HEADER OXIDOREDUCTASE 09-JUL-08 3DQ0
TITLE MAIZE CYTOKININ OXIDASE/DEHYDROGENASE COMPLEXED WITH N6-(3-METHOXY-
TITLE 2 PHENYL)ADENINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYTOKININ DEHYDROGENASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CYTOKININ OXIDASE 1, CKO 1, COX 1, ZMCKX1;
COMPND 5 EC: 1.5.99.12;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ZEA MAYS;
SOURCE 3 ORGANISM_COMMON: MAIZE;
SOURCE 4 ORGANISM_TAXID: 4577;
SOURCE 5 STRAIN: CULTIVAR NOBILIS;
SOURCE 6 GENE: CKX1;
SOURCE 7 EXPRESSION_SYSTEM: YARROWIA LIPOLYTICA;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 4952;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: PO1G;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PINA6703
KEYWDS CYTOKININ OXIDASE/DEHYDROGENASE, FLAVOPROTEIN, FAD, INHIBITOR,
KEYWDS 2 OXIDOREDUCTASE, GLYCOPROTEIN, SECRETED
EXPDTA X-RAY DIFFRACTION
AUTHOR D.KOPECNY,P.BRIOZZO
REVDAT 4 01-NOV-23 3DQ0 1 HETSYN
REVDAT 3 29-JUL-20 3DQ0 1 COMPND REMARK HETNAM LINK
REVDAT 3 2 1 SITE ATOM
REVDAT 2 13-JUL-11 3DQ0 1 VERSN
REVDAT 1 14-JUL-09 3DQ0 0
JRNL AUTH L.SPICHAL,T.WERNER,P.GALUSZKA,T.ZATLOUKAL,D.KOPECNY,
JRNL AUTH 2 P.BRIOZZO,J.NISLER,J.GRUZ,J.FREBORTOVA,T.SCHMULLING,M.STRNAD
JRNL TITL CHARACTERIZATION AND BIOLOGICAL ACTIVITY OF NOVEL
JRNL TITL 2 PURINE-DERIVED INHIBITOR OF CYTOKININ OXIDASE/DEHYDROGENASE
JRNL TITL 3 AND ITS POTENTIAL USE FOR IN VIVO STUDIES
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
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) : 46.18
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 3 NUMBER OF REFLECTIONS : 48202
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) : 0.207
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4821
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) : 2775
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 309
REMARK 3 BIN FREE R VALUE : 0.3330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3800
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 169
REMARK 3 SOLVENT ATOMS : 365
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.99
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.45000
REMARK 3 B22 (A**2) : 2.09000
REMARK 3 B33 (A**2) : -0.64000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.04000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.165
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.148
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.488
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.941
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4138 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5664 ; 1.099 ; 1.994
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 512 ; 5.541 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 180 ;32.136 ;22.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 595 ;13.462 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 37 ;17.535 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 636 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3163 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1899 ; 0.185 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2843 ; 0.303 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 381 ; 0.123 ; 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): 42 ; 0.178 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 18 ; 0.155 ; 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): 2558 ; 0.499 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4000 ; 0.872 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1854 ; 1.123 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1657 ; 1.831 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3DQ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048344.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : BM30A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XSCALE
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 48203
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 46.180
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.9500
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) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.15900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 7.000
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: PDB ENTRY 3BW7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% PEG 1500, 0.5% N-OCTYL BETA-D
REMARK 280 -GLUCOSIDE, TRIS-HCL, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 126.35000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.20000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 126.35000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.20000
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 LEU A 19
REMARK 465 ALA A 20
REMARK 465 ALA A 21
REMARK 465 GLY A 22
REMARK 465 THR A 23
REMARK 465 PRO A 24
REMARK 465 ALA A 25
REMARK 465 LEU A 26
REMARK 465 GLY A 27
REMARK 465 ASP A 28
REMARK 465 ASP A 29
REMARK 465 ARG A 30
REMARK 465 GLY A 31
REMARK 465 PRO A 274
REMARK 465 GLY A 275
REMARK 465 GLY A 276
REMARK 465 GLY A 277
REMARK 465 GLY A 278
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 SER A 106 151.72 -49.62
REMARK 500 ALA A 127 -133.62 -84.00
REMARK 500 ALA A 128 -35.72 -148.18
REMARK 500 TYR A 172 58.69 -92.25
REMARK 500 TYR A 172 59.55 -92.76
REMARK 500 ASN A 181 -71.45 -116.04
REMARK 500 ALA A 182 -52.11 -174.03
REMARK 500 PHE A 363 51.00 -103.14
REMARK 500 VAL A 414 -62.84 -109.38
REMARK 500 ALA A 463 -164.01 60.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 UNIPROT IS VARIANT AT THESE POSITIONS
DBREF 3DQ0 A 19 534 UNP Q9T0N8 CKX1_MAIZE 19 534
SEQADV 3DQ0 ALA A 79 UNP Q9T0N8 GLY 79 SEE REMARK 999
SEQADV 3DQ0 THR A 168 UNP Q9T0N8 ASN 168 SEE REMARK 999
SEQADV 3DQ0 LEU A 254 UNP Q9T0N8 PHE 254 SEE REMARK 999
SEQRES 1 A 516 LEU ALA ALA GLY THR PRO ALA LEU GLY ASP ASP ARG GLY
SEQRES 2 A 516 ARG PRO TRP PRO ALA SER LEU ALA ALA LEU ALA LEU ASP
SEQRES 3 A 516 GLY LYS LEU ARG THR ASP SER ASN ALA THR ALA ALA ALA
SEQRES 4 A 516 SER THR ASP PHE GLY ASN ILE THR SER ALA LEU PRO ALA
SEQRES 5 A 516 ALA VAL LEU TYR PRO SER SER THR ALA ASP LEU VAL ALA
SEQRES 6 A 516 LEU LEU SER ALA ALA ASN SER THR PRO GLY TRP PRO TYR
SEQRES 7 A 516 THR ILE ALA PHE ARG GLY ARG GLY HIS SER LEU MET GLY
SEQRES 8 A 516 GLN ALA PHE ALA PRO GLY GLY VAL VAL VAL ASN MET ALA
SEQRES 9 A 516 SER LEU GLY ASP ALA ALA ALA PRO PRO ARG ILE ASN VAL
SEQRES 10 A 516 SER ALA ASP GLY ARG TYR VAL ASP ALA GLY GLY GLU GLN
SEQRES 11 A 516 VAL TRP ILE ASP VAL LEU ARG ALA SER LEU ALA ARG GLY
SEQRES 12 A 516 VAL ALA PRO ARG SER TRP THR ASP TYR LEU TYR LEU THR
SEQRES 13 A 516 VAL GLY GLY THR LEU SER ASN ALA GLY ILE SER GLY GLN
SEQRES 14 A 516 ALA PHE ARG HIS GLY PRO GLN ILE SER ASN VAL LEU GLU
SEQRES 15 A 516 MET ASP VAL ILE THR GLY HIS GLY GLU MET VAL THR CYS
SEQRES 16 A 516 SER LYS GLN LEU ASN ALA ASP LEU PHE ASP ALA VAL LEU
SEQRES 17 A 516 GLY GLY LEU GLY GLN PHE GLY VAL ILE THR ARG ALA ARG
SEQRES 18 A 516 ILE ALA VAL GLU PRO ALA PRO ALA ARG ALA ARG TRP VAL
SEQRES 19 A 516 ARG LEU VAL TYR THR ASP PHE ALA ALA PHE SER ALA ASP
SEQRES 20 A 516 GLN GLU ARG LEU THR ALA PRO ARG PRO GLY GLY GLY GLY
SEQRES 21 A 516 ALA SER PHE GLY PRO MET SER TYR VAL GLU GLY SER VAL
SEQRES 22 A 516 PHE VAL ASN GLN SER LEU ALA THR ASP LEU ALA ASN THR
SEQRES 23 A 516 GLY PHE PHE THR ASP ALA ASP VAL ALA ARG ILE VAL ALA
SEQRES 24 A 516 LEU ALA GLY GLU ARG ASN ALA THR THR VAL TYR SER ILE
SEQRES 25 A 516 GLU ALA THR LEU ASN TYR ASP ASN ALA THR ALA ALA ALA
SEQRES 26 A 516 ALA ALA VAL ASP GLN GLU LEU ALA SER VAL LEU GLY THR
SEQRES 27 A 516 LEU SER TYR VAL GLU GLY PHE ALA PHE GLN ARG ASP VAL
SEQRES 28 A 516 ALA TYR ALA ALA PHE LEU ASP ARG VAL HIS GLY GLU GLU
SEQRES 29 A 516 VAL ALA LEU ASN LYS LEU GLY LEU TRP ARG VAL PRO HIS
SEQRES 30 A 516 PRO TRP LEU ASN MET PHE VAL PRO ARG SER ARG ILE ALA
SEQRES 31 A 516 ASP PHE ASP ARG GLY VAL PHE LYS GLY ILE LEU GLN GLY
SEQRES 32 A 516 THR ASP ILE VAL GLY PRO LEU ILE VAL TYR PRO LEU ASN
SEQRES 33 A 516 LYS SER MET TRP ASP ASP GLY MET SER ALA ALA THR PRO
SEQRES 34 A 516 SER GLU ASP VAL PHE TYR ALA VAL SER LEU LEU PHE SER
SEQRES 35 A 516 SER VAL ALA PRO ASN ASP LEU ALA ARG LEU GLN GLU GLN
SEQRES 36 A 516 ASN ARG ARG ILE LEU ARG PHE CYS ASP LEU ALA GLY ILE
SEQRES 37 A 516 GLN TYR LYS THR TYR LEU ALA ARG HIS THR ASP ARG SER
SEQRES 38 A 516 ASP TRP VAL ARG HIS PHE GLY ALA ALA LYS TRP ASN ARG
SEQRES 39 A 516 PHE VAL GLU MET LYS ASN LYS TYR ASP PRO LYS ARG LEU
SEQRES 40 A 516 LEU SER PRO GLY GLN ASP ILE PHE ASN
MODRES 3DQ0 ASN A 63 ASN GLYCOSYLATION SITE
MODRES 3DQ0 ASN A 134 ASN GLYCOSYLATION SITE
MODRES 3DQ0 ASN A 294 ASN GLYCOSYLATION SITE
MODRES 3DQ0 ASN A 323 ASN GLYCOSYLATION SITE
MODRES 3DQ0 ASN A 338 ASN GLYCOSYLATION SITE
HET NAG B 1 14
HET NAG B 2 14
HET NAG C 1 14
HET NAG C 2 14
HET NAG A 701 14
HET NAG A 706 14
HET NAG A 708 14
HET FAD A 600 53
HET MZO A 601 18
HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM MZO N-(3-METHOXYPHENYL)-9H-PURIN-6-AMINE
HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-
HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-
HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE
FORMUL 2 NAG 7(C8 H15 N O6)
FORMUL 7 FAD C27 H33 N9 O15 P2
FORMUL 8 MZO C12 H11 N5 O
FORMUL 9 HOH *365(H2 O)
HELIX 1 1 PRO A 35 ASP A 44 1 10
HELIX 2 2 ASP A 50 ALA A 57 1 8
HELIX 3 3 SER A 77 THR A 91 1 15
HELIX 4 4 ALA A 122 ASP A 126 5 5
HELIX 5 5 VAL A 149 ALA A 159 1 11
HELIX 6 6 THR A 174 SER A 180 1 7
HELIX 7 7 GLN A 187 GLY A 192 1 6
HELIX 8 8 PRO A 193 SER A 196 5 4
HELIX 9 9 ASN A 218 LEU A 226 1 9
HELIX 10 10 ASP A 258 ALA A 271 1 14
HELIX 11 11 SER A 296 THR A 304 1 9
HELIX 12 12 THR A 308 ASN A 323 1 16
HELIX 13 13 ALA A 341 GLY A 355 1 15
HELIX 14 14 TYR A 371 ASP A 376 1 6
HELIX 15 15 ASP A 376 LEU A 388 1 13
HELIX 16 16 ARG A 406 VAL A 414 1 9
HELIX 17 17 SER A 436 TRP A 438 5 3
HELIX 18 18 ASN A 465 GLY A 485 1 21
HELIX 19 19 ASP A 497 GLY A 506 1 10
HELIX 20 20 GLY A 506 ASP A 521 1 16
HELIX 21 21 SER A 527 ASP A 531 5 5
SHEET 1 A 4 LEU A 47 ARG A 48 0
SHEET 2 A 4 ALA A 71 LEU A 73 -1 O VAL A 72 N ARG A 48
SHEET 3 A 4 VAL A 117 ASN A 120 1 O ASN A 120 N LEU A 73
SHEET 4 A 4 ILE A 98 ARG A 101 1 N ALA A 99 O VAL A 119
SHEET 1 B 4 ILE A 133 VAL A 135 0
SHEET 2 B 4 TYR A 141 GLY A 145 -1 O ASP A 143 N ASN A 134
SHEET 3 B 4 GLY A 233 PRO A 244 -1 O ILE A 240 N VAL A 142
SHEET 4 B 4 VAL A 162 PRO A 164 -1 N ALA A 163 O GLU A 243
SHEET 1 C 5 ILE A 133 VAL A 135 0
SHEET 2 C 5 TYR A 141 GLY A 145 -1 O ASP A 143 N ASN A 134
SHEET 3 C 5 GLY A 233 PRO A 244 -1 O ILE A 240 N VAL A 142
SHEET 4 C 5 VAL A 198 THR A 205 -1 N GLU A 200 O ARG A 239
SHEET 5 C 5 MET A 210 SER A 214 -1 O VAL A 211 N VAL A 203
SHEET 1 D 4 TYR A 286 VAL A 293 0
SHEET 2 D 4 THR A 326 TYR A 336 -1 O GLU A 331 N GLU A 288
SHEET 3 D 4 ARG A 248 TYR A 256 -1 N VAL A 252 O ALA A 332
SHEET 4 D 4 ALA A 364 ALA A 370 -1 O ARG A 367 N TRP A 251
SHEET 1 E 4 LEU A 428 ASN A 434 0
SHEET 2 E 4 VAL A 451 LEU A 457 -1 O PHE A 452 N LEU A 433
SHEET 3 E 4 LEU A 398 PRO A 403 -1 N LEU A 398 O LEU A 457
SHEET 4 E 4 LYS A 489 THR A 490 -1 O LYS A 489 N PHE A 401
LINK ND2 ASN A 63 C1 NAG A 701 1555 1555 1.45
LINK ND1 HIS A 105 C8M FAD A 600 1555 1555 1.35
LINK ND2 ASN A 134 C1 NAG B 1 1555 1555 1.45
LINK ND2 ASN A 294 C1 NAG C 1 1555 1555 1.44
LINK ND2 ASN A 323 C1 NAG A 706 1555 1555 1.44
LINK ND2 ASN A 338 C1 NAG A 708 1555 1555 1.45
LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.45
LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44
CISPEP 1 ALA A 129 PRO A 130 0 -7.19
CISPEP 2 PRO A 464 ASN A 465 0 -7.52
CRYST1 252.700 50.400 51.000 90.00 93.70 90.00 C 1 2 1 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 0.003957 0.000000 0.000256 0.00000
SCALE2 0.000000 0.019841 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019649 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
