HEADER LYASE 30-JAN-09 3G24
TITLE CRYSTAL STRUCTURE OF THE MUTANT D70N OF OROTIDINE 5'-MONOPHOSPHATE
TITLE 2 DECARBOXYLASE FROM METHANOBACTERIUM THERMOAUTOTROPHICUM COMPLEXED
TITLE 3 WITH 6-AZAURIDINE 5'-MONOPHOSPHATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OROTIDINE 5'-PHOSPHATE DECARBOXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: OMP DECARBOXYLASE, OMPDCASE, OMPDECASE;
COMPND 5 EC: 4.1.1.23;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS STR.
SOURCE 3 DELTA H;
SOURCE 4 ORGANISM_TAXID: 187420;
SOURCE 5 GENE: PYRF, MTH_129;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE, 6-AZAUMP, D70N,
KEYWDS 2 DECARBOXYLASE, PYRIMIDINE BIOSYNTHESIS, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.A.FEDOROV,E.V.FEDOROV,K.K.CHAN,J.A.GERLT,S.C.ALMO
REVDAT 3 06-SEP-23 3G24 1 REMARK
REVDAT 2 20-OCT-21 3G24 1 REMARK SEQADV
REVDAT 1 23-JUN-09 3G24 0
JRNL AUTH K.K.CHAN,B.M.WOOD,A.A.FEDOROV,E.V.FEDOROV,H.J.IMKER,
JRNL AUTH 2 T.L.AMYES,J.P.RICHARD,S.C.ALMO,J.A.GERLT
JRNL TITL MECHANISM OF THE OROTIDINE 5'-MONOPHOSPHATE
JRNL TITL 2 DECARBOXYLASE-CATALYZED REACTION: EVIDENCE FOR SUBSTRATE
JRNL TITL 3 DESTABILIZATION.
JRNL REF BIOCHEMISTRY V. 48 5518 2009
JRNL REFN ISSN 0006-2960
JRNL PMID 19435314
JRNL DOI 10.1021/BI900623R
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1094438.690
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 60695
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 SET) : 0.183
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3049
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.55
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 55.60
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3516
REMARK 3 BIN R VALUE (WORKING SET) : 0.2250
REMARK 3 BIN FREE R VALUE : 0.2410
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.70
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 173
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.018
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3299
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.30000
REMARK 3 B22 (A**2) : 1.66000
REMARK 3 B33 (A**2) : 1.64000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.55000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.15
REMARK 3 ESD FROM SIGMAA (A) : 0.08
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.17
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.09
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.200
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.880
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.000 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.480 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.940 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.840 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.41
REMARK 3 BSOL : 49.99
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : UP6_PAR.TXT
REMARK 3 PARAMETER FILE 5 : &_1_PARAMETER_INFILE_5
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : UP6_TOP.TXT
REMARK 3 TOPOLOGY FILE 5 : &_1_TOPOLOGY_INFILE_5
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3G24 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-09.
REMARK 100 THE DEPOSITION ID IS D_1000051326.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X4A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97915
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60695
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.08300
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: BALBES
REMARK 200 STARTING MODEL: 3G1Y
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.1M TRIS, 0.2M
REMARK 280 MAGNESIUM CHLORIDE, PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 31.89100
REMARK 290 SMTRY3 2 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: 4850 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 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 ARG A 2
REMARK 465 SER A 3
REMARK 465 ARG A 4
REMARK 465 ARG A 5
REMARK 465 VAL A 6
REMARK 465 ASP A 7
REMARK 465 LEU A 226
REMARK 465 ASN A 227
REMARK 465 PRO A 228
REMARK 465 MET B 1
REMARK 465 ARG B 2
REMARK 465 SER B 3
REMARK 465 ARG B 4
REMARK 465 ARG B 5
REMARK 465 VAL B 6
REMARK 465 ASP B 7
REMARK 465 VAL B 8
REMARK 465 LEU B 226
REMARK 465 ASN B 227
REMARK 465 PRO B 228
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 ASN A 13 16.50 58.01
REMARK 500 LYS A 72 54.81 35.46
REMARK 500 ALA A 74 51.55 -146.82
REMARK 500 THR A 124 -84.63 -94.28
REMARK 500 PHE A 134 -40.92 -132.66
REMARK 500 ASN B 13 16.85 59.17
REMARK 500 ASP B 39 13.93 -146.48
REMARK 500 ALA B 74 49.48 -147.60
REMARK 500 PHE B 134 -40.06 -130.36
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 UP6 A 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UP6 B 229
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KM0 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF OROTIDINE MONOPHOSPHATE DECARBOXYLASE MUTANT
REMARK 900 D70N COMPLEXED WITH 6-AZAUMP
REMARK 900 RELATED ID: 3G18 RELATED DB: PDB
REMARK 900 RELATED ID: 3G1A RELATED DB: PDB
REMARK 900 RELATED ID: 3G1D RELATED DB: PDB
REMARK 900 RELATED ID: 3G1F RELATED DB: PDB
REMARK 900 RELATED ID: 3G1H RELATED DB: PDB
REMARK 900 RELATED ID: 3G1S RELATED DB: PDB
REMARK 900 RELATED ID: 3G1V RELATED DB: PDB
REMARK 900 RELATED ID: 3G1X RELATED DB: PDB
REMARK 900 RELATED ID: 3G1Y RELATED DB: PDB
REMARK 900 RELATED ID: 3G22 RELATED DB: PDB
REMARK 900 RELATED ID: 3G24 RELATED DB: PDB
DBREF 3G24 A 1 228 UNP O26232 PYRF_METTH 1 228
DBREF 3G24 B 1 228 UNP O26232 PYRF_METTH 1 228
SEQADV 3G24 ASN A 70 UNP O26232 ASP 70 ENGINEERED MUTATION
SEQADV 3G24 PRO A 101 UNP O26232 ARG 101 ENGINEERED MUTATION
SEQADV 3G24 ASN B 70 UNP O26232 ASP 70 ENGINEERED MUTATION
SEQADV 3G24 PRO B 101 UNP O26232 ARG 101 ENGINEERED MUTATION
SEQRES 1 A 228 MET ARG SER ARG ARG VAL ASP VAL MET ASP VAL MET ASN
SEQRES 2 A 228 ARG LEU ILE LEU ALA MET ASP LEU MET ASN ARG ASP ASP
SEQRES 3 A 228 ALA LEU ARG VAL THR GLY GLU VAL ARG GLU TYR ILE ASP
SEQRES 4 A 228 THR VAL LYS ILE GLY TYR PRO LEU VAL LEU SER GLU GLY
SEQRES 5 A 228 MET ASP ILE ILE ALA GLU PHE ARG LYS ARG PHE GLY CYS
SEQRES 6 A 228 ARG ILE ILE ALA ASN PHE LYS VAL ALA ASP ILE PRO GLU
SEQRES 7 A 228 THR ASN GLU LYS ILE CYS ARG ALA THR PHE LYS ALA GLY
SEQRES 8 A 228 ALA ASP ALA ILE ILE VAL HIS GLY PHE PRO GLY ALA ASP
SEQRES 9 A 228 SER VAL ARG ALA CYS LEU ASN VAL ALA GLU GLU MET GLY
SEQRES 10 A 228 ARG GLU VAL PHE LEU LEU THR GLU MET SER HIS PRO GLY
SEQRES 11 A 228 ALA GLU MET PHE ILE GLN GLY ALA ALA ASP GLU ILE ALA
SEQRES 12 A 228 ARG MET GLY VAL ASP LEU GLY VAL LYS ASN TYR VAL GLY
SEQRES 13 A 228 PRO SER THR ARG PRO GLU ARG LEU SER ARG LEU ARG GLU
SEQRES 14 A 228 ILE ILE GLY GLN ASP SER PHE LEU ILE SER PRO GLY VAL
SEQRES 15 A 228 GLY ALA GLN GLY GLY ASP PRO GLY GLU THR LEU ARG PHE
SEQRES 16 A 228 ALA ASP ALA ILE ILE VAL GLY ARG SER ILE TYR LEU ALA
SEQRES 17 A 228 ASP ASN PRO ALA ALA ALA ALA ALA GLY ILE ILE GLU SER
SEQRES 18 A 228 ILE LYS ASP LEU LEU ASN PRO
SEQRES 1 B 228 MET ARG SER ARG ARG VAL ASP VAL MET ASP VAL MET ASN
SEQRES 2 B 228 ARG LEU ILE LEU ALA MET ASP LEU MET ASN ARG ASP ASP
SEQRES 3 B 228 ALA LEU ARG VAL THR GLY GLU VAL ARG GLU TYR ILE ASP
SEQRES 4 B 228 THR VAL LYS ILE GLY TYR PRO LEU VAL LEU SER GLU GLY
SEQRES 5 B 228 MET ASP ILE ILE ALA GLU PHE ARG LYS ARG PHE GLY CYS
SEQRES 6 B 228 ARG ILE ILE ALA ASN PHE LYS VAL ALA ASP ILE PRO GLU
SEQRES 7 B 228 THR ASN GLU LYS ILE CYS ARG ALA THR PHE LYS ALA GLY
SEQRES 8 B 228 ALA ASP ALA ILE ILE VAL HIS GLY PHE PRO GLY ALA ASP
SEQRES 9 B 228 SER VAL ARG ALA CYS LEU ASN VAL ALA GLU GLU MET GLY
SEQRES 10 B 228 ARG GLU VAL PHE LEU LEU THR GLU MET SER HIS PRO GLY
SEQRES 11 B 228 ALA GLU MET PHE ILE GLN GLY ALA ALA ASP GLU ILE ALA
SEQRES 12 B 228 ARG MET GLY VAL ASP LEU GLY VAL LYS ASN TYR VAL GLY
SEQRES 13 B 228 PRO SER THR ARG PRO GLU ARG LEU SER ARG LEU ARG GLU
SEQRES 14 B 228 ILE ILE GLY GLN ASP SER PHE LEU ILE SER PRO GLY VAL
SEQRES 15 B 228 GLY ALA GLN GLY GLY ASP PRO GLY GLU THR LEU ARG PHE
SEQRES 16 B 228 ALA ASP ALA ILE ILE VAL GLY ARG SER ILE TYR LEU ALA
SEQRES 17 B 228 ASP ASN PRO ALA ALA ALA ALA ALA GLY ILE ILE GLU SER
SEQRES 18 B 228 ILE LYS ASP LEU LEU ASN PRO
HET UP6 A 229 21
HET UP6 B 229 21
HETNAM UP6 6-AZA URIDINE 5'-MONOPHOSPHATE
HETSYN UP6 6-AZA-UMP
FORMUL 3 UP6 2(C8 H12 N3 O9 P)
FORMUL 5 HOH *300(H2 O)
HELIX 1 1 VAL A 11 ASN A 13 5 3
HELIX 2 2 ASN A 23 ARG A 35 1 13
HELIX 3 3 TYR A 45 GLY A 52 1 8
HELIX 4 4 MET A 53 PHE A 63 1 11
HELIX 5 5 ILE A 76 ALA A 90 1 15
HELIX 6 6 GLY A 102 GLY A 117 1 16
HELIX 7 7 HIS A 128 MET A 133 5 6
HELIX 8 8 PHE A 134 GLY A 150 1 17
HELIX 9 9 ARG A 160 GLY A 172 1 13
HELIX 10 10 ASP A 188 LEU A 193 1 6
HELIX 11 11 GLY A 202 LEU A 207 1 6
HELIX 12 12 ASN A 210 ILE A 222 1 13
HELIX 13 13 VAL B 11 ASN B 13 5 3
HELIX 14 14 ASN B 23 ARG B 35 1 13
HELIX 15 15 TYR B 45 GLY B 52 1 8
HELIX 16 16 MET B 53 GLY B 64 1 12
HELIX 17 17 ILE B 76 ALA B 90 1 15
HELIX 18 18 GLY B 102 GLY B 117 1 16
HELIX 19 19 HIS B 128 MET B 133 5 6
HELIX 20 20 PHE B 134 GLY B 150 1 17
HELIX 21 21 ARG B 160 GLY B 172 1 13
HELIX 22 22 ASP B 188 LEU B 193 1 6
HELIX 23 23 GLY B 202 LEU B 207 1 6
HELIX 24 24 ASN B 210 ILE B 222 1 13
SHEET 1 A 9 LEU A 15 MET A 19 0
SHEET 2 A 9 THR A 40 GLY A 44 1 O LYS A 42 N LEU A 17
SHEET 3 A 9 ARG A 66 VAL A 73 1 O ARG A 66 N VAL A 41
SHEET 4 A 9 ALA A 94 HIS A 98 1 O ALA A 94 N ALA A 69
SHEET 5 A 9 GLU A 119 LEU A 123 1 O PHE A 121 N VAL A 97
SHEET 6 A 9 ASN A 153 VAL A 155 1 O ASN A 153 N LEU A 122
SHEET 7 A 9 PHE A 176 SER A 179 1 O PHE A 176 N TYR A 154
SHEET 8 A 9 ALA A 198 VAL A 201 1 O ILE A 200 N SER A 179
SHEET 9 A 9 LEU A 15 MET A 19 1 N ILE A 16 O ILE A 199
SHEET 1 B 9 LEU B 15 MET B 19 0
SHEET 2 B 9 THR B 40 GLY B 44 1 O LYS B 42 N LEU B 17
SHEET 3 B 9 ARG B 66 VAL B 73 1 O ARG B 66 N VAL B 41
SHEET 4 B 9 ALA B 94 HIS B 98 1 O ALA B 94 N ALA B 69
SHEET 5 B 9 GLU B 119 LEU B 123 1 O PHE B 121 N VAL B 97
SHEET 6 B 9 ASN B 153 VAL B 155 1 O ASN B 153 N LEU B 122
SHEET 7 B 9 PHE B 176 SER B 179 1 O PHE B 176 N TYR B 154
SHEET 8 B 9 ALA B 198 VAL B 201 1 O ILE B 200 N SER B 179
SHEET 9 B 9 LEU B 15 MET B 19 1 N ILE B 16 O ILE B 199
SITE 1 AC1 19 ASP A 20 LYS A 42 ASN A 70 LYS A 72
SITE 2 AC1 19 MET A 126 SER A 127 PRO A 180 GLN A 185
SITE 3 AC1 19 GLY A 202 ARG A 203 HOH A 240 HOH A 249
SITE 4 AC1 19 HOH A 254 HOH A 261 HOH A 268 HOH A 288
SITE 5 AC1 19 ASP B 75 ILE B 76 THR B 79
SITE 1 AC2 19 ASP A 75 ILE A 76 THR A 79 ASP B 20
SITE 2 AC2 19 LYS B 42 ASN B 70 LYS B 72 MET B 126
SITE 3 AC2 19 SER B 127 PRO B 180 GLN B 185 GLY B 202
SITE 4 AC2 19 ARG B 203 HOH B 237 HOH B 253 HOH B 262
SITE 5 AC2 19 HOH B 265 HOH B 305 HOH B 316
CRYST1 59.592 63.782 61.293 90.00 115.03 90.00 P 1 21 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 0.016781 0.000000 0.007836 0.00000
SCALE2 0.000000 0.015678 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018006 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
