HEADER LYASE 13-DEC-01 1KLY
TITLE OROTIDINE MONOPHOSPHATE DECARBOXYLASE D70G MUTANT COMPLEXED WITH 6-
TITLE 2 AZAUMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OROTIDINE 5'-PHOSPHATE DECARBOXYLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: OMP DECARBOXYLASE; OMPDCASE;
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;
SOURCE 3 ORGANISM_TAXID: 145262;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS TIM BARREL, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.WU,W.GILLON,E.F.PAI
REVDAT 5 14-FEB-24 1KLY 1 REMARK
REVDAT 4 27-OCT-21 1KLY 1 REMARK SEQADV
REVDAT 3 13-JUL-11 1KLY 1 VERSN
REVDAT 2 24-FEB-09 1KLY 1 VERSN
REVDAT 1 28-JUN-02 1KLY 0
JRNL AUTH N.WU,W.GILLON,E.F.PAI
JRNL TITL MAPPING THE ACTIVE SITE-LIGAND INTERACTIONS OF OROTIDINE
JRNL TITL 2 5'-MONOPHOSPHATE DECARBOXYLASE BY CRYSTALLOGRAPHY.
JRNL REF BIOCHEMISTRY V. 41 4002 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11900543
JRNL DOI 10.1021/BI015758P
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
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 : CNS LIBRARY
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.49
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 569291.550
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 98.0
REMARK 3 NUMBER OF REFLECTIONS : 35507
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) : 0.167
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.400
REMARK 3 FREE R VALUE TEST SET COUNT : 2616
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 : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.59
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5366
REMARK 3 BIN R VALUE (WORKING SET) : 0.1780
REMARK 3 BIN FREE R VALUE : 0.2040
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 306
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.012
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1601
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 21
REMARK 3 SOLVENT ATOMS : 217
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 13.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 14.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.69000
REMARK 3 B22 (A**2) : -1.44000
REMARK 3 B33 (A**2) : 2.13000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.14
REMARK 3 ESD FROM SIGMAA (A) : 0.05
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) : 0.16
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.06
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.500
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.260
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) : 1.220 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.810 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.290 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.340 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.39
REMARK 3 BSOL : 49.51
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 : AZA.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : AZA.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KLY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000015092.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-98
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 : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : BEND CYLINDRICAL GE(111)
REMARK 200 MONOCHROMATOR
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 : 35507
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.500
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
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) : 1.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.5
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: TRISODIUM CITRATE, PH 7.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP AT 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 37.06600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 37.06600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 29.19150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.51550
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 29.19150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.51550
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 37.06600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 29.19150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.51550
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 37.06600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 29.19150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 51.51550
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ACTIVE ENZYME IS
REMARK 300 GENERATED BY THE TWO-FOLD AXIS X, -Y, -Z
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 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 58.38300
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 111.19800
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 4760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 103.03100
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 74.13200
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 A3001 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 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 VAL A 8
REMARK 465 MET A 9
REMARK 465 ASP A 10
REMARK 465 LYS A 223
REMARK 465 ASP A 224
REMARK 465 LEU A 225
REMARK 465 LEU A 226
REMARK 465 ASN A 227
REMARK 465 PRO A 228
REMARK 465 GLU A 229
REMARK 465 ASP A 230
REMARK 465 PRO A 231
REMARK 465 ALA A 232
REMARK 465 ALA A 233
REMARK 465 ASN A 234
REMARK 465 LYS A 235
REMARK 465 ALA A 236
REMARK 465 ARG A 237
REMARK 465 LYS A 238
REMARK 465 GLU A 239
REMARK 465 ALA A 240
REMARK 465 GLU A 241
REMARK 465 LEU A 242
REMARK 465 ALA A 243
REMARK 465 ALA A 244
REMARK 465 ALA A 245
REMARK 465 THR A 246
REMARK 465 ALA A 247
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 14.12 59.09
REMARK 500 ASP A 39 1.61 -152.10
REMARK 500 ALA A 74 50.23 -150.29
REMARK 500 THR A 124 -84.90 -91.72
REMARK 500 PHE A 134 -38.28 -132.84
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 2001
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KLZ RELATED DB: PDB
REMARK 900 RELATED ID: 1KM0 RELATED DB: PDB
REMARK 900 RELATED ID: 1KM1 RELATED DB: PDB
REMARK 900 RELATED ID: 1KM2 RELATED DB: PDB
REMARK 900 RELATED ID: 1KM3 RELATED DB: PDB
REMARK 900 RELATED ID: 1KM4 RELATED DB: PDB
REMARK 900 RELATED ID: 1KM5 RELATED DB: PDB
REMARK 900 RELATED ID: 1KM6 RELATED DB: PDB
DBREF 1KLY A 1 228 UNP O26232 PYRF_METTH 1 228
SEQADV 1KLY GLY A 70 UNP O26232 ASP 70 ENGINEERED MUTATION
SEQADV 1KLY PRO A 101 UNP O26232 ARG 101 ENGINEERED MUTATION
SEQADV 1KLY GLU A 229 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY ASP A 230 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY PRO A 231 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY ALA A 232 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY ALA A 233 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY ASN A 234 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY LYS A 235 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY ALA A 236 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY ARG A 237 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY LYS A 238 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY GLU A 239 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY ALA A 240 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY GLU A 241 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY LEU A 242 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY ALA A 243 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY ALA A 244 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY ALA A 245 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY THR A 246 UNP O26232 CLONING ARTIFACT
SEQADV 1KLY ALA A 247 UNP O26232 CLONING ARTIFACT
SEQRES 1 A 247 MET ARG SER ARG ARG VAL ASP VAL MET ASP VAL MET ASN
SEQRES 2 A 247 ARG LEU ILE LEU ALA MET ASP LEU MET ASN ARG ASP ASP
SEQRES 3 A 247 ALA LEU ARG VAL THR GLY GLU VAL ARG GLU TYR ILE ASP
SEQRES 4 A 247 THR VAL LYS ILE GLY TYR PRO LEU VAL LEU SER GLU GLY
SEQRES 5 A 247 MET ASP ILE ILE ALA GLU PHE ARG LYS ARG PHE GLY CYS
SEQRES 6 A 247 ARG ILE ILE ALA GLY PHE LYS VAL ALA ASP ILE PRO GLU
SEQRES 7 A 247 THR ASN GLU LYS ILE CYS ARG ALA THR PHE LYS ALA GLY
SEQRES 8 A 247 ALA ASP ALA ILE ILE VAL HIS GLY PHE PRO GLY ALA ASP
SEQRES 9 A 247 SER VAL ARG ALA CYS LEU ASN VAL ALA GLU GLU MET GLY
SEQRES 10 A 247 ARG GLU VAL PHE LEU LEU THR GLU MET SER HIS PRO GLY
SEQRES 11 A 247 ALA GLU MET PHE ILE GLN GLY ALA ALA ASP GLU ILE ALA
SEQRES 12 A 247 ARG MET GLY VAL ASP LEU GLY VAL LYS ASN TYR VAL GLY
SEQRES 13 A 247 PRO SER THR ARG PRO GLU ARG LEU SER ARG LEU ARG GLU
SEQRES 14 A 247 ILE ILE GLY GLN ASP SER PHE LEU ILE SER PRO GLY VAL
SEQRES 15 A 247 GLY ALA GLN GLY GLY ASP PRO GLY GLU THR LEU ARG PHE
SEQRES 16 A 247 ALA ASP ALA ILE ILE VAL GLY ARG SER ILE TYR LEU ALA
SEQRES 17 A 247 ASP ASN PRO ALA ALA ALA ALA ALA GLY ILE ILE GLU SER
SEQRES 18 A 247 ILE LYS ASP LEU LEU ASN PRO GLU ASP PRO ALA ALA ASN
SEQRES 19 A 247 LYS ALA ARG LYS GLU ALA GLU LEU ALA ALA ALA THR ALA
HET UP6 A2001 29
HETNAM UP6 6-AZA URIDINE 5'-MONOPHOSPHATE
HETSYN UP6 6-AZA-UMP
FORMUL 2 UP6 C8 H12 N3 O9 P
FORMUL 3 HOH *217(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 GLU A 36 ILE A 38 5 3
HELIX 4 4 TYR A 45 GLY A 52 1 8
HELIX 5 5 MET A 53 GLY A 64 1 12
HELIX 6 6 ILE A 76 ALA A 90 1 15
HELIX 7 7 GLY A 102 GLY A 117 1 16
HELIX 8 8 HIS A 128 MET A 133 5 6
HELIX 9 9 PHE A 134 GLY A 150 1 17
HELIX 10 10 ARG A 160 GLY A 172 1 13
HELIX 11 11 ASP A 188 LEU A 193 1 6
HELIX 12 12 GLY A 202 LEU A 207 1 6
HELIX 13 13 ASN A 210 ILE A 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 LEU A 123 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
SITE 1 AC1 19 ASP A 20 LYS A 42 LYS A 72 ASP A 75
SITE 2 AC1 19 ILE A 76 THR A 79 MET A 126 SER A 127
SITE 3 AC1 19 PRO A 180 GLN A 185 GLY A 202 ARG A 203
SITE 4 AC1 19 HOH A3006 HOH A3009 HOH A3011 HOH A3012
SITE 5 AC1 19 HOH A3013 HOH A3014 HOH A3015
CRYST1 58.383 103.031 74.132 90.00 90.00 90.00 C 2 2 21 8
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 0.017128 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009706 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013489 0.00000
(ATOM LINES ARE NOT SHOWN.)
END