HEADER TRANSFERASE 22-SEP-05 2C1Z
TITLE STRUCTURE AND ACTIVITY OF A FLAVONOID 3-O
TITLE 2 GLUCOSYLTRANSFERASE REVEALS THE BASIS FOR PLANT NATURAL
TITLE 3 PRODUCT MODIFICATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-GLUCOSE FLAVONOID 3-O GLYCOSYLTRANSFERASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.4.1.91;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: VITIS VINIFERA;
SOURCE 3 ORGANISM_COMMON: GRAPE;
SOURCE 4 ORGANISM_TAXID: 29760;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: B834
KEYWDS GLYCOSYLTRANSFERASE, FLAVONOID, WINE, CATALYSIS,
KEYWDS 2 GLYCOSYLATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.OFFEN,C.MARTINEZ-FLEITES,E.KIAT-LIM,M.YANG,B.G.DAVIS,
AUTHOR 2 C.A.TARLING,C.M.FORD,D.J.BOWLES,G.J.DAVIES
REVDAT 4 24-FEB-09 2C1Z 1 VERSN
REVDAT 3 20-DEC-06 2C1Z 1 JRNL
REVDAT 2 22-FEB-06 2C1Z 1 JRNL
REVDAT 1 09-JAN-06 2C1Z 0
JRNL AUTH W.OFFEN,C.MARTINEZ-FLEITES,M.YANG,E.KIAT-LIM,
JRNL AUTH 2 B.G.DAVIS,C.A.TARLING,C.M.FORD,D.J.BOWLES,
JRNL AUTH 3 G.J.DAVIES
JRNL TITL STRUCTURE OF A FLAVONOID GLUCOSYLTRANSFERASE
JRNL TITL 2 REVEALS THE BASIS FOR PLANT NATURAL PRODUCT
JRNL TITL 3 MODIFICATION.
JRNL REF EMBO J. V. 25 1396 2006
JRNL REFN ISSN 0261-4189
JRNL PMID 16482224
JRNL DOI 10.1038/SJ.EMBOJ.7600970
REMARK 2
REMARK 2 RESOLUTION. 1.9 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.78
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 36494
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1951
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2721
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2350
REMARK 3 BIN FREE R VALUE SET COUNT : 126
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3430
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 57
REMARK 3 SOLVENT ATOMS : 306
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.08000
REMARK 3 B33 (A**2) : 0.08000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.159
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.146
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.091
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.986
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.936
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3578 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4871 ; 1.373 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 446 ; 5.518 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 153 ;32.802 ;23.203
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 577 ;14.757 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;15.180 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 543 ; 0.097 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2710 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1712 ; 0.202 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2469 ; 0.304 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 265 ; 0.141 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 37 ; 0.178 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.174 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2275 ; 0.944 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3551 ; 1.472 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1531 ; 2.192 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1315 ; 3.329 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 2C1Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-SEP-05.
REMARK 100 THE PDBE ID CODE IS EBI-25718.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : 120.0
REMARK 200 PH : 7.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36495
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 46.780
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.900
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.33000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.3
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 10000, 0.1M
REMARK 280 BISTRIS-PROPANE PH 7.0, 0.5% PLUCORONIC F-68
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 24.55300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.33500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.76550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.33500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.55300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.76550
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 GENERATING THE BIOMOLECULE
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 2
REMARK 465 GLN A 3
REMARK 465 THR A 4
REMARK 465 THR A 5
REMARK 465 SER A 56
REMARK 465 MET A 57
REMARK 465 PRO A 251
REMARK 465 PRO A 252
REMARK 465 PRO A 253
REMARK 465 VAL A 254
REMARK 465 VAL A 255
REMARK 465 PRO A 256
REMARK 465 ASN A 257
REMARK 465 THR A 258
REMARK 465 THR A 259
REMARK 465 VAL A 456
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 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 18 -142.02 44.99
REMARK 500 THR A 19 78.07 -103.05
REMARK 500 LEU A 173 37.21 -90.12
REMARK 500 ILE A 191 -72.40 -86.18
REMARK 500 ASP A 226 102.32 -161.05
REMARK 500 VAL A 385 -61.75 -103.56
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KMP A1456
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE U2F A1457
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2C1X RELATED DB: PDB
REMARK 900 STRUCTURE AND ACTIVITY OF A FLAVONOID 3-O
REMARK 900 GLUCOSYLTRANSFERASE REVEALS THE BASIS FOR
REMARK 900 PLANT NATURAL PRODUCT MODIFICATION
REMARK 900 RELATED ID: 2C9Z RELATED DB: PDB
REMARK 900 STRUCTURE AND ACTIVITY OF A FLAVONOID 3-0
REMARK 900 GLUCOSYLTRANSFERASE REVEALS THE BASIS FOR
REMARK 900 PLANT NATURAL PRODUCT MODIFICATION
DBREF 2C1Z A 1 456 UNP O22304 O22304_VITVI 1 456
SEQADV 2C1Z VAL A 134 UNP O22304 LEU 134 CONFLICT
SEQRES 1 A 456 MET SER GLN THR THR THR ASN PRO HIS VAL ALA VAL LEU
SEQRES 2 A 456 ALA PHE PRO PHE SER THR HIS ALA ALA PRO LEU LEU ALA
SEQRES 3 A 456 VAL VAL ARG ARG LEU ALA ALA ALA ALA PRO HIS ALA VAL
SEQRES 4 A 456 PHE SER PHE PHE SER THR SER GLN SER ASN ALA SER ILE
SEQRES 5 A 456 PHE HIS ASP SER MET HIS THR MET GLN CYS ASN ILE LYS
SEQRES 6 A 456 SER TYR ASP ILE SER ASP GLY VAL PRO GLU GLY TYR VAL
SEQRES 7 A 456 PHE ALA GLY ARG PRO GLN GLU ASP ILE GLU LEU PHE THR
SEQRES 8 A 456 ARG ALA ALA PRO GLU SER PHE ARG GLN GLY MET VAL MET
SEQRES 9 A 456 ALA VAL ALA GLU THR GLY ARG PRO VAL SER CYS LEU VAL
SEQRES 10 A 456 ALA ASP ALA PHE ILE TRP PHE ALA ALA ASP MET ALA ALA
SEQRES 11 A 456 GLU MET GLY VAL ALA TRP LEU PRO PHE TRP THR ALA GLY
SEQRES 12 A 456 PRO ASN SER LEU SER THR HIS VAL TYR ILE ASP GLU ILE
SEQRES 13 A 456 ARG GLU LYS ILE GLY VAL SER GLY ILE GLN GLY ARG GLU
SEQRES 14 A 456 ASP GLU LEU LEU ASN PHE ILE PRO GLY MET SER LYS VAL
SEQRES 15 A 456 ARG PHE ARG ASP LEU GLN GLU GLY ILE VAL PHE GLY ASN
SEQRES 16 A 456 LEU ASN SER LEU PHE SER ARG MET LEU HIS ARG MET GLY
SEQRES 17 A 456 GLN VAL LEU PRO LYS ALA THR ALA VAL PHE ILE ASN SER
SEQRES 18 A 456 PHE GLU GLU LEU ASP ASP SER LEU THR ASN ASP LEU LYS
SEQRES 19 A 456 SER LYS LEU LYS THR TYR LEU ASN ILE GLY PRO PHE ASN
SEQRES 20 A 456 LEU ILE THR PRO PRO PRO VAL VAL PRO ASN THR THR GLY
SEQRES 21 A 456 CYS LEU GLN TRP LEU LYS GLU ARG LYS PRO THR SER VAL
SEQRES 22 A 456 VAL TYR ILE SER PHE GLY THR VAL THR THR PRO PRO PRO
SEQRES 23 A 456 ALA GLU VAL VAL ALA LEU SER GLU ALA LEU GLU ALA SER
SEQRES 24 A 456 ARG VAL PRO PHE ILE TRP SER LEU ARG ASP LYS ALA ARG
SEQRES 25 A 456 VAL HIS LEU PRO GLU GLY PHE LEU GLU LYS THR ARG GLY
SEQRES 26 A 456 TYR GLY MET VAL VAL PRO TRP ALA PRO GLN ALA GLU VAL
SEQRES 27 A 456 LEU ALA HIS GLU ALA VAL GLY ALA PHE VAL THR HIS CYS
SEQRES 28 A 456 GLY TRP ASN SER LEU TRP GLU SER VAL ALA GLY GLY VAL
SEQRES 29 A 456 PRO LEU ILE CYS ARG PRO PHE PHE GLY ASP GLN ARG LEU
SEQRES 30 A 456 ASN GLY ARG MET VAL GLU ASP VAL LEU GLU ILE GLY VAL
SEQRES 31 A 456 ARG ILE GLU GLY GLY VAL PHE THR LYS SER GLY LEU MET
SEQRES 32 A 456 SER CYS PHE ASP GLN ILE LEU SER GLN GLU LYS GLY LYS
SEQRES 33 A 456 LYS LEU ARG GLU ASN LEU ARG ALA LEU ARG GLU THR ALA
SEQRES 34 A 456 ASP ARG ALA VAL GLY PRO LYS GLY SER SER THR GLU ASN
SEQRES 35 A 456 PHE ILE THR LEU VAL ASP LEU VAL SER LYS PRO LYS ASP
SEQRES 36 A 456 VAL
HET KMP A1456 21
HET U2F A1457 36
HETNAM KMP 3,5,7-TRIHYDROXY-2-(4-HYDROXYPHENYL)-4H-
HETNAM 2 KMP CHROMEN-4-ONE
HETNAM U2F URIDINE-5'-DIPHOSPHATE-2-DEOXY-2-FLUORO-
HETNAM 2 U2F ALPHA-D-GLUCOSE
HETSYN KMP KAEMPHEROL
FORMUL 2 KMP C15 H10 O6
FORMUL 3 U2F C15 H23 F N2 O16 P2
FORMUL 4 HOH *306(H2 O1)
HELIX 1 1 HIS A 20 ALA A 35 1 16
HELIX 2 2 SER A 46 PHE A 53 1 8
HELIX 3 3 GLN A 84 GLY A 110 1 27
HELIX 4 4 PHE A 124 GLY A 133 1 10
HELIX 5 5 GLY A 143 TYR A 152 1 10
HELIX 6 6 TYR A 152 GLY A 161 1 10
HELIX 7 7 PHE A 184 LEU A 187 5 4
HELIX 8 8 SER A 198 LEU A 211 1 14
HELIX 9 9 PRO A 212 ALA A 214 5 3
HELIX 10 10 PHE A 222 LEU A 225 5 4
HELIX 11 11 ASP A 226 LEU A 237 1 12
HELIX 12 12 PRO A 245 THR A 250 1 6
HELIX 13 13 GLY A 260 LYS A 266 1 7
HELIX 14 14 PRO A 285 ARG A 300 1 16
HELIX 15 15 ARG A 308 LEU A 315 5 8
HELIX 16 16 GLY A 318 ARG A 324 1 7
HELIX 17 17 PRO A 334 ALA A 340 1 7
HELIX 18 18 GLY A 352 GLY A 363 1 12
HELIX 19 19 ASP A 374 VAL A 385 1 12
HELIX 20 20 GLU A 393 VAL A 396 5 4
HELIX 21 21 THR A 398 GLN A 412 1 15
HELIX 22 22 GLN A 412 VAL A 433 1 22
HELIX 23 23 GLY A 437 LYS A 452 1 16
SHEET 1 AA 7 ILE A 64 ILE A 69 0
SHEET 2 AA 7 VAL A 39 THR A 45 1 O PHE A 40 N LYS A 65
SHEET 3 AA 7 HIS A 9 LEU A 13 1 O VAL A 10 N SER A 41
SHEET 4 AA 7 CYS A 115 ASP A 119 1 O CYS A 115 N ALA A 11
SHEET 5 AA 7 ALA A 135 TRP A 140 1 O ALA A 135 N LEU A 116
SHEET 6 AA 7 VAL A 217 ILE A 219 1 O PHE A 218 N TRP A 140
SHEET 7 AA 7 TYR A 240 ASN A 242 1 O LEU A 241 N ILE A 219
SHEET 1 AB 6 GLY A 327 VAL A 330 0
SHEET 2 AB 6 PHE A 303 SER A 306 1 O PHE A 303 N MET A 328
SHEET 3 AB 6 VAL A 273 SER A 277 1 O VAL A 274 N ILE A 304
SHEET 4 AB 6 VAL A 344 THR A 349 1 N GLY A 345 O VAL A 273
SHEET 5 AB 6 LEU A 366 CYS A 368 1 O ILE A 367 N THR A 349
SHEET 6 AB 6 GLY A 389 ARG A 391 1 O VAL A 390 N CYS A 368
CISPEP 1 GLY A 244 PRO A 245 0 -1.62
SITE 1 AC1 11 SER A 18 HIS A 20 GLN A 84 ILE A 87
SITE 2 AC1 11 PHE A 121 SER A 146 HIS A 150 GLN A 188
SITE 3 AC1 11 PHE A 200 PHE A 372 HOH A2304
SITE 1 AC2 23 SER A 18 THR A 19 HIS A 20 THR A 141
SITE 2 AC2 23 TYR A 275 SER A 277 THR A 280 SER A 306
SITE 3 AC2 23 TRP A 332 ALA A 333 GLN A 335 HIS A 350
SITE 4 AC2 23 GLY A 352 TRP A 353 ASN A 354 SER A 355
SITE 5 AC2 23 GLU A 358 PHE A 372 ASP A 374 GLN A 375
SITE 6 AC2 23 HOH A2200 HOH A2305 HOH A2306
CRYST1 49.106 93.531 106.670 90.00 90.00 90.00 P 21 21 21 4
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 0.020364 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010692 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009375 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
