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HEADER HYDROLASE 25-JUN-15 5C7Y
TITLE ZHD-INTERMEDIATE COMPLEX AFTER ZHD CRYSTAL SOAKING IN ZEN FOR 9MIN
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 1 29-JUN-16 5C7Y 0
JRNL AUTH D.-M.MING,Q.QI,W.-J.YANG,K.-L.SUN,T.-Y.XU,Q.HUANG,X.-J.HU,
JRNL AUTH 2 H.LV
JRNL TITL A CASE STUDY OF LACTONASE ZHD
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.86
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 76860
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) : 0.153
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3839
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 47.8807 - 5.2478 0.99 2887 163 0.1965 0.1972
REMARK 3 2 5.2478 - 4.1661 1.00 2826 109 0.1598 0.2045
REMARK 3 3 4.1661 - 3.6397 0.97 2689 157 0.1424 0.1627
REMARK 3 4 3.6397 - 3.3070 0.98 2701 145 0.1443 0.1853
REMARK 3 5 3.3070 - 3.0700 0.99 2721 146 0.1459 0.1574
REMARK 3 6 3.0700 - 2.8890 0.99 2704 148 0.1530 0.1729
REMARK 3 7 2.8890 - 2.7444 0.99 2703 153 0.1441 0.1781
REMARK 3 8 2.7444 - 2.6249 1.00 2732 113 0.1504 0.1901
REMARK 3 9 2.6249 - 2.5239 0.99 2719 130 0.1551 0.1927
REMARK 3 10 2.5239 - 2.4368 1.00 2687 155 0.1499 0.1665
REMARK 3 11 2.4368 - 2.3606 1.00 2693 137 0.1470 0.1861
REMARK 3 12 2.3606 - 2.2931 1.00 2684 143 0.1485 0.1943
REMARK 3 13 2.2931 - 2.2327 1.00 2708 135 0.1441 0.1675
REMARK 3 14 2.2327 - 2.1783 1.00 2693 148 0.1405 0.1653
REMARK 3 15 2.1783 - 2.1288 1.00 2680 145 0.1405 0.1588
REMARK 3 16 2.1288 - 2.0835 1.00 2656 145 0.1496 0.1809
REMARK 3 17 2.0835 - 2.0418 1.00 2724 137 0.1416 0.1789
REMARK 3 18 2.0418 - 2.0032 1.00 2687 131 0.1435 0.1709
REMARK 3 19 2.0032 - 1.9675 1.00 2659 175 0.1397 0.1718
REMARK 3 20 1.9675 - 1.9341 1.00 2698 143 0.1421 0.1735
REMARK 3 21 1.9341 - 1.9029 1.00 2665 153 0.1481 0.1829
REMARK 3 22 1.9029 - 1.8736 1.00 2647 131 0.1505 0.2228
REMARK 3 23 1.8736 - 1.8461 1.00 2716 153 0.1595 0.1997
REMARK 3 24 1.8461 - 1.8201 1.00 2663 134 0.1609 0.1889
REMARK 3 25 1.8201 - 1.7955 1.00 2679 142 0.1801 0.2029
REMARK 3 26 1.7955 - 1.7722 1.00 2711 135 0.1792 0.2250
REMARK 3 27 1.7722 - 1.7500 1.00 2689 133 0.1812 0.2194
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.030
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 : 0.007 4586
REMARK 3 ANGLE : 1.061 6297
REMARK 3 CHIRALITY : 0.045 696
REMARK 3 PLANARITY : 0.005 836
REMARK 3 DIHEDRAL : 12.673 1679
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): 18.3745 16.0038 -5.8549
REMARK 3 T TENSOR
REMARK 3 T11: 0.0662 T22: 0.0960
REMARK 3 T33: 0.0998 T12: 0.0004
REMARK 3 T13: -0.0020 T23: -0.0225
REMARK 3 L TENSOR
REMARK 3 L11: 0.1781 L22: 0.5908
REMARK 3 L33: 0.7104 L12: 0.0496
REMARK 3 L13: -0.0793 L23: -0.4330
REMARK 3 S TENSOR
REMARK 3 S11: 0.0161 S12: 0.0100 S13: 0.0007
REMARK 3 S21: -0.0026 S22: 0.0047 S23: 0.0220
REMARK 3 S31: -0.0109 S32: 0.0284 S33: -0.0188
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 5C7Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000211190.
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 : 76939
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
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 (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.84
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 0.47900
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 37.34500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.60000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.83500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.60000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.34500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.83500
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: 2850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 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 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: 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 NE2 GLN B 37 O HOH B 401 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG A 185 C GLY A 186 N 0.144
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 186 C - N - CA ANGL. DEV. = -14.3 DEGREES
REMARK 500 GLY A 186 C - N - CA ANGL. DEV. = -13.0 DEGREES
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 ASP A 31 -176.12 -65.94
REMARK 500 SER A 62 -124.14 51.26
REMARK 500 SER A 102 -127.33 66.16
REMARK 500 GLU A 126 73.93 45.77
REMARK 500 PRO A 196 46.85 -78.72
REMARK 500 MET A 241 -110.48 -130.43
REMARK 500 ASP B 31 -173.65 -69.21
REMARK 500 SER B 62 -124.54 51.62
REMARK 500 SER B 102 -127.56 65.17
REMARK 500 GLU B 126 71.38 47.63
REMARK 500 PRO B 196 43.82 -81.75
REMARK 500 MET B 241 -106.66 -129.55
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 ZFR AND FMT ARE USED TO SIMULATE THE INTERMEDIATE IN THE CRYSTAL
REMARK 600 STRUCTURE.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZFR 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 FMT 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 K A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZFR B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 305
REMARK 900
REMARK 900 RELATED ENTRIES
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 900 RELATED ID: 5C8Z RELATED DB: PDB
REMARK 900 5C8Z CONTAINS THE SAME PROTEIN COMPLEXED WITH ZGR.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE STRAIN OF CLONOSTACHYS ROSEA IS DIFFERENT FROM UNP Q8NKB0.
DBREF 5C7Y A 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
DBREF 5C7Y B 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
SEQADV 5C7Y ILE A 26 UNP Q8NKB0 VAL 26 SEE SEQUENCE DETAILS
SEQADV 5C7Y ALA A 69 UNP Q8NKB0 PRO 69 SEE SEQUENCE DETAILS
SEQADV 5C7Y ILE A 87 UNP Q8NKB0 VAL 87 SEE SEQUENCE DETAILS
SEQADV 5C7Y ASN A 148 UNP Q8NKB0 LYS 148 SEE SEQUENCE DETAILS
SEQADV 5C7Y LEU A 168 UNP Q8NKB0 MET 168 SEE SEQUENCE DETAILS
SEQADV 5C7Y VAL A 170 UNP Q8NKB0 ASP 170 SEE SEQUENCE DETAILS
SEQADV 5C7Y GLN A 198 UNP Q8NKB0 LYS 198 SEE SEQUENCE DETAILS
SEQADV 5C7Y VAL A 200 UNP Q8NKB0 LEU 200 SEE SEQUENCE DETAILS
SEQADV 5C7Y TRP A 265 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y ASN A 266 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y SER A 267 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y SER A 268 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y SER A 269 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y VAL A 270 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y ASP A 271 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y LYS A 272 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y LEU A 273 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y ALA A 274 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y ALA A 275 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y ALA A 276 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y LEU A 277 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y GLU A 278 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y HIS A 279 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y HIS A 280 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y HIS A 281 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y HIS A 282 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y HIS A 283 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y HIS A 284 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y ILE B 26 UNP Q8NKB0 VAL 26 SEE SEQUENCE DETAILS
SEQADV 5C7Y ALA B 69 UNP Q8NKB0 PRO 69 SEE SEQUENCE DETAILS
SEQADV 5C7Y ILE B 87 UNP Q8NKB0 VAL 87 SEE SEQUENCE DETAILS
SEQADV 5C7Y ASN B 148 UNP Q8NKB0 LYS 148 SEE SEQUENCE DETAILS
SEQADV 5C7Y LEU B 168 UNP Q8NKB0 MET 168 SEE SEQUENCE DETAILS
SEQADV 5C7Y VAL B 170 UNP Q8NKB0 ASP 170 SEE SEQUENCE DETAILS
SEQADV 5C7Y GLN B 198 UNP Q8NKB0 LYS 198 SEE SEQUENCE DETAILS
SEQADV 5C7Y VAL B 200 UNP Q8NKB0 LEU 200 SEE SEQUENCE DETAILS
SEQADV 5C7Y TRP B 265 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y ASN B 266 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y SER B 267 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y SER B 268 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y SER B 269 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y VAL B 270 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y ASP B 271 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y LYS B 272 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y LEU B 273 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y ALA B 274 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y ALA B 275 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y ALA B 276 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y LEU B 277 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y GLU B 278 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y HIS B 279 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y HIS B 280 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y HIS B 281 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y HIS B 282 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y HIS B 283 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C7Y 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 ZFR A 301 21
HET GOL A 302 6
HET FMT A 303 3
HET FMT A 304 3
HET K A 305 1
HET ZFR B 301 21
HET GOL B 302 6
HET GOL B 303 6
HET FMT B 304 3
HET K B 305 1
HETNAM ZFR (1E,10S)-1-(3,5-DIHYDROXYPHENYL)-10-HYDROXYUNDEC-1-EN-
HETNAM 2 ZFR 6-ONE
HETNAM GOL GLYCEROL
HETNAM FMT FORMIC ACID
HETNAM K POTASSIUM ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ZFR 2(C17 H24 O4)
FORMUL 4 GOL 3(C3 H8 O3)
FORMUL 5 FMT 3(C H2 O2)
FORMUL 7 K 2(K 1+)
FORMUL 13 HOH *403(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 ALA A 231 1 15
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 TYR B 72 5 5
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 GLY B 169 TYR B 187 1 19
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 268 1 21
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 LEU A 28 O THR A 54
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 15 ASP A 31 GLY A 32 SER A 102 LYS A 130
SITE 2 AC1 15 LEU A 132 LEU A 135 MET A 154 TRP A 183
SITE 3 AC1 15 TYR A 187 PRO A 188 ILE A 191 PRO A 192
SITE 4 AC1 15 HIS A 242 PHE A 243 HOH A 487
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 527
SITE 1 AC3 2 GLN A 166 HOH A 441
SITE 1 AC4 2 GLU A 74 LYS A 79
SITE 1 AC5 4 HIS A 248 PRO A 249 ASP A 250 VAL A 251
SITE 1 AC6 15 ASP B 31 GLY B 32 SER B 102 LYS B 130
SITE 2 AC6 15 LEU B 132 LEU B 135 MET B 154 TRP B 183
SITE 3 AC6 15 TYR B 187 PRO B 188 ILE B 191 PRO B 192
SITE 4 AC6 15 HIS B 242 PHE B 243 HOH B 455
SITE 1 AC7 8 LEU B 127 PRO B 128 THR B 129 LYS B 130
SITE 2 AC7 8 SER B 220 PHE B 221 ASP B 223 HOH B 530
SITE 1 AC8 8 ARG A 189 THR A 190 HOH A 489 GLN B 78
SITE 2 AC8 8 PRO B 193 SER B 194 ALA B 195 HOH B 509
SITE 1 AC9 3 ASP B 89 ASP B 92 LYS B 94
SITE 1 AD1 4 HIS B 248 PRO B 249 ASP B 250 VAL B 251
CRYST1 74.690 89.670 113.200 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 0.013389 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011152 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008834 0.00000
TER 2201 SER A 267
TER 4387 SER B 268
MASTER 413 0 10 32 16 0 19 6 4556 2 69 44
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