HEADER TRANSFERASE 08-JUN-06 2IV7
TITLE CRYSTAL STRUCTURE OF WAAG, A GLYCOSYLTRANSFERASE INVOLVED IN
TITLE 2 LIPOPOLYSACCHARIDE BIOSYNTHESIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOPOLYSACCHARIDE CORE BIOSYNTHESIS PROTEIN RFAG;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: WAAG, GLUCOSYLTRANSFERASE I;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 316407;
SOURCE 4 STRAIN: W3110;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: C41
KEYWDS LIPOPOLYSACCHARIDE BIOSYNTHESIS, LPS, TRANSFERASE, FAMILY GT-4,
KEYWDS 2 GLYCOSYLTRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.MARTINEZ-FLEITES,M.PROCTOR,S.ROBERTS,D.N.BOLAM,H.J.GILBERT,
AUTHOR 2 G.J.DAVIES
REVDAT 4 24-JAN-18 2IV7 1 SOURCE
REVDAT 3 24-FEB-09 2IV7 1 VERSN
REVDAT 2 29-NOV-06 2IV7 1 JRNL
REVDAT 1 11-OCT-06 2IV7 0
JRNL AUTH C.MARTINEZ-FLEITES,M.PROCTOR,S.ROBERTS,D.N.BOLAM,
JRNL AUTH 2 H.J.GILBERT,G.J.DAVIES
JRNL TITL INSIGHTS INTO THE SYNTHESIS OF LIPOPOLYSACCHARIDE AND
JRNL TITL 2 ANTIBIOTICS THROUGH THE STRUCTURES OF TWO RETAINING
JRNL TITL 3 GLYCOSYLTRANSFERASES FROM FAMILY GT4
JRNL REF CHEM.BIOL. V. 13 1143 2006
JRNL REFN ISSN 1074-5521
JRNL PMID 17113996
JRNL DOI 10.1016/J.CHEMBIOL.2006.09.005
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 51242
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) : 0.173
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.201
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2745
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3714
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.1850
REMARK 3 BIN FREE R VALUE SET COUNT : 195
REMARK 3 BIN FREE R VALUE : 0.2200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2937
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 25
REMARK 3 SOLVENT ATOMS : 540
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : -0.01000
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): 0.086
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.086
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.048
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.295
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3054 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4140 ; 1.192 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 369 ; 5.234 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;35.176 ;23.487
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 504 ;11.561 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;14.881 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 441 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2358 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1506 ; 0.194 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2097 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 392 ; 0.120 ; 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): 29 ; 0.227 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 38 ; 0.118 ; 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): 1885 ; 0.735 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2955 ; 1.131 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1314 ; 2.158 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1185 ; 3.176 ; 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 : 1.40
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 2IV7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1290029055.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JAN-06
REMARK 200 TEMPERATURE (KELVIN) : 120.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54088
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 33.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.19000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.600
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 (%): 51.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 6.75, 0.2M NABR,
REMARK 280 15%PEG3350
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 25.34500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.79700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.33200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.79700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.34500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.33200
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: 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 400
REMARK 400 COMPOUND
REMARK 400 INVOLVED IN THE ADDITION OF THE FIRST GLUCOSE RESIDUE TO
REMARK 400 THE LIPOPOLYSACCHARIDE CORE.
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 MSE A 1
REMARK 465 LEU A 372
REMARK 465 ASP A 373
REMARK 465 GLY A 374
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 18 CB
REMARK 470 ARG A 22 CD NE CZ NH1 NH2
REMARK 470 GLN A 53 CG CD OE1 NE2
REMARK 470 ASN A 228 OD1 ND2
REMARK 470 ARG A 240 NE CZ NH1 NH2
REMARK 470 LYS A 333 CD CE NZ
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 204 31.89 -91.31
REMARK 500 ASP A 205 86.64 -151.44
REMARK 500 GLU A 281 110.75 -163.77
REMARK 500 ALA A 283 -78.69 -138.93
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 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2051 DISTANCE = 5.97 ANGSTROMS
REMARK 525 HOH A2059 DISTANCE = 5.82 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UDP A1372
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2IW1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF WAAG, A GLYCOSYLTRANSFERASE INVOLVED IN
REMARK 900 LIPOPOLYSACCHARIDE BIOSYNTHESIS
DBREF 2IV7 A 1 374 UNP P25740 RFAG_ECOLI 1 374
SEQRES 1 A 374 MSE ILE VAL ALA PHE CYS LEU TYR LYS TYR PHE PRO PHE
SEQRES 2 A 374 GLY GLY LEU GLN ARG ASP PHE MSE ARG ILE ALA SER THR
SEQRES 3 A 374 VAL ALA ALA ARG GLY HIS HIS VAL ARG VAL TYR THR GLN
SEQRES 4 A 374 SER TRP GLU GLY ASP CYS PRO LYS ALA PHE GLU LEU ILE
SEQRES 5 A 374 GLN VAL PRO VAL LYS SER HIS THR ASN HIS GLY ARG ASN
SEQRES 6 A 374 ALA GLU TYR TYR ALA TRP VAL GLN ASN HIS LEU LYS GLU
SEQRES 7 A 374 HIS PRO ALA ASP ARG VAL VAL GLY PHE ASN LYS MSE PRO
SEQRES 8 A 374 GLY LEU ASP VAL TYR PHE ALA ALA ASP VAL CYS TYR ALA
SEQRES 9 A 374 GLU LYS VAL ALA GLN GLU LYS GLY PHE LEU TYR ARG LEU
SEQRES 10 A 374 THR SER ARG TYR ARG HIS TYR ALA ALA PHE GLU ARG ALA
SEQRES 11 A 374 THR PHE GLU GLN GLY LYS SER THR LYS LEU MSE MSE LEU
SEQRES 12 A 374 THR ASP LYS GLN ILE ALA ASP PHE GLN LYS HIS TYR GLN
SEQRES 13 A 374 THR GLU PRO GLU ARG PHE GLN ILE LEU PRO PRO GLY ILE
SEQRES 14 A 374 TYR PRO ASP ARG LYS TYR SER GLU GLN ILE PRO ASN SER
SEQRES 15 A 374 ARG GLU ILE TYR ARG GLN LYS ASN GLY ILE LYS GLU GLN
SEQRES 16 A 374 GLN ASN LEU LEU LEU GLN VAL GLY SER ASP PHE GLY ARG
SEQRES 17 A 374 LYS GLY VAL ASP ARG SER ILE GLU ALA LEU ALA SER LEU
SEQRES 18 A 374 PRO GLU SER LEU ARG HIS ASN THR LEU LEU PHE VAL VAL
SEQRES 19 A 374 GLY GLN ASP LYS PRO ARG LYS PHE GLU ALA LEU ALA GLU
SEQRES 20 A 374 LYS LEU GLY VAL ARG SER ASN VAL HIS PHE PHE SER GLY
SEQRES 21 A 374 ARG ASN ASP VAL SER GLU LEU MSE ALA ALA ALA ASP LEU
SEQRES 22 A 374 LEU LEU HIS PRO ALA TYR GLN GLU ALA ALA GLY ILE VAL
SEQRES 23 A 374 LEU LEU GLU ALA ILE THR ALA GLY LEU PRO VAL LEU THR
SEQRES 24 A 374 THR ALA VAL CYS GLY TYR ALA HIS TYR ILE ALA ASP ALA
SEQRES 25 A 374 ASN CYS GLY THR VAL ILE ALA GLU PRO PHE SER GLN GLU
SEQRES 26 A 374 GLN LEU ASN GLU VAL LEU ARG LYS ALA LEU THR GLN SER
SEQRES 27 A 374 PRO LEU ARG MSE ALA TRP ALA GLU ASN ALA ARG HIS TYR
SEQRES 28 A 374 ALA ASP THR GLN ASP LEU TYR SER LEU PRO GLU LYS ALA
SEQRES 29 A 374 ALA ASP ILE ILE THR GLY GLY LEU ASP GLY
MODRES 2IV7 MSE A 21 MET SELENOMETHIONINE
MODRES 2IV7 MSE A 90 MET SELENOMETHIONINE
MODRES 2IV7 MSE A 141 MET SELENOMETHIONINE
MODRES 2IV7 MSE A 142 MET SELENOMETHIONINE
MODRES 2IV7 MSE A 268 MET SELENOMETHIONINE
MODRES 2IV7 MSE A 342 MET SELENOMETHIONINE
HET MSE A 21 8
HET MSE A 90 8
HET MSE A 141 8
HET MSE A 142 8
HET MSE A 268 8
HET MSE A 342 8
HET UDP A1372 25
HETNAM MSE SELENOMETHIONINE
HETNAM UDP URIDINE-5'-DIPHOSPHATE
FORMUL 1 MSE 6(C5 H11 N O2 SE)
FORMUL 2 UDP C9 H14 N2 O12 P2
FORMUL 3 HOH *540(H2 O)
HELIX 1 1 GLY A 14 ARG A 30 1 17
HELIX 2 2 THR A 60 HIS A 79 1 20
HELIX 3 3 CYS A 102 LYS A 111 1 10
HELIX 4 4 GLY A 112 LEU A 117 1 6
HELIX 5 5 THR A 118 GLU A 133 1 16
HELIX 6 6 THR A 144 GLN A 156 1 13
HELIX 7 7 GLU A 158 GLU A 160 5 3
HELIX 8 8 TYR A 170 LYS A 174 5 5
HELIX 9 9 LYS A 174 GLN A 178 5 5
HELIX 10 10 ASN A 181 ASN A 190 1 10
HELIX 11 11 GLY A 210 LEU A 221 1 12
HELIX 12 12 PRO A 222 ASN A 228 1 7
HELIX 13 13 PRO A 239 LEU A 249 1 11
HELIX 14 14 VAL A 251 SER A 253 5 3
HELIX 15 15 ASP A 263 ALA A 271 1 9
HELIX 16 16 GLY A 284 GLY A 294 1 11
HELIX 17 17 TYR A 305 ASN A 313 1 9
HELIX 18 18 SER A 323 GLN A 337 1 15
HELIX 19 19 GLN A 337 GLN A 355 1 19
HELIX 20 20 SER A 359 GLY A 370 1 12
SHEET 1 AA 7 GLU A 50 GLN A 53 0
SHEET 2 AA 7 VAL A 34 THR A 38 1 O VAL A 34 N GLU A 50
SHEET 3 AA 7 VAL A 3 CYS A 6 1 O VAL A 3 N ARG A 35
SHEET 4 AA 7 ARG A 83 GLY A 86 1 O ARG A 83 N ALA A 4
SHEET 5 AA 7 VAL A 95 PHE A 97 1 O VAL A 95 N GLY A 86
SHEET 6 AA 7 LYS A 139 MSE A 142 1 O LYS A 139 N TYR A 96
SHEET 7 AA 7 PHE A 162 ILE A 164 1 O GLN A 163 N MSE A 142
SHEET 1 AB 2 LYS A 9 TYR A 10 0
SHEET 2 AB 2 SER A 40 TRP A 41 1 O SER A 40 N TYR A 10
SHEET 1 AC 6 VAL A 255 PHE A 258 0
SHEET 2 AC 6 THR A 229 VAL A 234 1 O LEU A 231 N HIS A 256
SHEET 3 AC 6 ASN A 197 VAL A 202 1 O ASN A 197 N LEU A 230
SHEET 4 AC 6 LEU A 273 HIS A 276 1 O LEU A 273 N LEU A 200
SHEET 5 AC 6 VAL A 297 THR A 300 1 O LEU A 298 N HIS A 276
SHEET 6 AC 6 GLY A 315 ILE A 318 1 O THR A 316 N THR A 299
LINK C PHE A 20 N MSE A 21 1555 1555 1.33
LINK C MSE A 21 N ARG A 22 1555 1555 1.33
LINK C LYS A 89 N MSE A 90 1555 1555 1.33
LINK C MSE A 90 N PRO A 91 1555 1555 1.34
LINK C LEU A 140 N MSE A 141 1555 1555 1.33
LINK C MSE A 141 N MSE A 142 1555 1555 1.33
LINK C MSE A 142 N LEU A 143 1555 1555 1.33
LINK C LEU A 267 N MSE A 268 1555 1555 1.33
LINK C MSE A 268 N ALA A 269 1555 1555 1.33
LINK C ARG A 341 N MSE A 342 1555 1555 1.34
LINK C MSE A 342 N ALA A 343 1555 1555 1.33
CISPEP 1 GLU A 320 PRO A 321 0 -3.91
SITE 1 AC1 25 PHE A 13 GLY A 14 GLY A 15 ARG A 18
SITE 2 AC1 25 ARG A 173 ARG A 208 LYS A 209 VAL A 234
SITE 3 AC1 25 GLY A 235 GLY A 260 ARG A 261 VAL A 264
SITE 4 AC1 25 GLU A 281 GLY A 284 ILE A 285 VAL A 286
SITE 5 AC1 25 GLU A 289 HOH A2015 HOH A2534 HOH A2535
SITE 6 AC1 25 HOH A2536 HOH A2537 HOH A2538 HOH A2539
SITE 7 AC1 25 HOH A2540
CRYST1 50.690 88.664 89.594 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 0.019728 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011279 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011161 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
