HEADER OXIDOREDUCTASE 29-MAY-12 3VTF
TITLE STRUCTURE OF A UDP-GLUCOSE DEHYDROGENASE FROM THE HYPERTHERMOPHILIC
TITLE 2 ARCHAEON PYROBACULUM ISLANDICUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UDP-GLUCOSE 6-DEHYDROGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.1.1.22;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PYROBACULUM ISLANDICUM;
SOURCE 3 ORGANISM_TAXID: 384616;
SOURCE 4 STRAIN: DSM 4184;
SOURCE 5 GENE: PISL_1505;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15
KEYWDS TWO DISCRETE ALPHA/BETA DOMAINS, DEHYDROGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.SAKURABA,T.OHSHIMA,K.YONEDA
REVDAT 3 08-NOV-23 3VTF 1 REMARK SEQADV
REVDAT 2 22-NOV-17 3VTF 1 REMARK
REVDAT 1 19-SEP-12 3VTF 0
JRNL AUTH H.SAKURABA,T.KAWAI,K.YONEDA,T.OHSHIMA
JRNL TITL STRUCTURE OF A UDP-GLUCOSE DEHYDROGENASE FROM THE
JRNL TITL 2 HYPERTHERMOPHILIC ARCHAEON PYROBACULUM ISLANDICUM.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 68 1003 2012
JRNL REFN ESSN 1744-3091
JRNL PMID 22949183
JRNL DOI 10.1107/S1744309112030667
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 3 NUMBER OF REFLECTIONS : 36570
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) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.217
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1826
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2438
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.55
REMARK 3 BIN R VALUE (WORKING SET) : 0.2060
REMARK 3 BIN FREE R VALUE SET COUNT : 136
REMARK 3 BIN FREE R VALUE : 0.2620
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3287
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 185
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.96000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : -0.26000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.149
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.085
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.947
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
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): 3393 ; 0.023 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4597 ; 2.057 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 431 ; 5.527 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 143 ;33.169 ;21.888
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 545 ;14.616 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 36 ;19.836 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 513 ; 0.165 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2570 ; 0.012 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3VTF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-MAY-12.
REMARK 100 THE DEPOSITION ID IS D_1000095478.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-MAR-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-5A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : RHODIUM COATED SILICON SINGLE
REMARK 200 CRYSTAL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36575
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 3GG2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.35
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NACL, HEPES, PH 7.5, SITTING 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 58.82600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.36950
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.82600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 38.36950
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: 8140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 31850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -58.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1102 LIES ON A SPECIAL POSITION.
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
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 TYR A 408 76.34 63.22
REMARK 500 ALA A 422 35.59 -146.24
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 UPG A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1002
DBREF 3VTF A 1 424 UNP A1RUM9 A1RUM9_PYRIL 1 424
SEQADV 3VTF MET A -19 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF GLY A -18 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF SER A -17 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF SER A -16 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF HIS A -15 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF HIS A -14 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF HIS A -13 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF HIS A -12 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF HIS A -11 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF HIS A -10 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF SER A -9 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF SER A -8 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF GLY A -7 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF LEU A -6 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF VAL A -5 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF PRO A -4 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF ARG A -3 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF GLY A -2 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF SER A -1 UNP A1RUM9 EXPRESSION TAG
SEQADV 3VTF HIS A 0 UNP A1RUM9 EXPRESSION TAG
SEQRES 1 A 444 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 444 LEU VAL PRO ARG GLY SER HIS MET ALA SER LEU SER VAL
SEQRES 3 A 444 LEU GLY LEU GLY TYR VAL GLY VAL VAL HIS ALA VAL GLY
SEQRES 4 A 444 PHE ALA LEU LEU GLY HIS ARG VAL VAL GLY TYR ASP VAL
SEQRES 5 A 444 ASN PRO SER ILE VAL GLU ARG LEU ARG ALA GLY ARG PRO
SEQRES 6 A 444 HIS ILE TYR GLU PRO GLY LEU GLU GLU ALA LEU GLY ARG
SEQRES 7 A 444 ALA LEU SER SER GLY ARG LEU SER PHE ALA GLU SER ALA
SEQRES 8 A 444 GLU GLU ALA VAL ALA ALA THR ASP ALA THR PHE ILE ALA
SEQRES 9 A 444 VAL GLY THR PRO PRO ALA PRO ASP GLY SER ALA ASP LEU
SEQRES 10 A 444 ARG TYR VAL GLU ALA ALA ALA ARG ALA VAL GLY ARG GLY
SEQRES 11 A 444 ILE ARG ALA LYS GLY ARG TRP HIS LEU VAL VAL VAL LYS
SEQRES 12 A 444 SER THR VAL PRO PRO GLY THR THR GLU GLY LEU VAL ALA
SEQRES 13 A 444 ARG ALA VAL ALA GLU GLU ALA GLY GLY VAL LYS PHE SER
SEQRES 14 A 444 VAL ALA SER ASN PRO GLU PHE LEU ARG GLU GLY SER ALA
SEQRES 15 A 444 LEU GLU ASP PHE PHE LYS PRO ASP ARG ILE VAL ILE GLY
SEQRES 16 A 444 ALA GLY ASP GLU ARG ALA ALA SER PHE LEU LEU ASP VAL
SEQRES 17 A 444 TYR LYS ALA VAL ASP ALA PRO LYS LEU VAL MET LYS PRO
SEQRES 18 A 444 ARG GLU ALA GLU LEU VAL LYS TYR ALA SER ASN VAL PHE
SEQRES 19 A 444 LEU ALA LEU LYS ILE SER PHE ALA ASN GLU VAL GLY LEU
SEQRES 20 A 444 LEU ALA LYS ARG LEU GLY VAL ASP THR TYR ARG VAL PHE
SEQRES 21 A 444 GLU ALA VAL GLY LEU ASP LYS ARG ILE GLY ARG HIS TYR
SEQRES 22 A 444 PHE GLY ALA GLY LEU GLY PHE GLY GLY SER CYS PHE PRO
SEQRES 23 A 444 LYS ASP THR LEU ALA PHE ILE ARG PHE GLY GLU SER LEU
SEQRES 24 A 444 GLY LEU GLU MET ALA ILE SER LYS ALA VAL LEU ARG VAL
SEQRES 25 A 444 ASN GLU TYR MET PRO ARG TYR ALA VAL GLN LEU LEU GLU
SEQRES 26 A 444 GLU ARG LEU GLY GLY LEU ARG GLY ARG HIS VAL GLY VAL
SEQRES 27 A 444 LEU GLY LEU ALA PHE LYS PRO ASN THR ASP ASP VAL ARG
SEQRES 28 A 444 GLU SER ARG GLY VAL GLU VAL ALA ARG LEU LEU LEU GLU
SEQRES 29 A 444 ARG GLY ALA ARG VAL TYR VAL HIS ASP PRO MET ALA MET
SEQRES 30 A 444 GLU LYS ALA ARG ALA VAL LEU GLY ASP SER VAL THR TYR
SEQRES 31 A 444 VAL GLU ASP PRO GLN ALA LEU LEU ASP GLN VAL GLU GLY
SEQRES 32 A 444 VAL ILE ILE ALA THR ALA TRP PRO GLN TYR GLU GLY LEU
SEQRES 33 A 444 ASP TYR ARG GLY LYS VAL VAL VAL ASP GLY ARG TYR VAL
SEQRES 34 A 444 LYS LYS ALA ARG GLU ALA LYS ILE TYR GLU GLY VAL ALA
SEQRES 35 A 444 TRP ALA
HET UPG A1001 36
HET EDO A1002 4
HETNAM UPG URIDINE-5'-DIPHOSPHATE-GLUCOSE
HETNAM EDO 1,2-ETHANEDIOL
HETSYN UPG URIDINE-5'-MONOPHOSPHATE GLUCOPYRANOSYL-MONOPHOSPHATE
HETSYN 2 UPG ESTER
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 UPG C15 H24 N2 O17 P2
FORMUL 3 EDO C2 H6 O2
FORMUL 4 HOH *185(H2 O)
HELIX 1 1 GLY A 10 GLY A 24 1 15
HELIX 2 2 ASN A 33 ALA A 42 1 10
HELIX 3 3 GLY A 51 SER A 62 1 12
HELIX 4 4 SER A 70 ALA A 77 1 8
HELIX 5 5 LEU A 97 GLY A 115 1 19
HELIX 6 6 GLY A 133 GLU A 141 1 9
HELIX 7 7 SER A 161 LYS A 168 1 8
HELIX 8 8 ASP A 178 TYR A 189 1 12
HELIX 9 9 LYS A 200 LEU A 232 1 33
HELIX 10 10 ASP A 235 LEU A 245 1 11
HELIX 11 11 CYS A 264 LEU A 279 1 16
HELIX 12 12 MET A 283 GLY A 309 1 27
HELIX 13 13 SER A 333 ARG A 345 1 13
HELIX 14 14 ALA A 356 GLY A 365 1 10
HELIX 15 15 ASP A 366 VAL A 368 5 3
HELIX 16 16 ASP A 373 VAL A 381 1 9
HELIX 17 17 TRP A 390 LEU A 396 5 7
HELIX 18 18 VAL A 409 ALA A 415 5 7
SHEET 1 A 8 LEU A 65 PHE A 67 0
SHEET 2 A 8 ARG A 26 TYR A 30 1 N GLY A 29 O SER A 66
SHEET 3 A 8 SER A 3 LEU A 7 1 N LEU A 4 O ARG A 26
SHEET 4 A 8 ALA A 80 ILE A 83 1 O PHE A 82 N SER A 5
SHEET 5 A 8 LEU A 119 VAL A 122 1 O VAL A 121 N ILE A 83
SHEET 6 A 8 SER A 149 SER A 152 1 O SER A 149 N VAL A 120
SHEET 7 A 8 ILE A 172 ALA A 176 -1 O GLY A 175 N SER A 152
SHEET 8 A 8 LYS A 196 MET A 199 1 O LEU A 197 N ILE A 172
SHEET 1 B 6 THR A 369 TYR A 370 0
SHEET 2 B 6 ARG A 348 HIS A 352 1 N VAL A 351 O THR A 369
SHEET 3 B 6 HIS A 315 LEU A 319 1 N VAL A 316 O ARG A 348
SHEET 4 B 6 GLY A 383 ILE A 386 1 O GLY A 383 N GLY A 317
SHEET 5 B 6 VAL A 402 ASP A 405 1 O VAL A 404 N VAL A 384
SHEET 6 B 6 ILE A 417 GLY A 420 1 O GLU A 419 N VAL A 403
SITE 1 AC1 25 GLU A 155 PHE A 156 LEU A 157 ARG A 158
SITE 2 AC1 25 GLU A 159 LYS A 208 ASN A 212 ILE A 219
SITE 3 AC1 25 ARG A 248 TYR A 253 GLY A 255 GLY A 259
SITE 4 AC1 25 PHE A 260 GLY A 261 CYS A 264 PHE A 265
SITE 5 AC1 25 PHE A 323 LYS A 324 ARG A 407 HOH A1114
SITE 6 AC1 25 HOH A1123 HOH A1127 HOH A1142 HOH A1177
SITE 7 AC1 25 HOH A1226
SITE 1 AC2 6 GLY A 144 GLY A 145 GLY A 400 LYS A 416
SITE 2 AC2 6 HOH A1146 HOH A1278
CRYST1 117.652 76.739 75.551 90.00 125.80 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 0.008500 0.000000 0.006130 0.00000
SCALE2 0.000000 0.013031 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016319 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
