 N THR A 262
SHEET 1 AA3 8 GLU B 34 ASP B 38 0
SHEET 2 AA3 8 VAL B 43 ALA B 49 -1 O PHE B 46 N ARG B 35
SHEET 3 AA3 8 HIS B 82 VAL B 86 -1 O ALA B 85 N ALA B 47
SHEET 4 AA3 8 ALA B 56 LEU B 60 1 N LEU B 57 O PHE B 84
SHEET 5 AA3 8 VAL B 122 ASN B 127 1 O ALA B 125 N LEU B 58
SHEET 6 AA3 8 ILE B 146 GLU B 152 1 O LEU B 150 N VAL B 124
SHEET 7 AA3 8 ILE B 254 HIS B 258 1 O LEU B 255 N CYS B 151
SHEET 8 AA3 8 VAL B 293 SER B 297 1 O GLN B 296 N ILE B 256
SHEET 1 AA4 2 ARG B 261 ILE B 263 0
SHEET 2 AA4 2 LEU B 270 GLY B 272 -1 O LEU B 271 N THR B 262
SHEET 1 AA5 8 GLU C 34 ASP C 38 0
SHEET 2 AA5 8 VAL C 43 ALA C 49 -1 O PHE C 46 N ARG C 35
SHEET 3 AA5 8 HIS C 82 VAL C 86 -1 O ALA C 85 N ALA C 47
SHEET 4 AA5 8 ALA C 56 LEU C 60 1 N LEU C 59 O PHE C 84
SHEET 5 AA5 8 VAL C 122 ASN C 127 1 O ALA C 125 N LEU C 58
SHEET 6 AA5 8 ILE C 146 GLU C 152 1 O LEU C 150 N VAL C 124
SHEET 7 AA5 8 ILE C 254 HIS C 258 1 O LEU C 255 N CYS C 151
SHEET 8 AA5 8 VAL C 293 SER C 297 1 O ASP C 294 N ILE C 256
SHEET 1 AA6 2 ARG C 261 ILE C 263 0
SHEET 2 AA6 2 LEU C 270 GLY C 272 -1 O LEU C 271 N THR C 262
SHEET 1 AA7 8 GLU D 34 ASP D 38 0
SHEET 2 AA7 8 VAL D 43 ALA D 49 -1 O PHE D 46 N ARG D 35
SHEET 3 AA7 8 HIS D 82 VAL D 86 -1 O ALA D 85 N ALA D 47
SHEET 4 AA7 8 ALA D 56 LEU D 60 1 N LEU D 57 O PHE D 84
SHEET 5 AA7 8 VAL D 122 ASN D 127 1 O VAL D 123 N LEU D 58
SHEET 6 AA7 8 ILE D 146 GLU D 152 1 O LEU D 150 N VAL D 124
SHEET 7 AA7 8 ILE D 254 HIS D 258 1 O LEU D 255 N CYS D 151
SHEET 8 AA7 8 VAL D 293 SER D 297 1 O GLN D 296 N HIS D 258
SHEET 1 AA8 2 ARG D 261 ILE D 263 0
SHEET 2 AA8 2 LEU D 270 GLY D 272 -1 O LEU D 271 N THR D 262
CRYST1 123.380 172.090 136.130 90.00 90.00 90.00 C 2 2 21 32
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 0.008105 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005811 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007346 0.00000
TER 4635 ALA A 326
TER 9270 ALA B 326
TER 13905 ALA C 326
TER 18541 ALA D 326
MASTER 408 0 4 59 40 0 0 6 9675 4 188 104
END |