HEADER LYASE 11-AUG-03 1UJQ
TITLE CRYSTAL STRUCTURE OF 2-METHYLISOCITRATE LYASE (PRPB) FROM SALMONELLA
TITLE 2 ENTERICA SEROVAR TYPHIMURIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE METHYLISOCITRATE LYASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: 2-METHYLISOCITRATE LYASE;
COMPND 5 EC: 4.1.3.30;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR
SOURCE 3 TYPHIMURIUM;
SOURCE 4 ORGANISM_TAXID: 90371;
SOURCE 5 STRAIN: IFO 12529;
SOURCE 6 GENE: PRPB;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-BLUE VECTOR(NOVAGEN)
KEYWDS PRPB, LYASE, METHYLISOCITRATE, METHYLCITRATE CYCLE, TIM-2 BARREL
EXPDTA X-RAY DIFFRACTION
AUTHOR D.K.SIMANSHU,M.R.N.MURTHY
REVDAT 5 25-OCT-23 1UJQ 1 SEQADV
REVDAT 4 24-FEB-09 1UJQ 1 VERSN
REVDAT 3 25-NOV-03 1UJQ 1 JRNL
REVDAT 2 07-OCT-03 1UJQ 3 HETATM
REVDAT 1 02-SEP-03 1UJQ 0
JRNL AUTH D.K.SIMANSHU,P.S.SATHESHKUMAR,H.S.SAVITHRI,M.R.N.MURTHY
JRNL TITL CRYSTAL STRUCTURE OF SALMONELLA TYPHIMURIUM
JRNL TITL 2 2-METHYLISOCITRATE LYASE (PRPB) AND ITS COMPLEX WITH
JRNL TITL 3 PYRUVATE AND MG(2+)
JRNL REF BIOCHEM.BIOPHYS.RES.COMMUN. V. 311 193 2003
JRNL REFN ISSN 0006-291X
JRNL PMID 14575713
JRNL DOI 10.1016/J.BBRC.2003.09.193
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.99
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 499934.800
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 92.9
REMARK 3 NUMBER OF REFLECTIONS : 69022
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) : 0.205
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3514
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.23
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 10493
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE : 0.2760
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 575
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 : 8204
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 565
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.70
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -5.42000
REMARK 3 B22 (A**2) : 6.09000
REMARK 3 B33 (A**2) : -0.68000
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) : 0.24
REMARK 3 ESD FROM SIGMAA (A) : 0.15
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) : 0.28
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.100
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.40
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.860
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) : 1.440 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.230 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.170 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.160 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.36
REMARK 3 BSOL : 58.82
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: COORDINATES OF THE RESIDUES RANGING
REMARK 3 FROM 87 TO 96 IN THE D SUBUNIT ARE TENTATIVE DUE TO POOR
REMARK 3 ELECTRON DENSITY.
REMARK 4
REMARK 4 1UJQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000005902.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-FEB-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC MIRRORS
REMARK 200 OPTICS : OSMIC MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69022
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 5.500
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : 0.06100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.80
REMARK 200 R MERGE FOR SHELL (I) : 0.42100
REMARK 200 R SYM FOR SHELL (I) : 0.42300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: 1MUM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: IMIDAZOLE,SODIUM ACETATE TRIHYDRATE,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K. SODIUM
REMARK 280 FORMATE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K. SODIUM CHLORIDE, PEG6000, PH 8.0, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 291K. SODIUM FORMATE, SODIUM ACETATE
REMARK 280 TRIHYDRATE, PH 4.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 277K
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 31.40600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 100.78550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.54300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 100.78550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 31.40600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.54300
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17040 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 ALA A 0
REMARK 465 SER A 1
REMARK 465 SER A 2
REMARK 465 LEU A 3
REMARK 465 GLY A 119
REMARK 465 ALA A 120
REMARK 465 LYS A 121
REMARK 465 ARG A 122
REMARK 465 CYS A 123
REMARK 465 GLY A 124
REMARK 465 HIS A 125
REMARK 465 ARG A 126
REMARK 465 PRO A 127
REMARK 465 ASN A 128
REMARK 465 LYS A 129
REMARK 465 ASP A 287
REMARK 465 ALA A 288
REMARK 465 LEU A 289
REMARK 465 TYR A 290
REMARK 465 ARG A 291
REMARK 465 ASN A 292
REMARK 465 LYS A 293
REMARK 465 LYS A 294
REMARK 465 SER A 295
REMARK 465 LEU A 296
REMARK 465 GLU A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
REMARK 465 MET B -1
REMARK 465 ALA B 0
REMARK 465 SER B 1
REMARK 465 SER B 2
REMARK 465 LEU B 3
REMARK 465 HIS B 4
REMARK 465 GLY B 119
REMARK 465 ALA B 120
REMARK 465 LYS B 121
REMARK 465 ARG B 122
REMARK 465 CYS B 123
REMARK 465 GLY B 124
REMARK 465 HIS B 125
REMARK 465 ARG B 126
REMARK 465 PRO B 127
REMARK 465 ASN B 128
REMARK 465 LYS B 129
REMARK 465 GLU B 284
REMARK 465 LYS B 285
REMARK 465 LEU B 286
REMARK 465 ASP B 287
REMARK 465 ALA B 288
REMARK 465 LEU B 289
REMARK 465 TYR B 290
REMARK 465 ARG B 291
REMARK 465 ASN B 292
REMARK 465 LYS B 293
REMARK 465 LYS B 294
REMARK 465 SER B 295
REMARK 465 LEU B 296
REMARK 465 GLU B 297
REMARK 465 HIS B 298
REMARK 465 HIS B 299
REMARK 465 HIS B 300
REMARK 465 HIS B 301
REMARK 465 HIS B 302
REMARK 465 HIS B 303
REMARK 465 MET C -1
REMARK 465 ALA C 0
REMARK 465 SER C 1
REMARK 465 SER C 2
REMARK 465 LEU C 3
REMARK 465 GLY C 119
REMARK 465 ALA C 120
REMARK 465 LYS C 121
REMARK 465 ARG C 122
REMARK 465 CYS C 123
REMARK 465 GLY C 124
REMARK 465 HIS C 125
REMARK 465 ARG C 126
REMARK 465 PRO C 127
REMARK 465 ASN C 128
REMARK 465 LYS C 129
REMARK 465 TYR C 290
REMARK 465 ARG C 291
REMARK 465 ASN C 292
REMARK 465 LYS C 293
REMARK 465 LYS C 294
REMARK 465 SER C 295
REMARK 465 LEU C 296
REMARK 465 GLU C 297
REMARK 465 HIS C 298
REMARK 465 HIS C 299
REMARK 465 HIS C 300
REMARK 465 HIS C 301
REMARK 465 HIS C 302
REMARK 465 HIS C 303
REMARK 465 MET D -1
REMARK 465 ALA D 0
REMARK 465 SER D 1
REMARK 465 SER D 2
REMARK 465 LEU D 3
REMARK 465 GLY D 119
REMARK 465 ALA D 120
REMARK 465 LYS D 121
REMARK 465 ARG D 122
REMARK 465 CYS D 123
REMARK 465 GLY D 124
REMARK 465 HIS D 125
REMARK 465 ARG D 126
REMARK 465 PRO D 127
REMARK 465 ASN D 128
REMARK 465 LYS D 129
REMARK 465 GLU D 283
REMARK 465 GLU D 284
REMARK 465 LYS D 285
REMARK 465 LEU D 286
REMARK 465 ASP D 287
REMARK 465 ALA D 288
REMARK 465 LEU D 289
REMARK 465 TYR D 290
REMARK 465 ARG D 291
REMARK 465 ASN D 292
REMARK 465 LYS D 293
REMARK 465 LYS D 294
REMARK 465 SER D 295
REMARK 465 LEU D 296
REMARK 465 GLU D 297
REMARK 465 HIS D 298
REMARK 465 HIS D 299
REMARK 465 HIS D 300
REMARK 465 HIS D 301
REMARK 465 HIS D 302
REMARK 465 HIS D 303
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 HIS A 4 CB CG ND1 CD2 CE1 NE2
REMARK 470 ASP D 87 CB CG OD1 OD2
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 ASP A 87 -112.94 54.93
REMARK 500 ASP A 87 -112.94 54.93
REMARK 500 PHE A 90 83.66 47.47
REMARK 500 SER A 92 -13.49 -162.17
REMARK 500 ILE A 211 48.50 -96.10
REMARK 500 ASP B 87 -126.12 48.20
REMARK 500 ASP B 87 -126.12 48.20
REMARK 500 ILE B 211 41.65 -102.60
REMARK 500 SER C 5 127.91 -39.48
REMARK 500 ASP C 87 -121.85 48.63
REMARK 500 THR C 259 144.13 -174.17
REMARK 500 ASP D 87 -135.65 56.34
REMARK 500 PHE D 90 -10.00 56.75
REMARK 500 SER D 92 -51.21 -163.39
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1UJQ A 2 295 UNP Q56062 PRPB_SALTY 1 294
DBREF 1UJQ B 2 295 UNP Q56062 PRPB_SALTY 1 294
DBREF 1UJQ C 2 295 UNP Q56062 PRPB_SALTY 1 294
DBREF 1UJQ D 2 295 UNP Q56062 PRPB_SALTY 1 294
SEQADV 1UJQ MET A -1 UNP Q56062 CLONING ARTIFACT
SEQADV 1UJQ ALA A 0 UNP Q56062 CLONING ARTIFACT
SEQADV 1UJQ SER A 1 UNP Q56062 CLONING ARTIFACT
SEQADV 1UJQ LEU A 296 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ GLU A 297 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS A 298 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS A 299 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS A 300 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS A 301 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS A 302 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS A 303 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ MET B -1 UNP Q56062 CLONING ARTIFACT
SEQADV 1UJQ ALA B 0 UNP Q56062 CLONING ARTIFACT
SEQADV 1UJQ SER B 1 UNP Q56062 CLONING ARTIFACT
SEQADV 1UJQ LEU B 296 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ GLU B 297 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS B 298 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS B 299 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS B 300 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS B 301 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS B 302 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS B 303 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ MET C -1 UNP Q56062 CLONING ARTIFACT
SEQADV 1UJQ ALA C 0 UNP Q56062 CLONING ARTIFACT
SEQADV 1UJQ SER C 1 UNP Q56062 CLONING ARTIFACT
SEQADV 1UJQ LEU C 296 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ GLU C 297 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS C 298 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS C 299 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS C 300 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS C 301 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS C 302 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS C 303 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ MET D -1 UNP Q56062 CLONING ARTIFACT
SEQADV 1UJQ ALA D 0 UNP Q56062 CLONING ARTIFACT
SEQADV 1UJQ SER D 1 UNP Q56062 CLONING ARTIFACT
SEQADV 1UJQ LEU D 296 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ GLU D 297 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS D 298 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS D 299 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS D 300 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS D 301 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS D 302 UNP Q56062 EXPRESSION TAG
SEQADV 1UJQ HIS D 303 UNP Q56062 EXPRESSION TAG
SEQRES 1 A 305 MET ALA SER SER LEU HIS SER PRO GLY GLN ALA PHE ARG
SEQRES 2 A 305 ALA ALA LEU ALA LYS GLU ASN PRO LEU GLN ILE VAL GLY
SEQRES 3 A 305 ALA ILE ASN ALA ASN HIS ALA LEU LEU ALA GLN ARG ALA
SEQRES 4 A 305 GLY TYR GLN ALA ILE TYR LEU SER GLY GLY GLY VAL ALA
SEQRES 5 A 305 ALA GLY SER LEU GLY LEU PRO ASP LEU GLY ILE SER THR
SEQRES 6 A 305 LEU ASP ASP VAL LEU THR ASP ILE ARG ARG ILE THR ASP
SEQRES 7 A 305 VAL CYS PRO LEU PRO LEU LEU VAL ASP ALA ASP ILE GLY
SEQRES 8 A 305 PHE GLY SER SER ALA PHE ASN VAL ALA ARG THR VAL LYS
SEQRES 9 A 305 SER ILE ALA LYS ALA GLY ALA ALA ALA LEU HIS ILE GLU
SEQRES 10 A 305 ASP GLN VAL GLY ALA LYS ARG CYS GLY HIS ARG PRO ASN
SEQRES 11 A 305 LYS ALA ILE VAL SER LYS GLU GLU MET VAL ASP ARG ILE
SEQRES 12 A 305 ARG ALA ALA VAL ASP ALA ARG THR ASP PRO ASN PHE VAL
SEQRES 13 A 305 ILE MET ALA ARG THR ASP ALA LEU ALA VAL GLU GLY LEU
SEQRES 14 A 305 GLU ALA ALA LEU ASP ARG ALA GLN ALA TYR VAL ASP ALA
SEQRES 15 A 305 GLY ALA ASP MET LEU PHE PRO GLU ALA ILE THR GLU LEU
SEQRES 16 A 305 SER MET TYR ARG ARG PHE ALA ASP VAL ALA GLN VAL PRO
SEQRES 17 A 305 ILE LEU ALA ASN ILE THR GLU PHE GLY ALA THR PRO LEU
SEQRES 18 A 305 PHE THR THR ASP GLU LEU ARG SER ALA HIS VAL ALA MET
SEQRES 19 A 305 ALA LEU TYR PRO LEU SER ALA PHE ARG ALA MET ASN ARG
SEQRES 20 A 305 ALA ALA GLU LYS VAL TYR THR VAL LEU ARG GLN GLU GLY
SEQRES 21 A 305 THR GLN LYS ASN VAL ILE ASP ILE MET GLN THR ARG ASN
SEQRES 22 A 305 GLU LEU TYR GLU SER ILE ASN TYR TYR GLN PHE GLU GLU
SEQRES 23 A 305 LYS LEU ASP ALA LEU TYR ARG ASN LYS LYS SER LEU GLU
SEQRES 24 A 305 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 305 MET ALA SER SER LEU HIS SER PRO GLY GLN ALA PHE ARG
SEQRES 2 B 305 ALA ALA LEU ALA LYS GLU ASN PRO LEU GLN ILE VAL GLY
SEQRES 3 B 305 ALA ILE ASN ALA ASN HIS ALA LEU LEU ALA GLN ARG ALA
SEQRES 4 B 305 GLY TYR GLN ALA ILE TYR LEU SER GLY GLY GLY VAL ALA
SEQRES 5 B 305 ALA GLY SER LEU GLY LEU PRO ASP LEU GLY ILE SER THR
SEQRES 6 B 305 LEU ASP ASP VAL LEU THR ASP ILE ARG ARG ILE THR ASP
SEQRES 7 B 305 VAL CYS PRO LEU PRO LEU LEU VAL ASP ALA ASP ILE GLY
SEQRES 8 B 305 PHE GLY SER SER ALA PHE ASN VAL ALA ARG THR VAL LYS
SEQRES 9 B 305 SER ILE ALA LYS ALA GLY ALA ALA ALA LEU HIS ILE GLU
SEQRES 10 B 305 ASP GLN VAL GLY ALA LYS ARG CYS GLY HIS ARG PRO ASN
SEQRES 11 B 305 LYS ALA ILE VAL SER LYS GLU GLU MET VAL ASP ARG ILE
SEQRES 12 B 305 ARG ALA ALA VAL ASP ALA ARG THR ASP PRO ASN PHE VAL
SEQRES 13 B 305 ILE MET ALA ARG THR ASP ALA LEU ALA VAL GLU GLY LEU
SEQRES 14 B 305 GLU ALA ALA LEU ASP ARG ALA GLN ALA TYR VAL ASP ALA
SEQRES 15 B 305 GLY ALA ASP MET LEU PHE PRO GLU ALA ILE THR GLU LEU
SEQRES 16 B 305 SER MET TYR ARG ARG PHE ALA ASP VAL ALA GLN VAL PRO
SEQRES 17 B 305 ILE LEU ALA ASN ILE THR GLU PHE GLY ALA THR PRO LEU
SEQRES 18 B 305 PHE THR THR ASP GLU LEU ARG SER ALA HIS VAL ALA MET
SEQRES 19 B 305 ALA LEU TYR PRO LEU SER ALA PHE ARG ALA MET ASN ARG
SEQRES 20 B 305 ALA ALA GLU LYS VAL TYR THR VAL LEU ARG GLN GLU GLY
SEQRES 21 B 305 THR GLN LYS ASN VAL ILE ASP ILE MET GLN THR ARG ASN
SEQRES 22 B 305 GLU LEU TYR GLU SER ILE ASN TYR TYR GLN PHE GLU GLU
SEQRES 23 B 305 LYS LEU ASP ALA LEU TYR ARG ASN LYS LYS SER LEU GLU
SEQRES 24 B 305 HIS HIS HIS HIS HIS HIS
SEQRES 1 C 305 MET ALA SER SER LEU HIS SER PRO GLY GLN ALA PHE ARG
SEQRES 2 C 305 ALA ALA LEU ALA LYS GLU ASN PRO LEU GLN ILE VAL GLY
SEQRES 3 C 305 ALA ILE ASN ALA ASN HIS ALA LEU LEU ALA GLN ARG ALA
SEQRES 4 C 305 GLY TYR GLN ALA ILE TYR LEU SER GLY GLY GLY VAL ALA
SEQRES 5 C 305 ALA GLY SER LEU GLY LEU PRO ASP LEU GLY ILE SER THR
SEQRES 6 C 305 LEU ASP ASP VAL LEU THR ASP ILE ARG ARG ILE THR ASP
SEQRES 7 C 305 VAL CYS PRO LEU PRO LEU LEU VAL ASP ALA ASP ILE GLY
SEQRES 8 C 305 PHE GLY SER SER ALA PHE ASN VAL ALA ARG THR VAL LYS
SEQRES 9 C 305 SER ILE ALA LYS ALA GLY ALA ALA ALA LEU HIS ILE GLU
SEQRES 10 C 305 ASP GLN VAL GLY ALA LYS ARG CYS GLY HIS ARG PRO ASN
SEQRES 11 C 305 LYS ALA ILE VAL SER LYS GLU GLU MET VAL ASP ARG ILE
SEQRES 12 C 305 ARG ALA ALA VAL ASP ALA ARG THR ASP PRO ASN PHE VAL
SEQRES 13 C 305 ILE MET ALA ARG THR ASP ALA LEU ALA VAL GLU GLY LEU
SEQRES 14 C 305 GLU ALA ALA LEU ASP ARG ALA GLN ALA TYR VAL ASP ALA
SEQRES 15 C 305 GLY ALA ASP MET LEU PHE PRO GLU ALA ILE THR GLU LEU
SEQRES 16 C 305 SER MET TYR ARG ARG PHE ALA ASP VAL ALA GLN VAL PRO
SEQRES 17 C 305 ILE LEU ALA ASN ILE THR GLU PHE GLY ALA THR PRO LEU
SEQRES 18 C 305 PHE THR THR ASP GLU LEU ARG SER ALA HIS VAL ALA MET
SEQRES 19 C 305 ALA LEU TYR PRO LEU SER ALA PHE ARG ALA MET ASN ARG
SEQRES 20 C 305 ALA ALA GLU LYS VAL TYR THR VAL LEU ARG GLN GLU GLY
SEQRES 21 C 305 THR GLN LYS ASN VAL ILE ASP ILE MET GLN THR ARG ASN
SEQRES 22 C 305 GLU LEU TYR GLU SER ILE ASN TYR TYR GLN PHE GLU GLU
SEQRES 23 C 305 LYS LEU ASP ALA LEU TYR ARG ASN LYS LYS SER LEU GLU
SEQRES 24 C 305 HIS HIS HIS HIS HIS HIS
SEQRES 1 D 305 MET ALA SER SER LEU HIS SER PRO GLY GLN ALA PHE ARG
SEQRES 2 D 305 ALA ALA LEU ALA LYS GLU ASN PRO LEU GLN ILE VAL GLY
SEQRES 3 D 305 ALA ILE ASN ALA ASN HIS ALA LEU LEU ALA GLN ARG ALA
SEQRES 4 D 305 GLY TYR GLN ALA ILE TYR LEU SER GLY GLY GLY VAL ALA
SEQRES 5 D 305 ALA GLY SER LEU GLY LEU PRO ASP LEU GLY ILE SER THR
SEQRES 6 D 305 LEU ASP ASP VAL LEU THR ASP ILE ARG ARG ILE THR ASP
SEQRES 7 D 305 VAL CYS PRO LEU PRO LEU LEU VAL ASP ALA ASP ILE GLY
SEQRES 8 D 305 PHE GLY SER SER ALA PHE ASN VAL ALA ARG THR VAL LYS
SEQRES 9 D 305 SER ILE ALA LYS ALA GLY ALA ALA ALA LEU HIS ILE GLU
SEQRES 10 D 305 ASP GLN VAL GLY ALA LYS ARG CYS GLY HIS ARG PRO ASN
SEQRES 11 D 305 LYS ALA ILE VAL SER LYS GLU GLU MET VAL ASP ARG ILE
SEQRES 12 D 305 ARG ALA ALA VAL ASP ALA ARG THR ASP PRO ASN PHE VAL
SEQRES 13 D 305 ILE MET ALA ARG THR ASP ALA LEU ALA VAL GLU GLY LEU
SEQRES 14 D 305 GLU ALA ALA LEU ASP ARG ALA GLN ALA TYR VAL ASP ALA
SEQRES 15 D 305 GLY ALA ASP MET LEU PHE PRO GLU ALA ILE THR GLU LEU
SEQRES 16 D 305 SER MET TYR ARG ARG PHE ALA ASP VAL ALA GLN VAL PRO
SEQRES 17 D 305 ILE LEU ALA ASN ILE THR GLU PHE GLY ALA THR PRO LEU
SEQRES 18 D 305 PHE THR THR ASP GLU LEU ARG SER ALA HIS VAL ALA MET
SEQRES 19 D 305 ALA LEU TYR PRO LEU SER ALA PHE ARG ALA MET ASN ARG
SEQRES 20 D 305 ALA ALA GLU LYS VAL TYR THR VAL LEU ARG GLN GLU GLY
SEQRES 21 D 305 THR GLN LYS ASN VAL ILE ASP ILE MET GLN THR ARG ASN
SEQRES 22 D 305 GLU LEU TYR GLU SER ILE ASN TYR TYR GLN PHE GLU GLU
SEQRES 23 D 305 LYS LEU ASP ALA LEU TYR ARG ASN LYS LYS SER LEU GLU
SEQRES 24 D 305 HIS HIS HIS HIS HIS HIS
FORMUL 5 HOH *565(H2 O)
HELIX 1 1 SER A 5 GLU A 17 1 13
HELIX 2 2 ASN A 27 GLY A 38 1 12
HELIX 3 3 SER A 45 GLY A 52 1 8
HELIX 4 4 THR A 63 CYS A 78 1 16
HELIX 5 5 SER A 93 ALA A 107 1 15
HELIX 6 6 SER A 133 ARG A 148 1 16
HELIX 7 7 ASP A 160 GLY A 166 1 7
HELIX 8 8 GLY A 166 ALA A 180 1 15
HELIX 9 9 GLU A 192 GLN A 204 1 13
HELIX 10 10 THR A 221 ALA A 228 1 8
HELIX 11 11 LEU A 237 GLY A 258 1 22
HELIX 12 12 GLN A 260 MET A 267 5 8
HELIX 13 13 THR A 269 ILE A 277 1 9
HELIX 14 14 ASN A 278 LEU A 286 1 9
HELIX 15 15 SER B 5 GLU B 17 1 13
HELIX 16 16 ASN B 27 GLY B 38 1 12
HELIX 17 17 SER B 45 GLY B 52 1 8
HELIX 18 18 THR B 63 CYS B 78 1 16
HELIX 19 19 SER B 93 ALA B 107 1 15
HELIX 20 20 SER B 133 ARG B 148 1 16
HELIX 21 21 ASP B 160 GLY B 166 1 7
HELIX 22 22 GLY B 166 ALA B 180 1 15
HELIX 23 23 GLU B 192 GLN B 204 1 13
HELIX 24 24 THR B 221 ALA B 228 1 8
HELIX 25 25 LEU B 237 GLY B 258 1 22
HELIX 26 26 GLN B 260 MET B 267 5 8
HELIX 27 27 THR B 269 ILE B 277 1 9
HELIX 28 28 ASN B 278 GLU B 283 1 6
HELIX 29 29 SER C 5 GLU C 17 1 13
HELIX 30 30 ASN C 27 ALA C 37 1 11
HELIX 31 31 SER C 45 LEU C 54 1 10
HELIX 32 32 THR C 63 CYS C 78 1 16
HELIX 33 33 SER C 93 ALA C 107 1 15
HELIX 34 34 SER C 133 ARG C 148 1 16
HELIX 35 35 ASP C 160 VAL C 164 5 5
HELIX 36 36 GLY C 166 ALA C 180 1 15
HELIX 37 37 GLU C 192 GLN C 204 1 13
HELIX 38 38 THR C 221 ALA C 228 1 8
HELIX 39 39 LEU C 237 GLY C 258 1 22
HELIX 40 40 GLN C 260 MET C 267 5 8
HELIX 41 41 THR C 269 ILE C 277 1 9
HELIX 42 42 ASN C 278 LEU C 289 1 12
HELIX 43 43 SER D 5 GLU D 17 1 13
HELIX 44 44 ASN D 27 ALA D 37 1 11
HELIX 45 45 SER D 45 GLY D 52 1 8
HELIX 46 46 THR D 63 CYS D 78 1 16
HELIX 47 47 SER D 93 GLY D 108 1 16
HELIX 48 48 SER D 133 ARG D 148 1 16
HELIX 49 49 GLY D 166 ALA D 180 1 15
HELIX 50 50 GLU D 192 GLN D 204 1 13
HELIX 51 51 THR D 221 SER D 227 1 7
HELIX 52 52 LEU D 237 GLY D 258 1 22
HELIX 53 53 GLN D 260 MET D 267 5 8
HELIX 54 54 THR D 269 ILE D 277 1 9
SHEET 1 A 8 MET A 184 PRO A 187 0
SHEET 2 A 8 VAL A 154 THR A 159 1 N ALA A 157 O PHE A 186
SHEET 3 A 8 ALA A 111 GLU A 115 1 N ILE A 114 O ARG A 158
SHEET 4 A 8 LEU A 82 ASP A 85 1 N VAL A 84 O ALA A 111
SHEET 5 A 8 ALA A 41 LEU A 44 1 N ILE A 42 O LEU A 83
SHEET 6 A 8 LEU A 20 GLY A 24 1 N VAL A 23 O TYR A 43
SHEET 7 A 8 MET A 232 TYR A 235 1 O ALA A 233 N ILE A 22
SHEET 8 A 8 LEU A 208 ASN A 210 1 N ALA A 209 O MET A 232
SHEET 1 B 8 MET B 184 PRO B 187 0
SHEET 2 B 8 VAL B 154 THR B 159 1 N ALA B 157 O PHE B 186
SHEET 3 B 8 ALA B 111 GLU B 115 1 N ILE B 114 O ARG B 158
SHEET 4 B 8 LEU B 82 ASP B 85 1 N VAL B 84 O ALA B 111
SHEET 5 B 8 ILE B 42 LEU B 44 1 N LEU B 44 O LEU B 83
SHEET 6 B 8 LEU B 20 GLY B 24 1 N VAL B 23 O TYR B 43
SHEET 7 B 8 MET B 232 TYR B 235 1 O ALA B 233 N ILE B 22
SHEET 8 B 8 LEU B 208 ASN B 210 1 N ALA B 209 O MET B 232
SHEET 1 C 8 MET C 184 PRO C 187 0
SHEET 2 C 8 VAL C 154 THR C 159 1 N ALA C 157 O MET C 184
SHEET 3 C 8 ALA C 111 GLU C 115 1 N LEU C 112 O MET C 156
SHEET 4 C 8 LEU C 82 ASP C 85 1 N VAL C 84 O ALA C 111
SHEET 5 C 8 ILE C 42 LEU C 44 1 N ILE C 42 O LEU C 83
SHEET 6 C 8 LEU C 20 GLY C 24 1 N VAL C 23 O TYR C 43
SHEET 7 C 8 MET C 232 TYR C 235 1 O ALA C 233 N ILE C 22
SHEET 8 C 8 LEU C 208 ASN C 210 1 N ALA C 209 O MET C 232
SHEET 1 D 8 MET D 184 PRO D 187 0
SHEET 2 D 8 VAL D 154 THR D 159 1 N ALA D 157 O PHE D 186
SHEET 3 D 8 ALA D 111 GLU D 115 1 N LEU D 112 O MET D 156
SHEET 4 D 8 LEU D 82 ASP D 85 1 N VAL D 84 O ALA D 111
SHEET 5 D 8 ALA D 41 LEU D 44 1 N ILE D 42 O LEU D 83
SHEET 6 D 8 LEU D 20 GLY D 24 1 N VAL D 23 O TYR D 43
SHEET 7 D 8 MET D 232 TYR D 235 1 O ALA D 233 N ILE D 22
SHEET 8 D 8 LEU D 208 ASN D 210 1 N ALA D 209 O LEU D 234
CISPEP 1 ASN A 18 PRO A 19 0 -0.06
CISPEP 2 ASN B 18 PRO B 19 0 -0.17
CISPEP 3 ASN C 18 PRO C 19 0 -0.20
CISPEP 4 ASN D 18 PRO D 19 0 -0.32
CRYST1 62.812 99.086 201.571 90.00 90.00 90.00 P 21 21 21 16
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 0.015921 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010092 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004961 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
