HEADER LYASE 14-JUL-04 1U11
TITLE PURE (N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE MUTASE) FROM THE
TITLE 2 ACIDOPHILE ACETOBACTER ACETI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PURE (N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE MUTASE);
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACETOBACTER ACETI;
SOURCE 3 ORGANISM_TAXID: 435;
SOURCE 4 GENE: PURE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-23A
KEYWDS ACIDOPHILE, PURE, PROTEIN STABILITY, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.C.SETTEMBRE,J.R.CHITTULURU,C.P.MILL,T.J.KAPPOCK,S.E.EALICK
REVDAT 4 14-FEB-24 1U11 1 REMARK
REVDAT 3 13-JUL-11 1U11 1 VERSN
REVDAT 2 24-FEB-09 1U11 1 VERSN
REVDAT 1 28-SEP-04 1U11 0
JRNL AUTH E.C.SETTEMBRE,J.R.CHITTULURU,C.P.MILL,T.J.KAPPOCK,S.E.EALICK
JRNL TITL ACIDOPHILIC ADAPTATIONS IN THE STRUCTURE OF ACETOBACTER
JRNL TITL 2 ACETI N5-CARBOXYAMINOIMIDAZOLE RIBONUCLEOTIDE MUTASE (PURE).
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 60 1753 2004
JRNL REFN ISSN 0907-4449
JRNL PMID 15388921
JRNL DOI 10.1107/S090744490401858X
REMARK 2
REMARK 2 RESOLUTION. 1.55 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 : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 59415
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : RANDOM
REMARK 3 FREE R VALUE TEST SET SELECTION : THROUGHOUT
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5941
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2326
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 262
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U11 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000023111.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-SEP-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59415
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.550
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 (%) : 99.8
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) : 1.55
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.60
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: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG4K, 0.19 M AMMONIUM ACETATE, 90
REMARK 280 MM CITRATE, PH 5.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-Z+1/2
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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 49.62500
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 49.62500
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 82.40500
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 49.62500
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 49.62500
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 82.40500
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 49.62500
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 49.62500
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 82.40500
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 49.62500
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 49.62500
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 82.40500
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 49.62500
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 49.62500
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 82.40500
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 49.62500
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 49.62500
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 82.40500
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 49.62500
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 49.62500
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 82.40500
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 49.62500
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 49.62500
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 82.40500
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: OCTAMER
REMARK 300 GENERATED WITH
REMARK 300 X,Y,Z AND
REMARK 300 Y,-X+1,Z AND
REMARK 300 -Y+1,X,Z AND
REMARK 300 -X+1,-Y+1,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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 35420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 99.25000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 99.25000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 99.25000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 99.25000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 73940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 71230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -344.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 99.25000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 99.25000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 99.25000
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 99.25000
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 5 -1.000000 0.000000 0.000000 99.25000
REMARK 350 BIOMT2 5 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 5 0.000000 0.000000 -1.000000 -329.62000
REMARK 350 BIOMT1 6 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 6 0.000000 -1.000000 0.000000 99.25000
REMARK 350 BIOMT3 6 0.000000 0.000000 -1.000000 -329.62000
REMARK 350 BIOMT1 7 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 7 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 7 0.000000 0.000000 -1.000000 -329.62000
REMARK 350 BIOMT1 8 0.000000 -1.000000 0.000000 99.25000
REMARK 350 BIOMT2 8 -1.000000 0.000000 0.000000 99.25000
REMARK 350 BIOMT3 8 0.000000 0.000000 -1.000000 -329.62000
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 A 680 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 SER A 2
REMARK 465 GLU A 3
REMARK 465 THR A 4
REMARK 465 ALA A 5
REMARK 465 PRO A 6
REMARK 465 LEU A 7
REMARK 465 PRO A 8
REMARK 465 SER A 9
REMARK 465 ALA A 10
REMARK 465 SER A 11
REMARK 465 SER A 12
REMARK 465 ALA A 13
REMARK 465 LEU A 14
REMARK 465 GLU A 15
REMARK 465 ASP A 16
REMARK 465 LYS A 17
REMARK 465 ALA A 18
REMARK 465 ALA A 19
REMARK 465 THR A 179
REMARK 465 GLU A 180
REMARK 465 ASP A 181
REMARK 465 LYS A 182
REMARK 465 MET B 1
REMARK 465 SER B 2
REMARK 465 GLU B 3
REMARK 465 THR B 4
REMARK 465 ALA B 5
REMARK 465 PRO B 6
REMARK 465 LEU B 7
REMARK 465 PRO B 8
REMARK 465 SER B 9
REMARK 465 ALA B 10
REMARK 465 SER B 11
REMARK 465 SER B 12
REMARK 465 ALA B 13
REMARK 465 LEU B 14
REMARK 465 GLU B 15
REMARK 465 ASP B 16
REMARK 465 LYS B 17
REMARK 465 ASP B 181
REMARK 465 LYS B 182
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 GLN A 123 36.70 -77.84
REMARK 500 GLN B 123 36.46 -79.39
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 CIT A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT B 1002
DBREF 1U11 A 1 182 UNP Q2QJL3 Q2QJL3_ACEAC 1 182
DBREF 1U11 B 1 182 UNP Q2QJL3 Q2QJL3_ACEAC 1 182
SEQRES 1 A 182 MET SER GLU THR ALA PRO LEU PRO SER ALA SER SER ALA
SEQRES 2 A 182 LEU GLU ASP LYS ALA ALA SER ALA PRO VAL VAL GLY ILE
SEQRES 3 A 182 ILE MET GLY SER GLN SER ASP TRP GLU THR MET ARG HIS
SEQRES 4 A 182 ALA ASP ALA LEU LEU THR GLU LEU GLU ILE PRO HIS GLU
SEQRES 5 A 182 THR LEU ILE VAL SER ALA HIS ARG THR PRO ASP ARG LEU
SEQRES 6 A 182 ALA ASP TYR ALA ARG THR ALA ALA GLU ARG GLY LEU ASN
SEQRES 7 A 182 VAL ILE ILE ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO
SEQRES 8 A 182 GLY MET CYS ALA ALA TRP THR ARG LEU PRO VAL LEU GLY
SEQRES 9 A 182 VAL PRO VAL GLU SER ARG ALA LEU LYS GLY MET ASP SER
SEQRES 10 A 182 LEU LEU SER ILE VAL GLN MET PRO GLY GLY VAL PRO VAL
SEQRES 11 A 182 GLY THR LEU ALA ILE GLY ALA SER GLY ALA LYS ASN ALA
SEQRES 12 A 182 ALA LEU LEU ALA ALA SER ILE LEU ALA LEU TYR ASN PRO
SEQRES 13 A 182 ALA LEU ALA ALA ARG LEU GLU THR TRP ARG ALA LEU GLN
SEQRES 14 A 182 THR ALA SER VAL PRO ASN SER PRO ILE THR GLU ASP LYS
SEQRES 1 B 182 MET SER GLU THR ALA PRO LEU PRO SER ALA SER SER ALA
SEQRES 2 B 182 LEU GLU ASP LYS ALA ALA SER ALA PRO VAL VAL GLY ILE
SEQRES 3 B 182 ILE MET GLY SER GLN SER ASP TRP GLU THR MET ARG HIS
SEQRES 4 B 182 ALA ASP ALA LEU LEU THR GLU LEU GLU ILE PRO HIS GLU
SEQRES 5 B 182 THR LEU ILE VAL SER ALA HIS ARG THR PRO ASP ARG LEU
SEQRES 6 B 182 ALA ASP TYR ALA ARG THR ALA ALA GLU ARG GLY LEU ASN
SEQRES 7 B 182 VAL ILE ILE ALA GLY ALA GLY GLY ALA ALA HIS LEU PRO
SEQRES 8 B 182 GLY MET CYS ALA ALA TRP THR ARG LEU PRO VAL LEU GLY
SEQRES 9 B 182 VAL PRO VAL GLU SER ARG ALA LEU LYS GLY MET ASP SER
SEQRES 10 B 182 LEU LEU SER ILE VAL GLN MET PRO GLY GLY VAL PRO VAL
SEQRES 11 B 182 GLY THR LEU ALA ILE GLY ALA SER GLY ALA LYS ASN ALA
SEQRES 12 B 182 ALA LEU LEU ALA ALA SER ILE LEU ALA LEU TYR ASN PRO
SEQRES 13 B 182 ALA LEU ALA ALA ARG LEU GLU THR TRP ARG ALA LEU GLN
SEQRES 14 B 182 THR ALA SER VAL PRO ASN SER PRO ILE THR GLU ASP LYS
HET CIT A1001 13
HET CIT B1002 13
HETNAM CIT CITRIC ACID
FORMUL 3 CIT 2(C6 H8 O7)
FORMUL 5 HOH *262(H2 O)
HELIX 1 1 SER A 30 SER A 32 5 3
HELIX 2 2 ASP A 33 LEU A 47 1 15
HELIX 3 3 THR A 61 ALA A 72 1 12
HELIX 4 4 HIS A 89 THR A 98 1 10
HELIX 5 5 GLY A 114 GLN A 123 1 10
HELIX 6 6 GLY A 136 ALA A 152 1 17
HELIX 7 7 ASN A 155 VAL A 173 1 19
HELIX 8 8 SER B 30 SER B 32 5 3
HELIX 9 9 ASP B 33 LEU B 47 1 15
HELIX 10 10 THR B 61 ALA B 72 1 12
HELIX 11 11 HIS B 89 THR B 98 1 10
HELIX 12 12 GLY B 114 GLN B 123 1 10
HELIX 13 13 GLY B 136 ALA B 152 1 17
HELIX 14 14 ASN B 155 SER B 172 1 18
SHEET 1 A 5 HIS A 51 ILE A 55 0
SHEET 2 A 5 VAL A 24 MET A 28 1 N ILE A 26 O GLU A 52
SHEET 3 A 5 VAL A 79 GLY A 85 1 O ILE A 81 N GLY A 25
SHEET 4 A 5 VAL A 102 VAL A 107 1 O LEU A 103 N ALA A 82
SHEET 5 A 5 GLY A 131 THR A 132 1 O GLY A 131 N GLY A 104
SHEET 1 B 5 HIS B 51 ILE B 55 0
SHEET 2 B 5 VAL B 24 MET B 28 1 N ILE B 26 O GLU B 52
SHEET 3 B 5 VAL B 79 GLY B 85 1 O ILE B 81 N GLY B 25
SHEET 4 B 5 VAL B 102 VAL B 107 1 O LEU B 103 N ILE B 80
SHEET 5 B 5 GLY B 131 THR B 132 1 O GLY B 131 N GLY B 104
SITE 1 AC1 12 GLY A 29 SER A 30 SER A 32 ASP A 33
SITE 2 AC1 12 SER A 57 HIS A 59 ALA A 84 GLY A 85
SITE 3 AC1 12 HOH A 564 HOH A 688 HOH A 691 PRO B 125
SITE 1 AC2 11 PRO A 125 GLY B 29 SER B 30 ASP B 33
SITE 2 AC2 11 SER B 57 HIS B 59 ALA B 84 GLY B 85
SITE 3 AC2 11 ALA B 87 HOH B 682 HOH B 692
CRYST1 99.250 99.250 164.810 90.00 90.00 90.00 I 4 2 2 32
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 0.010076 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010076 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006068 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
