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HEADER HYDROLASE 26-JUN-15 5C8Z
TITLE ZHD-ZGR COMPLEX AFTER ZHD CRYSTAL SOAKING IN ZEN FOR 30MIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZEARALENONE HYDROLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLONOSTACHYS ROSEA;
SOURCE 3 ORGANISM_TAXID: 29856;
SOURCE 4 GENE: ZHD101;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LACTONASE, HYDROLASE, ALPHA-BETA FOLD, ZEARALENONE DEGRADE
KEYWDS 2 INTERMEDIATE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.-J.HU,Q.QI,W.-J.YANG
REVDAT 2 25-APR-18 5C8Z 1 JRNL REMARK
REVDAT 1 29-JUN-16 5C8Z 0
JRNL AUTH Q.QI,W.J.YANG,H.J.ZHOU,D.M.MING,K.L.SUN,T.Y.XU,X.J.HU,H.LV
JRNL TITL THE STRUCTURE OF A COMPLEX OF THE LACTONOHYDROLASE
JRNL TITL 2 ZEARALENONE HYDROLASE WITH THE HYDROLYSIS PRODUCT OF
JRNL TITL 3 ZEARALENONE AT 1.60 ANGSTROM RESOLUTION.
JRNL REF ACTA CRYSTALLOGR F STRUCT V. 73 376 2017
JRNL REF 2 BIOL COMMUN
JRNL REFN ESSN 2053-230X
JRNL PMID 28695844
JRNL DOI 10.1107/S2053230X17007713
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.03
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 101261
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.154
REMARK 3 FREE R VALUE : 0.168
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5060
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 48.0501 - 4.9698 0.97 3323 189 0.2081 0.2058
REMARK 3 2 4.9698 - 3.9453 1.00 3312 163 0.1645 0.1980
REMARK 3 3 3.9453 - 3.4467 1.00 3271 176 0.1451 0.1599
REMARK 3 4 3.4467 - 3.1317 1.00 3243 182 0.1463 0.1557
REMARK 3 5 3.1317 - 2.9072 1.00 3244 160 0.1453 0.1509
REMARK 3 6 2.9072 - 2.7358 1.00 3222 184 0.1443 0.1498
REMARK 3 7 2.7358 - 2.5988 1.00 3233 169 0.1548 0.1684
REMARK 3 8 2.5988 - 2.4857 1.00 3218 168 0.1578 0.1635
REMARK 3 9 2.4857 - 2.3900 1.00 3213 158 0.1500 0.1565
REMARK 3 10 2.3900 - 2.3076 1.00 3214 188 0.1507 0.1648
REMARK 3 11 2.3076 - 2.2354 1.00 3187 171 0.1434 0.1591
REMARK 3 12 2.2354 - 2.1715 1.00 3214 177 0.1448 0.1466
REMARK 3 13 2.1715 - 2.1143 1.00 3193 172 0.1469 0.1585
REMARK 3 14 2.1143 - 2.0628 1.00 3171 168 0.1419 0.1443
REMARK 3 15 2.0628 - 2.0159 1.00 3204 177 0.1419 0.1604
REMARK 3 16 2.0159 - 1.9730 1.00 3190 162 0.1373 0.1322
REMARK 3 17 1.9730 - 1.9335 1.00 3208 167 0.1313 0.1622
REMARK 3 18 1.9335 - 1.8970 1.00 3144 178 0.1328 0.1724
REMARK 3 19 1.8970 - 1.8631 1.00 3202 164 0.1372 0.1442
REMARK 3 20 1.8631 - 1.8315 1.00 3182 149 0.1362 0.1508
REMARK 3 21 1.8315 - 1.8020 1.00 3223 162 0.1439 0.1601
REMARK 3 22 1.8020 - 1.7743 1.00 3165 174 0.1465 0.1678
REMARK 3 23 1.7743 - 1.7482 1.00 3182 151 0.1502 0.1841
REMARK 3 24 1.7482 - 1.7236 1.00 3202 151 0.1585 0.2005
REMARK 3 25 1.7236 - 1.7003 1.00 3172 162 0.1586 0.1958
REMARK 3 26 1.7003 - 1.6782 1.00 3210 163 0.1599 0.1889
REMARK 3 27 1.6782 - 1.6572 1.00 3181 158 0.1622 0.2088
REMARK 3 28 1.6572 - 1.6372 1.00 3191 171 0.1646 0.1834
REMARK 3 29 1.6372 - 1.6182 1.00 3148 171 0.1664 0.1775
REMARK 3 30 1.6182 - 1.6000 1.00 3139 175 0.1726 0.1981
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) : 0.120
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 14.180
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 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 : 0.006 4559
REMARK 3 ANGLE : 1.117 6262
REMARK 3 CHIRALITY : 0.047 693
REMARK 3 PLANARITY : 0.006 827
REMARK 3 DIHEDRAL : 12.820 1659
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4650 15.9828 -5.5950
REMARK 3 T TENSOR
REMARK 3 T11: 0.0886 T22: 0.1125
REMARK 3 T33: 0.1173 T12: -0.0044
REMARK 3 T13: -0.0002 T23: -0.0173
REMARK 3 L TENSOR
REMARK 3 L11: 0.2091 L22: 0.4851
REMARK 3 L33: 0.6038 L12: 0.0442
REMARK 3 L13: -0.0899 L23: -0.3232
REMARK 3 S TENSOR
REMARK 3 S11: 0.0204 S12: 0.0060 S13: -0.0001
REMARK 3 S21: 0.0071 S22: 0.0051 S23: 0.0080
REMARK 3 S31: -0.0281 S32: 0.0142 S33: -0.0247
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 5C8Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000211229.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-JAN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97923
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101351
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.20
REMARK 200 R MERGE FOR SHELL (I) : 0.42500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3WZL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M AMMONIUM DIBASIC PHOSPHATE, 200
REMARK 280 MM KCL, 100 MM IMIDAZOLE, PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 37.45000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.89500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.79500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.89500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.45000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.79500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
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 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 SER A 268
REMARK 465 SER A 269
REMARK 465 VAL A 270
REMARK 465 ASP A 271
REMARK 465 LYS A 272
REMARK 465 LEU A 273
REMARK 465 ALA A 274
REMARK 465 ALA A 275
REMARK 465 ALA A 276
REMARK 465 LEU A 277
REMARK 465 GLU A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 HIS A 282
REMARK 465 HIS A 283
REMARK 465 HIS A 284
REMARK 465 MET B 1
REMARK 465 SER B 268
REMARK 465 SER B 269
REMARK 465 VAL B 270
REMARK 465 ASP B 271
REMARK 465 LYS B 272
REMARK 465 LEU B 273
REMARK 465 ALA B 274
REMARK 465 ALA B 275
REMARK 465 ALA B 276
REMARK 465 LEU B 277
REMARK 465 GLU B 278
REMARK 465 HIS B 279
REMARK 465 HIS B 280
REMARK 465 HIS B 281
REMARK 465 HIS B 282
REMARK 465 HIS B 283
REMARK 465 HIS B 284
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 ASP A 31 -174.35 -65.26
REMARK 500 SER A 62 -125.52 52.72
REMARK 500 SER A 102 -128.76 67.28
REMARK 500 GLU A 126 71.87 46.93
REMARK 500 MET A 241 -109.01 -129.84
REMARK 500 ASP B 31 -173.68 -67.02
REMARK 500 SER B 62 -124.18 53.14
REMARK 500 SER B 102 -128.32 66.72
REMARK 500 GLU B 126 72.44 48.02
REMARK 500 PRO B 196 49.35 -80.18
REMARK 500 MET B 241 -110.08 -130.42
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA B 65 10.82
REMARK 500 ALA B 65 11.22
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 ZGR A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZGR B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 304
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5C7Y RELATED DB: PDB
REMARK 900 5C7Y CONTAINS THE SAME PROTEIN COMPLEXED WITH SUBSTRATE
REMARK 900 INTERMEDIATE.
REMARK 900 RELATED ID: 5C81 RELATED DB: PDB
REMARK 900 5C81 CONTAINS THE SAME PROTEIN COMPLEXED WITH SUBSTRATE
REMARK 900 INTERMEDIATE.
REMARK 900 RELATED ID: 5C8X RELATED DB: PDB
REMARK 900 5C8X CONTAINS THE SAME PROTEIN COMPLEXED WITH SUBSTRATE
REMARK 900 INTERMEDIATE AND PRODUCT ZGR.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE STRAIN OF CLONOSTACHYS ROSEA IS DIFFERENT FROM UNP Q8NKB0.
DBREF 5C8Z A 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
DBREF 5C8Z B 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
SEQADV 5C8Z ILE A 26 UNP Q8NKB0 VAL 26 SEE SEQUENCE DETAILS
SEQADV 5C8Z ALA A 69 UNP Q8NKB0 PRO 69 SEE SEQUENCE DETAILS
SEQADV 5C8Z ILE A 87 UNP Q8NKB0 VAL 87 SEE SEQUENCE DETAILS
SEQADV 5C8Z ASN A 148 UNP Q8NKB0 LYS 148 SEE SEQUENCE DETAILS
SEQADV 5C8Z LEU A 168 UNP Q8NKB0 MET 168 SEE SEQUENCE DETAILS
SEQADV 5C8Z VAL A 170 UNP Q8NKB0 ASP 170 SEE SEQUENCE DETAILS
SEQADV 5C8Z GLN A 198 UNP Q8NKB0 LYS 198 SEE SEQUENCE DETAILS
SEQADV 5C8Z VAL A 200 UNP Q8NKB0 LEU 200 SEE SEQUENCE DETAILS
SEQADV 5C8Z TRP A 265 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z ASN A 266 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z SER A 267 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z SER A 268 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z SER A 269 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z VAL A 270 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z ASP A 271 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z LYS A 272 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z LEU A 273 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z ALA A 274 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z ALA A 275 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z ALA A 276 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z LEU A 277 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z GLU A 278 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z HIS A 279 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z HIS A 280 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z HIS A 281 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z HIS A 282 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z HIS A 283 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z HIS A 284 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z ILE B 26 UNP Q8NKB0 VAL 26 SEE SEQUENCE DETAILS
SEQADV 5C8Z ALA B 69 UNP Q8NKB0 PRO 69 SEE SEQUENCE DETAILS
SEQADV 5C8Z ILE B 87 UNP Q8NKB0 VAL 87 SEE SEQUENCE DETAILS
SEQADV 5C8Z ASN B 148 UNP Q8NKB0 LYS 148 SEE SEQUENCE DETAILS
SEQADV 5C8Z LEU B 168 UNP Q8NKB0 MET 168 SEE SEQUENCE DETAILS
SEQADV 5C8Z VAL B 170 UNP Q8NKB0 ASP 170 SEE SEQUENCE DETAILS
SEQADV 5C8Z GLN B 198 UNP Q8NKB0 LYS 198 SEE SEQUENCE DETAILS
SEQADV 5C8Z VAL B 200 UNP Q8NKB0 LEU 200 SEE SEQUENCE DETAILS
SEQADV 5C8Z TRP B 265 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z ASN B 266 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z SER B 267 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z SER B 268 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z SER B 269 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z VAL B 270 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z ASP B 271 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z LYS B 272 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z LEU B 273 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z ALA B 274 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z ALA B 275 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z ALA B 276 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z LEU B 277 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z GLU B 278 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z HIS B 279 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z HIS B 280 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z HIS B 281 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z HIS B 282 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z HIS B 283 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C8Z HIS B 284 UNP Q8NKB0 EXPRESSION TAG
SEQRES 1 A 284 MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE
SEQRES 2 A 284 THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP ILE
SEQRES 3 A 284 VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET PHE
SEQRES 4 A 284 ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG
SEQRES 5 A 284 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER ALA
SEQRES 6 A 284 LYS ALA PRO ALA GLU THR TYR THR GLU VAL THR ALA GLN
SEQRES 7 A 284 LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP ALA LEU
SEQRES 8 A 284 ASP ILE LYS HIS ALA THR VAL TRP GLY CYS SER SER GLY
SEQRES 9 A 284 ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP
SEQRES 10 A 284 ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR LYS
SEQRES 11 A 284 LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP
SEQRES 12 A 284 GLU GLU ILE SER ASN ILE LEU ALA ASN VAL MET LEU ASN
SEQRES 13 A 284 ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA LEU GLY
SEQRES 14 A 284 VAL GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL
SEQRES 15 A 284 TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 A 284 PRO VAL GLN ASP VAL GLU ALA LEU ARG GLY LYS PRO LEU
SEQRES 17 A 284 ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE
SEQRES 18 A 284 PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN
SEQRES 19 A 284 ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL SER
SEQRES 20 A 284 HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR
SEQRES 21 A 284 GLN LYS HIS LEU TRP ASN SER SER SER VAL ASP LYS LEU
SEQRES 22 A 284 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 284 MET ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE
SEQRES 2 B 284 THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP ILE
SEQRES 3 B 284 VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MET PHE
SEQRES 4 B 284 ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG
SEQRES 5 B 284 VAL THR THR PHE ASP MET PRO GLY MET SER ARG SER ALA
SEQRES 6 B 284 LYS ALA PRO ALA GLU THR TYR THR GLU VAL THR ALA GLN
SEQRES 7 B 284 LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP ALA LEU
SEQRES 8 B 284 ASP ILE LYS HIS ALA THR VAL TRP GLY CYS SER SER GLY
SEQRES 9 B 284 ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP
SEQRES 10 B 284 ARG ILE ARG ASN ALA MET CYS HIS GLU LEU PRO THR LYS
SEQRES 11 B 284 LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP
SEQRES 12 B 284 GLU GLU ILE SER ASN ILE LEU ALA ASN VAL MET LEU ASN
SEQRES 13 B 284 ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA LEU GLY
SEQRES 14 B 284 VAL GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL
SEQRES 15 B 284 TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 B 284 PRO VAL GLN ASP VAL GLU ALA LEU ARG GLY LYS PRO LEU
SEQRES 17 B 284 ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE
SEQRES 18 B 284 PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN
SEQRES 19 B 284 ILE GLY LEU LEU PRO GLY MET HIS PHE PRO TYR VAL SER
SEQRES 20 B 284 HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR
SEQRES 21 B 284 GLN LYS HIS LEU TRP ASN SER SER SER VAL ASP LYS LEU
SEQRES 22 B 284 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET ZGR A 301 24
HET GOL A 302 6
HET GOL A 303 6
HET FMT A 304 3
HET FMT A 305 3
HET FMT A 306 3
HET K A 307 1
HET ZGR B 301 24
HET GOL B 302 6
HET GOL B 303 6
HET K B 304 1
HETNAM ZGR 2,4-DIHYDROXY-6-[(1E,10S)-10-HYDROXY-6-OXOUNDEC-1-EN-1-
HETNAM 2 ZGR YL]BENZOIC ACID
HETNAM GOL GLYCEROL
HETNAM FMT FORMIC ACID
HETNAM K POTASSIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ZGR 2(C18 H24 O6)
FORMUL 4 GOL 4(C3 H8 O3)
FORMUL 6 FMT 3(C H2 O2)
FORMUL 9 K 2(K 1+)
FORMUL 14 HOH *324(H2 O)
HELIX 1 AA1 GLU A 35 MET A 38 5 4
HELIX 2 AA2 PHE A 39 ALA A 48 1 10
HELIX 3 AA3 MET A 61 ALA A 65 5 5
HELIX 4 AA4 PRO A 68 TYR A 72 5 5
HELIX 5 AA5 THR A 76 LEU A 91 1 16
HELIX 6 AA6 SER A 102 TYR A 115 1 14
HELIX 7 AA7 LEU A 132 ASN A 137 1 6
HELIX 8 AA8 THR A 138 LEU A 141 5 4
HELIX 9 AA9 GLU A 142 ASP A 157 1 16
HELIX 10 AB1 GLY A 161 ALA A 167 1 7
HELIX 11 AB2 GLY A 169 TYR A 187 1 19
HELIX 12 AB3 ILE A 191 ALA A 195 5 5
HELIX 13 AB4 ASP A 199 ARG A 204 1 6
HELIX 14 AB5 PRO A 217 GLY A 232 1 16
HELIX 15 AB6 PHE A 243 HIS A 248 1 6
HELIX 16 AB7 HIS A 248 SER A 267 1 20
HELIX 17 AB8 GLU B 35 MET B 38 5 4
HELIX 18 AB9 PHE B 39 ALA B 48 1 10
HELIX 19 AC1 MET B 61 ALA B 65 5 5
HELIX 20 AC2 PRO B 68 THR B 73 5 6
HELIX 21 AC3 THR B 76 LEU B 91 1 16
HELIX 22 AC4 SER B 102 TYR B 115 1 14
HELIX 23 AC5 LEU B 132 ASN B 137 1 6
HELIX 24 AC6 THR B 138 LEU B 141 5 4
HELIX 25 AC7 GLU B 142 VAL B 158 1 17
HELIX 26 AC8 GLY B 161 ALA B 167 1 7
HELIX 27 AC9 LEU B 168 TYR B 187 1 20
HELIX 28 AD1 ILE B 191 ALA B 195 5 5
HELIX 29 AD2 ASP B 199 ARG B 204 1 6
HELIX 30 AD3 PRO B 217 ALA B 231 1 15
HELIX 31 AD4 PHE B 243 HIS B 248 1 6
HELIX 32 AD5 HIS B 248 SER B 267 1 20
SHEET 1 AA1 8 THR A 3 SER A 8 0
SHEET 2 AA1 8 THR A 14 GLU A 20 -1 O GLN A 19 N THR A 3
SHEET 3 AA1 8 ARG A 52 PHE A 56 -1 O VAL A 53 N GLU A 20
SHEET 4 AA1 8 ASP A 25 VAL A 29 1 N ILE A 26 O ARG A 52
SHEET 5 AA1 8 ALA A 96 CYS A 101 1 O THR A 97 N VAL A 27
SHEET 6 AA1 8 ILE A 119 HIS A 125 1 O MET A 123 N VAL A 98
SHEET 7 AA1 8 LEU A 208 GLY A 213 1 O THR A 211 N CYS A 124
SHEET 8 AA1 8 ASN A 234 LEU A 238 1 O ASN A 234 N TRP A 210
SHEET 1 AA2 8 THR B 3 SER B 8 0
SHEET 2 AA2 8 THR B 14 GLU B 20 -1 O GLN B 19 N THR B 3
SHEET 3 AA2 8 ARG B 52 PHE B 56 -1 O VAL B 53 N GLU B 20
SHEET 4 AA2 8 ASP B 25 VAL B 29 1 N ILE B 26 O ARG B 52
SHEET 5 AA2 8 ALA B 96 CYS B 101 1 O THR B 97 N VAL B 27
SHEET 6 AA2 8 ILE B 119 HIS B 125 1 O MET B 123 N VAL B 98
SHEET 7 AA2 8 LEU B 208 GLY B 213 1 O THR B 211 N CYS B 124
SHEET 8 AA2 8 ASN B 234 LEU B 238 1 O ASN B 234 N TRP B 210
SITE 1 AC1 16 ASP A 31 GLY A 32 SER A 102 SER A 103
SITE 2 AC1 16 LYS A 130 LEU A 132 LEU A 135 MET A 154
SITE 3 AC1 16 TRP A 183 TYR A 187 PRO A 188 ILE A 191
SITE 4 AC1 16 PRO A 192 HIS A 242 PHE A 243 HOH A 439
SITE 1 AC2 8 LEU A 127 PRO A 128 THR A 129 LYS A 130
SITE 2 AC2 8 SER A 220 PHE A 221 ASP A 223 HOH A 515
SITE 1 AC3 3 ARG A 120 HIS A 263 ASN A 266
SITE 1 AC4 6 ASN A 156 ASP A 157 VAL A 158 SER A 159
SITE 2 AC4 6 GLY A 160 MET A 241
SITE 1 AC5 2 TYR A 16 ARG A 63
SITE 1 AC6 4 ASP A 25 ASP A 92 LYS A 94 HIS A 95
SITE 1 AC7 4 HIS A 248 PRO A 249 ASP A 250 VAL A 251
SITE 1 AC8 16 ASP B 31 GLY B 32 SER B 102 SER B 103
SITE 2 AC8 16 LYS B 130 LEU B 132 LEU B 135 MET B 154
SITE 3 AC8 16 TRP B 183 TYR B 187 PRO B 188 ILE B 191
SITE 4 AC8 16 PRO B 192 HIS B 242 PHE B 243 HOH B 455
SITE 1 AC9 7 LEU B 127 PRO B 128 THR B 129 LYS B 130
SITE 2 AC9 7 SER B 220 ASP B 223 HOH B 475
SITE 1 AD1 3 GLY B 60 ALA B 65 TYR B 72
SITE 1 AD2 4 HIS B 248 PRO B 249 ASP B 250 VAL B 251
CRYST1 74.900 89.590 113.790 90.00 90.00 90.00 P 21 21 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 0.013351 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011162 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008788 0.00000
TER 2191 SER A 267
TER 4351 SER B 267
MASTER 382 0 11 32 16 0 20 6 4483 2 81 44
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