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HEADER HYDROLASE 01-MAY-08 3D0K
TITLE CRYSTAL STRUCTURE OF THE LPQC, POLY(3-HYDROXYBUTYRATE)
TITLE 2 DEPOLYMERASE FROM BORDETELLA PARAPERTUSSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE POLY(3-HYDROXYBUTYRATE) DEPOLYMERASE
COMPND 3 LPQC;
COMPND 4 CHAIN: A, B;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BORDETELLA PARAPERTUSSIS 12822;
SOURCE 3 STRAIN: 12822 / NCTC 13253;
SOURCE 4 ATCC: BAA-587;
SOURCE 5 GENE: BPP4128;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PMCSG19B
KEYWDS ALPHA-BETA-ALPHA SANDWICH, STRUCTURAL GENOMICS, PSI-2,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, MIDWEST CENTER FOR STRUCTURAL
KEYWDS 3 GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.KIM,C.TESAR,R.JEDRZEJCZAK,A.JOACHIMIAK,MIDWEST CENTER FOR
AUTHOR 2 STRUCTURAL GENOMICS (MCSG)
REVDAT 1 01-JUL-08 3D0K 0
JRNL AUTH Y.KIM,C.TESAR,R.JEDRZEJCZAK,A.JOACHIMIAK
JRNL TITL CRYSTAL STRUCTURE OF THE LPQC,
JRNL TITL 2 POLY(3-HYDROXYBUTYRATE) DEPOLYMERASE FROM
JRNL TITL 3 BORDETELLA PARAPERTUSSIS.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.83 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 WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 52230
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) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.164
REMARK 3 FREE R VALUE : 0.209
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2803
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH : 1.83
REMARK 3 BIN RESOLUTION RANGE LOW : 1.88
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3773
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.03
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 214
REMARK 3 BIN FREE R VALUE : 0.2740
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 ALL ATOMS : 5159
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.67
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.88000
REMARK 3 B22 (A**2) : 1.35000
REMARK 3 B33 (A**2) : -0.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.37000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.124
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.123
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.264
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4853 ; 0.019 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6643 ; 1.639 ; 1.944
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 599 ; 6.211 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 250 ;35.634 ;22.360
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 667 ;15.257 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;19.518 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 675 ; 0.119 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3920 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2397 ; 0.207 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3262 ; 0.309 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 416 ; 0.162 ; 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): 58 ; 0.237 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.182 ; 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): 3035 ; 1.077 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4738 ; 1.705 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2074 ; 3.075 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1905 ; 4.704 ; 4.500
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 : 0
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 5 A 296
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7433 30.1432 92.8531
REMARK 3 T TENSOR
REMARK 3 T11: -0.0599 T22: -0.0403
REMARK 3 T33: -0.0289 T12: 0.0137
REMARK 3 T13: -0.0100 T23: -0.0230
REMARK 3 L TENSOR
REMARK 3 L11: 0.5706 L22: 0.6383
REMARK 3 L33: 1.2958 L12: 0.1083
REMARK 3 L13: 0.3970 L23: 0.3952
REMARK 3 S TENSOR
REMARK 3 S11: 0.0075 S12: -0.0272 S13: -0.0049
REMARK 3 S21: 0.0170 S22: -0.0198 S23: -0.0233
REMARK 3 S31: -0.0016 S32: -0.0702 S33: 0.0123
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 296
REMARK 3 ORIGIN FOR THE GROUP (A): 13.3231 33.9353 42.2585
REMARK 3 T TENSOR
REMARK 3 T11: -0.0404 T22: -0.0551
REMARK 3 T33: -0.0286 T12: -0.0074
REMARK 3 T13: 0.0110 T23: -0.0092
REMARK 3 L TENSOR
REMARK 3 L11: 0.5549 L22: 0.5327
REMARK 3 L33: 0.9334 L12: -0.0642
REMARK 3 L13: 0.2626 L23: -0.1936
REMARK 3 S TENSOR
REMARK 3 S11: -0.0238 S12: -0.0040 S13: -0.0163
REMARK 3 S21: -0.0269 S22: 0.0276 S23: -0.0307
REMARK 3 S31: 0.0014 S32: 0.0066 S33: -0.0038
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3D0K COMPLIES WITH FORMAT V. 3.1, 01-AUG-2007
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE RCSB ID CODE IS RCSB047439.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-2008
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97920
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54978
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.830
REMARK 200 RESOLUTION RANGE LOW (A) : 41.830
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.12000
REMARK 200 FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.59800
REMARK 200 FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: HKL-3000, MLPHARE, DM, SHELXD, RESOLVE, COOT
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M AMMONIUM SULFATE, 0.1 M MES
REMARK 280 PH 6.5, 10% DIOXANE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
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,1/2+Y,-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 41.85500
REMARK 290 SMTRY3 2 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 300 REMARK: AUTHORS STATE THAT THE MONOMERIC ASSEMBLY OF THE
REMARK 300 BIOLOGICAL UNIT THAT IS SHOWN IN REMARK 350 IS PUTATIVE.
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: PISA
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSEQI
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 ALA A 0
REMARK 465 MSE A 1
REMARK 465 LYS A 2
REMARK 465 PRO A 3
REMARK 465 ALA A 4
REMARK 465 ASP A 29
REMARK 465 ASP A 30
REMARK 465 ARG A 31
REMARK 465 ASP A 217
REMARK 465 ASP A 218
REMARK 465 GLY A 297
REMARK 465 SER A 298
REMARK 465 GLN A 299
REMARK 465 SER A 300
REMARK 465 ALA A 301
REMARK 465 SER B -2
REMARK 465 ASN B -1
REMARK 465 ALA B 0
REMARK 465 MSE B 1
REMARK 465 ASP B 217
REMARK 465 ASP B 218
REMARK 465 GLY B 297
REMARK 465 SER B 298
REMARK 465 GLN B 299
REMARK 465 SER B 300
REMARK 465 ALA B 301
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI
REMARK 500 O HOH B 356 O HOH B 357 2.08
REMARK 500 O HOH B 464 O HOH B 556 2.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCELIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG B 153 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG B 153 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
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 LYS A 79 61.06 60.20
REMARK 500 TYR A 98 -80.52 -104.63
REMARK 500 SER A 145 -123.32 60.15
REMARK 500 ASP B 30 -73.32 -67.15
REMARK 500 ASN B 32 42.22 -143.83
REMARK 500 TYR B 98 -78.13 -104.63
REMARK 500 SER B 145 -121.96 60.56
REMARK 500 ASN B 170 48.62 39.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR RESIDUE B 302
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 304
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE B 303
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE B 304
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 305
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE B 305
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 306
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE B 306
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE B 307
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE B 308
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 307
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 308
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 SITE_DESCRIPTION: SO4 BINDING SITE FOR RESIDUE A 309
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE A 310
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE B 309
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 SITE_DESCRIPTION: FMT BINDING SITE FOR RESIDUE B 310
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC60195 RELATED DB: TARGETDB
DBREF 3D0K A 1 301 UNP Q7W3B7 Q7W3B7_BORPA 1 301
DBREF 3D0K B 1 301 UNP Q7W3B7 Q7W3B7_BORPA 1 301
SEQADV 3D0K SER A -2 UNP Q7W3B7 EXPRESSION TAG
SEQADV 3D0K ASN A -1 UNP Q7W3B7 EXPRESSION TAG
SEQADV 3D0K ALA A 0 UNP Q7W3B7 EXPRESSION TAG
SEQADV 3D0K SER B -2 UNP Q7W3B7 EXPRESSION TAG
SEQADV 3D0K ASN B -1 UNP Q7W3B7 EXPRESSION TAG
SEQADV 3D0K ALA B 0 UNP Q7W3B7 EXPRESSION TAG
SEQRES 1 A 304 SER ASN ALA MSE LYS PRO ALA ASP LEU THR ASN ALA ASP
SEQRES 2 A 304 ARG ILE ALA LEU GLU LEU GLY HIS ALA GLY ARG ASN ALA
SEQRES 3 A 304 ILE PRO TYR LEU ASP ASP ASP ARG ASN ALA ASP ARG PRO
SEQRES 4 A 304 PHE THR LEU ASN THR TYR ARG PRO TYR GLY TYR THR PRO
SEQRES 5 A 304 ASP ARG PRO VAL VAL VAL VAL GLN HIS GLY VAL LEU ARG
SEQRES 6 A 304 ASN GLY ALA ASP TYR ARG ASP PHE TRP ILE PRO ALA ALA
SEQRES 7 A 304 ASP ARG HIS LYS LEU LEU ILE VAL ALA PRO THR PHE SER
SEQRES 8 A 304 ASP GLU ILE TRP PRO GLY VAL GLU SER TYR ASN ASN GLY
SEQRES 9 A 304 ARG ALA PHE THR ALA ALA GLY ASN PRO ARG HIS VAL ASP
SEQRES 10 A 304 GLY TRP THR TYR ALA LEU VAL ALA ARG VAL LEU ALA ASN
SEQRES 11 A 304 ILE ARG ALA ALA GLU ILE ALA ASP CYS GLU GLN VAL TYR
SEQRES 12 A 304 LEU PHE GLY HIS SER ALA GLY GLY GLN PHE VAL HIS ARG
SEQRES 13 A 304 LEU MSE SER SER GLN PRO HIS ALA PRO PHE HIS ALA VAL
SEQRES 14 A 304 THR ALA ALA ASN PRO GLY TRP TYR THR LEU PRO THR PHE
SEQRES 15 A 304 GLU HIS ARG PHE PRO GLU GLY LEU ASP GLY VAL GLY LEU
SEQRES 16 A 304 THR GLU ASP HIS LEU ALA ARG LEU LEU ALA TYR PRO MSE
SEQRES 17 A 304 THR ILE LEU ALA GLY ASP GLN ASP ILE ALA THR ASP ASP
SEQRES 18 A 304 PRO ASN LEU PRO SER GLU PRO ALA ALA LEU ARG GLN GLY
SEQRES 19 A 304 PRO HIS ARG TYR ALA ARG ALA ARG HIS TYR TYR GLU ALA
SEQRES 20 A 304 GLY GLN ARG ALA ALA ALA GLN ARG GLY LEU PRO PHE GLY
SEQRES 21 A 304 TRP GLN LEU GLN VAL VAL PRO GLY ILE GLY HIS ASP GLY
SEQRES 22 A 304 GLN ALA MSE SER GLN VAL CYS ALA SER LEU TRP PHE ASP
SEQRES 23 A 304 GLY ARG MSE PRO ASP ALA ALA GLU LEU ALA ARG LEU ALA
SEQRES 24 A 304 GLY SER GLN SER ALA
SEQRES 1 B 304 SER ASN ALA MSE LYS PRO ALA ASP LEU THR ASN ALA ASP
SEQRES 2 B 304 ARG ILE ALA LEU GLU LEU GLY HIS ALA GLY ARG ASN ALA
SEQRES 3 B 304 ILE PRO TYR LEU ASP ASP ASP ARG ASN ALA ASP ARG PRO
SEQRES 4 B 304 PHE THR LEU ASN THR TYR ARG PRO TYR GLY TYR THR PRO
SEQRES 5 B 304 ASP ARG PRO VAL VAL VAL VAL GLN HIS GLY VAL LEU ARG
SEQRES 6 B 304 ASN GLY ALA ASP TYR ARG ASP PHE TRP ILE PRO ALA ALA
SEQRES 7 B 304 ASP ARG HIS LYS LEU LEU ILE VAL ALA PRO THR PHE SER
SEQRES 8 B 304 ASP GLU ILE TRP PRO GLY VAL GLU SER TYR ASN ASN GLY
SEQRES 9 B 304 ARG ALA PHE THR ALA ALA GLY ASN PRO ARG HIS VAL ASP
SEQRES 10 B 304 GLY TRP THR TYR ALA LEU VAL ALA ARG VAL LEU ALA ASN
SEQRES 11 B 304 ILE ARG ALA ALA GLU ILE ALA ASP CYS GLU GLN VAL TYR
SEQRES 12 B 304 LEU PHE GLY HIS SER ALA GLY GLY GLN PHE VAL HIS ARG
SEQRES 13 B 304 LEU MSE SER SER GLN PRO HIS ALA PRO PHE HIS ALA VAL
SEQRES 14 B 304 THR ALA ALA ASN PRO GLY TRP TYR THR LEU PRO THR PHE
SEQRES 15 B 304 GLU HIS ARG PHE PRO GLU GLY LEU ASP GLY VAL GLY LEU
SEQRES 16 B 304 THR GLU ASP HIS LEU ALA ARG LEU LEU ALA TYR PRO MSE
SEQRES 17 B 304 THR ILE LEU ALA GLY ASP GLN ASP ILE ALA THR ASP ASP
SEQRES 18 B 304 PRO ASN LEU PRO SER GLU PRO ALA ALA LEU ARG GLN GLY
SEQRES 19 B 304 PRO HIS ARG TYR ALA ARG ALA ARG HIS TYR TYR GLU ALA
SEQRES 20 B 304 GLY GLN ARG ALA ALA ALA GLN ARG GLY LEU PRO PHE GLY
SEQRES 21 B 304 TRP GLN LEU GLN VAL VAL PRO GLY ILE GLY HIS ASP GLY
SEQRES 22 B 304 GLN ALA MSE SER GLN VAL CYS ALA SER LEU TRP PHE ASP
SEQRES 23 B 304 GLY ARG MSE PRO ASP ALA ALA GLU LEU ALA ARG LEU ALA
SEQRES 24 B 304 GLY SER GLN SER ALA
MODRES 3D0K MSE A 155 MET SELENOMETHIONINE
MODRES 3D0K MSE A 205 MET SELENOMETHIONINE
MODRES 3D0K MSE A 273 MET SELENOMETHIONINE
MODRES 3D0K MSE A 286 MET SELENOMETHIONINE
MODRES 3D0K MSE B 155 MET SELENOMETHIONINE
MODRES 3D0K MSE B 205 MET SELENOMETHIONINE
MODRES 3D0K MSE B 273 MET SELENOMETHIONINE
MODRES 3D0K MSE B 286 MET SELENOMETHIONINE
HET MSE A 155 8
HET MSE A 205 8
HET MSE A 273 8
HET MSE A 286 8
HET MSE B 155 8
HET MSE B 205 8
HET MSE B 273 8
HET MSE B 286 8
HET CL A 302 1
HET CL A 303 1
HET SO4 A 304 5
HET SO4 A 305 5
HET SO4 A 306 5
HET SO4 A 307 5
HET SO4 A 308 5
HET SO4 A 309 5
HET CL B 302 1
HET SO4 B 303 5
HET SO4 B 304 5
HET SO4 B 305 5
HET SO4 B 306 5
HET SO4 B 307 5
HET SO4 B 308 5
HET FMT A 310 3
HET FMT B 309 3
HET FMT B 310 3
HETNAM MSE SELENOMETHIONINE
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM FMT FORMIC ACID
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 CL 3(CL 1-)
FORMUL 5 SO4 12(O4 S 2-)
FORMUL 18 FMT 3(C H2 O2)
FORMUL 21 HOH *439(H2 O)
HELIX 1 1 THR A 7 LEU A 16 1 10
HELIX 2 2 ASN A 63 TRP A 71 1 9
HELIX 3 3 TRP A 71 LYS A 79 1 9
HELIX 4 4 PRO A 93 TYR A 98 1 6
HELIX 5 5 HIS A 112 TYR A 118 5 7
HELIX 6 6 ALA A 119 ALA A 131 1 13
HELIX 7 7 SER A 145 GLN A 158 1 14
HELIX 8 8 THR A 193 TYR A 203 1 11
HELIX 9 9 GLU A 224 ARG A 229 1 6
HELIX 10 10 HIS A 233 ARG A 252 1 20
HELIX 11 11 ASP A 269 ASP A 283 1 15
HELIX 12 12 ASP A 288 ALA A 296 1 9
HELIX 13 13 LYS B 2 LEU B 6 5 5
HELIX 14 14 THR B 7 LEU B 16 1 10
HELIX 15 15 ASN B 63 TRP B 71 1 9
HELIX 16 16 TRP B 71 LYS B 79 1 9
HELIX 17 17 PRO B 93 TYR B 98 1 6
HELIX 18 18 HIS B 112 TYR B 118 5 7
HELIX 19 19 ALA B 119 ALA B 131 1 13
HELIX 20 20 SER B 145 GLN B 158 1 14
HELIX 21 21 THR B 193 TYR B 203 1 11
HELIX 22 22 GLU B 224 ARG B 229 1 6
HELIX 23 23 HIS B 233 ARG B 252 1 20
HELIX 24 24 ASP B 269 ASP B 283 1 15
HELIX 25 25 ASP B 288 ALA B 296 1 9
SHEET 1 A 8 GLY A 20 TYR A 26 0
SHEET 2 A 8 PHE A 37 ARG A 43 -1 O PHE A 37 N TYR A 26
SHEET 3 A 8 LEU A 81 THR A 86 -1 O THR A 86 N THR A 38
SHEET 4 A 8 VAL A 53 GLN A 57 1 N VAL A 54 O LEU A 81
SHEET 5 A 8 VAL A 139 HIS A 144 1 O TYR A 140 N VAL A 55
SHEET 6 A 8 ALA A 165 ALA A 169 1 O ALA A 169 N GLY A 143
SHEET 7 A 8 THR A 206 GLY A 210 1 O LEU A 208 N ALA A 168
SHEET 8 A 8 GLN A 259 VAL A 263 1 O GLN A 261 N ILE A 207
SHEET 1 B 8 GLY B 20 TYR B 26 0
SHEET 2 B 8 PHE B 37 ARG B 43 -1 O ARG B 43 N GLY B 20
SHEET 3 B 8 LEU B 81 THR B 86 -1 O THR B 86 N THR B 38
SHEET 4 B 8 VAL B 53 GLN B 57 1 N VAL B 54 O LEU B 81
SHEET 5 B 8 VAL B 139 HIS B 144 1 O TYR B 140 N VAL B 55
SHEET 6 B 8 ALA B 165 ALA B 169 1 O ALA B 169 N GLY B 143
SHEET 7 B 8 THR B 206 GLY B 210 1 O LEU B 208 N ALA B 168
SHEET 8 B 8 GLN B 259 VAL B 263 1 O GLN B 259 N ILE B 207
LINK C LEU A 154 N MSE A 155 1555 1555 1.32
LINK C MSE A 155 N SER A 156 1555 1555 1.34
LINK C PRO A 204 N MSE A 205 1555 1555 1.32
LINK C MSE A 205 N THR A 206 1555 1555 1.35
LINK C ALA A 272 N MSE A 273 1555 1555 1.34
LINK C MSE A 273 N SER A 274 1555 1555 1.33
LINK C ARG A 285 N MSE A 286 1555 1555 1.32
LINK C MSE A 286 N PRO A 287 1555 1555 1.35
LINK C LEU B 154 N MSE B 155 1555 1555 1.34
LINK C MSE B 155 N SER B 156 1555 1555 1.35
LINK C PRO B 204 N MSE B 205 1555 1555 1.32
LINK C MSE B 205 N THR B 206 1555 1555 1.34
LINK C ALA B 272 N MSE B 273 1555 1555 1.33
LINK C MSE B 273 N SER B 274 1555 1555 1.34
LINK C ARG B 285 N MSE B 286 1555 1555 1.33
LINK C MSE B 286 N PRO B 287 1555 1555 1.35
CISPEP 1 PHE A 183 PRO A 184 0 7.84
CISPEP 2 PHE B 183 PRO B 184 0 2.37
SITE 1 AC1 1 ARG B 111
SITE 1 AC2 6 SER A 145 ALA A 146 GLN A 149 GLY A 172
SITE 2 AC2 6 PRO A 222 ARG A 234
SITE 1 AC3 7 SER B 145 ALA B 146 GLN B 149 GLY B 172
SITE 2 AC3 7 ASN B 220 PRO B 222 ARG B 234
SITE 1 AC4 5 GLY B 59 TYR B 67 HIS B 144 SER B 145
SITE 2 AC4 5 HIS B 268
SITE 1 AC5 3 THR A 105 ALA A 107 ASN A 109
SITE 1 AC6 2 TYR B 45 GLY B 46
SITE 1 AC7 5 GLY A 59 TYR A 67 HIS A 144 SER A 145
SITE 2 AC7 5 HIS A 268
SITE 1 AC8 4 ARG A 21 SER B 88 ASP B 89 GLU B 90
SITE 1 AC9 3 ASP B 188 GLY B 189 GLY B 191
SITE 1 BC1 4 GLY B 94 GLU B 96 ARG B 285 ASP B 288
SITE 1 BC2 3 HIS A 18 ALA A 19 TYR A 45
SITE 1 BC3 3 GLY A 94 GLU A 96 ARG A 285
SITE 1 BC4 2 ASP A 288 ALA A 289
SITE 1 BC5 4 ASN A 63 GLY A 64 ALA A 65 ASP A 66
SITE 1 BC6 4 ASN B 63 GLY B 64 ALA B 65 ASP B 66
SITE 1 BC7 3 ALA B 33 ASP B 34 ARG B 35
CRYST1 41.879 83.710 90.792 90.00 92.68 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 0.023878 0.000000 0.001119 0.00000
SCALE2 0.000000 0.011946 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011026 0.00000
TER 2290 ALA A 296
TER 4650 ALA B 296
MASTER 396 0 26 25 16 0 20 6 5159 2 149 48
END |