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HEADER HYDROLASE 25-JUN-15 5C81
TITLE ZHD-INTERMEDIATE COMPLEX AFTER ZHD CRYSTAL SOAKING IN ZEN FOR 12MIN
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 5C81 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. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 70897
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.149
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3471
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 47.8566 - 5.2612 1.00 2897 168 0.1709 0.1916
REMARK 3 2 5.2612 - 4.1767 1.00 2784 130 0.1372 0.1601
REMARK 3 3 4.1767 - 3.6490 1.00 2772 129 0.1319 0.1544
REMARK 3 4 3.6490 - 3.3154 1.00 2720 132 0.1472 0.1463
REMARK 3 5 3.3154 - 3.0778 1.00 2737 123 0.1508 0.1636
REMARK 3 6 3.0778 - 2.8964 1.00 2706 147 0.1587 0.1810
REMARK 3 7 2.8964 - 2.7514 1.00 2695 147 0.1526 0.1806
REMARK 3 8 2.7514 - 2.6316 1.00 2709 124 0.1513 0.1977
REMARK 3 9 2.6316 - 2.5303 1.00 2689 147 0.1519 0.1988
REMARK 3 10 2.5303 - 2.4430 1.00 2691 129 0.1472 0.1885
REMARK 3 11 2.4430 - 2.3666 1.00 2689 146 0.1476 0.1769
REMARK 3 12 2.3666 - 2.2990 1.00 2658 150 0.1489 0.1870
REMARK 3 13 2.2990 - 2.2384 1.00 2679 154 0.1429 0.1725
REMARK 3 14 2.2384 - 2.1838 1.00 2676 137 0.1391 0.1611
REMARK 3 15 2.1838 - 2.1342 1.00 2675 128 0.1389 0.1596
REMARK 3 16 2.1342 - 2.0888 1.00 2673 139 0.1453 0.1690
REMARK 3 17 2.0888 - 2.0470 1.00 2663 138 0.1453 0.1833
REMARK 3 18 2.0470 - 2.0084 1.00 2652 146 0.1502 0.1756
REMARK 3 19 2.0084 - 1.9725 1.00 2708 131 0.1441 0.1935
REMARK 3 20 1.9725 - 1.9390 1.00 2672 140 0.1430 0.2419
REMARK 3 21 1.9390 - 1.9078 1.00 2641 137 0.1435 0.1928
REMARK 3 22 1.9078 - 1.8784 1.00 2668 130 0.1427 0.1747
REMARK 3 23 1.8784 - 1.8508 1.00 2652 141 0.1482 0.1682
REMARK 3 24 1.8508 - 1.8247 1.00 2673 130 0.1591 0.1707
REMARK 3 25 1.8247 - 1.8001 1.00 2647 148 0.1795 0.1960
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) : 15.160
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 4448
REMARK 3 ANGLE : 1.058 6107
REMARK 3 CHIRALITY : 0.045 688
REMARK 3 PLANARITY : 0.005 801
REMARK 3 DIHEDRAL : 11.945 1613
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): 18.3287 16.3747 -5.7321
REMARK 3 T TENSOR
REMARK 3 T11: 0.0833 T22: 0.1158
REMARK 3 T33: 0.1200 T12: 0.0035
REMARK 3 T13: -0.0060 T23: -0.0231
REMARK 3 L TENSOR
REMARK 3 L11: 0.2325 L22: 0.6786
REMARK 3 L33: 0.7948 L12: -0.0069
REMARK 3 L13: -0.0336 L23: -0.5041
REMARK 3 S TENSOR
REMARK 3 S11: 0.0112 S12: 0.0124 S13: -0.0037
REMARK 3 S21: -0.0252 S22: 0.0080 S23: 0.0339
REMARK 3 S31: 0.0139 S32: 0.0359 S33: -0.0172
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 5C81 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_1000211196.
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 : 70972
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
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 (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.70
REMARK 200 R MERGE (I) : 0.09500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 22.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 13.30
REMARK 200 R MERGE FOR SHELL (I) : 0.53600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.700
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 37.26500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.46000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.04000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.46000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.26500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.04000
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: 1920 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20540 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 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 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 OD1 ASP B 143 NH2 ARG B 185 2.19
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 -176.42 -65.41
REMARK 500 SER A 62 -124.18 51.96
REMARK 500 SER A 102 -126.97 64.20
REMARK 500 GLU A 126 73.19 47.86
REMARK 500 PRO A 196 37.54 -82.85
REMARK 500 MET A 241 -111.84 -131.25
REMARK 500 ASP B 31 -174.97 -66.29
REMARK 500 SER B 62 -125.07 52.00
REMARK 500 SER B 102 -126.48 64.59
REMARK 500 GLU B 126 73.75 46.34
REMARK 500 PRO B 196 33.96 -86.84
REMARK 500 MET B 241 -109.17 -130.41
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 K A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZFR B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5C7Y RELATED DB: PDB
REMARK 900 5C7Y CONTAINS THE SAME PROTEIN AND 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 5C81 A 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
DBREF 5C81 B 1 264 UNP Q8NKB0 Q8NKB0_BIOOC 1 264
SEQADV 5C81 ILE A 26 UNP Q8NKB0 VAL 26 SEE SEQUENCE DETAILS
SEQADV 5C81 ALA A 69 UNP Q8NKB0 PRO 69 SEE SEQUENCE DETAILS
SEQADV 5C81 ILE A 87 UNP Q8NKB0 VAL 87 SEE SEQUENCE DETAILS
SEQADV 5C81 ASN A 148 UNP Q8NKB0 LYS 148 SEE SEQUENCE DETAILS
SEQADV 5C81 LEU A 168 UNP Q8NKB0 MET 168 SEE SEQUENCE DETAILS
SEQADV 5C81 VAL A 170 UNP Q8NKB0 ASP 170 SEE SEQUENCE DETAILS
SEQADV 5C81 GLN A 198 UNP Q8NKB0 LYS 198 SEE SEQUENCE DETAILS
SEQADV 5C81 VAL A 200 UNP Q8NKB0 LEU 200 SEE SEQUENCE DETAILS
SEQADV 5C81 TRP A 265 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 ASN A 266 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 SER A 267 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 SER A 268 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 SER A 269 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 VAL A 270 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 ASP A 271 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 LYS A 272 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 LEU A 273 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 ALA A 274 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 ALA A 275 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 ALA A 276 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 LEU A 277 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 GLU A 278 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 HIS A 279 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 HIS A 280 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 HIS A 281 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 HIS A 282 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 HIS A 283 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 HIS A 284 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 ILE B 26 UNP Q8NKB0 VAL 26 SEE SEQUENCE DETAILS
SEQADV 5C81 ALA B 69 UNP Q8NKB0 PRO 69 SEE SEQUENCE DETAILS
SEQADV 5C81 ILE B 87 UNP Q8NKB0 VAL 87 SEE SEQUENCE DETAILS
SEQADV 5C81 ASN B 148 UNP Q8NKB0 LYS 148 SEE SEQUENCE DETAILS
SEQADV 5C81 LEU B 168 UNP Q8NKB0 MET 168 SEE SEQUENCE DETAILS
SEQADV 5C81 VAL B 170 UNP Q8NKB0 ASP 170 SEE SEQUENCE DETAILS
SEQADV 5C81 GLN B 198 UNP Q8NKB0 LYS 198 SEE SEQUENCE DETAILS
SEQADV 5C81 VAL B 200 UNP Q8NKB0 LEU 200 SEE SEQUENCE DETAILS
SEQADV 5C81 TRP B 265 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 ASN B 266 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 SER B 267 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 SER B 268 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 SER B 269 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 VAL B 270 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 ASP B 271 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 LYS B 272 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 LEU B 273 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 ALA B 274 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 ALA B 275 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 ALA B 276 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 LEU B 277 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 GLU B 278 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 HIS B 279 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 HIS B 280 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 HIS B 281 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 HIS B 282 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 HIS B 283 UNP Q8NKB0 EXPRESSION TAG
SEQADV 5C81 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 K A 304 1
HET ZFR B 301 21
HET K B 302 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 C3 H8 O3
FORMUL 5 FMT C H2 O2
FORMUL 6 K 2(K 1+)
FORMUL 9 HOH *499(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 268 1 21
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 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 GLY B 232 1 16
HELIX 31 AD4 PHE B 243 HIS B 248 1 6
HELIX 32 AD5 HIS B 248 SER B 269 1 22
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 ASP B 209 N ALA B 122
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 477
SITE 1 AC2 7 GLN A 78 PRO A 193 SER A 194 ALA A 195
SITE 2 AC2 7 GLN A 198 ARG B 189 HOH B 507
SITE 1 AC3 2 GLU A 74 LYS A 79
SITE 1 AC4 4 HIS A 248 PRO A 249 ASP A 250 VAL A 251
SITE 1 AC5 15 ASP B 31 GLY B 32 SER B 102 LYS B 130
SITE 2 AC5 15 LEU B 132 LEU B 135 MET B 154 TRP B 183
SITE 3 AC5 15 TYR B 187 PRO B 188 ILE B 191 PRO B 192
SITE 4 AC5 15 HIS B 242 PHE B 243 HOH B 481
SITE 1 AC6 4 HIS B 248 PRO B 249 ASP B 250 VAL B 251
CRYST1 74.530 90.080 112.920 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 0.013417 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011101 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008856 0.00000
TER 2132 SER A 268
TER 4274 SER B 269
MASTER 353 0 6 32 16 0 13 6 4646 2 51 44
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