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HEADER HYDROLASE 09-DEC-04 2BFN
TITLE THE CRYSTAL STRUCTURE OF THE COMPLEX OF THE HALOALKANE
TITLE 2 DEHALOGENASE LINB WITH THE PRODUCT OF DEHALOGENATION
TITLE 3 REACTION 1,2-DICHLOROPROPANE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOGENALKANE DEHALOGENASE;
COMPND 3 SYNONYM: 1,3,4,6-TETRACHLORO-1,4-CYCLOHEXADIENE
COMPND 4 HYDROLASE, 1,4-TCDN CHLOROHYDROLASE;
COMPND 5 CHAIN: A;
COMPND 6 EC 3.8.1.5
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOMONAS PAUCIMOBILIS;
SOURCE 3 STRAIN: UT26
KEYWDS HALOALKANE DEHALOGENASE LINB, 1,2,3-TRICHLOROPROPANE,
KEYWDS 2 HYDROLASE, ALPHA/BETA-HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR P.BANAS,M.OTYEPKA,P.JERABEK,J.VEVODOVA,M.BOHAC,J.DAMBORSKY
REVDAT 1 26-JUN-06 2BFN 0
JRNL AUTH P.BANAS,M.OTYEPKA,P.JERABEK,J.VEVODOVA,M.BOHAC,
JRNL AUTH 2 J.DAMBORSKY
JRNL TITL CRYSTAL STRUCTURE OF THE HALOALKANE DEHALOGENASE
JRNL TITL 2 LINB WITH THE PRODUCT OF DEHALOGENATION
JRNL TITL 3 REACTION 1,2-DICHLOROPROPANE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.MAREK,J.VEVODOVA,I.KUTA SMATANOVA,Y.NAGATA,
REMARK 1 AUTH 2 L.A.SVENSSON,J.NEWMAN,M.TAKAGI,J.DAMBORSKY
REMARK 1 TITL CRYSTAL STRUCTURE OF THE HALOALKANE DEHALOGENASE
REMARK 1 TITL 2 FROM SPHINGOMONAS PAUCIMOBILIS UT26
REMARK 1 REF BIOCHEMISTRY V. 39 14082 2000
REMARK 1 REFN ASTM BICHAW US ISSN 0006-2960
REMARK 2
REMARK 2 RESOLUTION. 1.6 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC_5.1.24 24/04/2001
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.600
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 72.548
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.72
REMARK 3 NUMBER OF REFLECTIONS : 34207
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) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.1487
REMARK 3 FREE R VALUE : 0.1705
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.08
REMARK 3 FREE R VALUE TEST SET COUNT : 1796
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.600
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.6416
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2464
REMARK 3 BIN R VALUE (WORKING SET) : 0.153
REMARK 3 BIN FREE R VALUE SET COUNT : 121
REMARK 3 BIN FREE R VALUE : 0.195
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2396
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 337
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.158
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.047
REMARK 3 B22 (A**2) : -0.273
REMARK 3 B33 (A**2) : 0.319
REMARK 3 B12 (A**2) : 0.000
REMARK 3 B13 (A**2) : 0.000
REMARK 3 B23 (A**2) : 0.000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.082
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.078
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.044
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.211
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED (A): 2457 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2217 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED (DEGREES): 3339 ; 1.478 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5132 ; 0.922 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED (A): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES OTHERS (A): 533 ; 0.012 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2689 ; 0.254 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1418 ; 0.083 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): 30 ; 0.272 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL PLUS MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS :1.400
REMARK 3 ION PROBE RADIUS : 0.800
REMARK 3 SHRINKAGE RADIUS : 0.800
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2BFN COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 10-DEC-2004.
REMARK 100 THE EBI ID CODE IS EBI-21920.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-DEC-2001
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF BEAMLINE ID14-EH2
REMARK 200 BEAMLINE : ID14-EH2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.93
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36132
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.60
REMARK 200 RESOLUTION RANGE LOW (A) : 30.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 9
REMARK 200 R MERGE (I) : 0.05
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.17
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 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: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1CV2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.5
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+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 25.28550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 36.65550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.07100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 36.65550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.28550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.07100
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 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 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 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 DISTANCE
REMARK 500 CD GLU A 94 O HOH Z 136 1.08
REMARK 500 OE1 GLU A 94 O HOH Z 136 0.76
REMARK 500 OE2 GLU A 94 O HOH Z 136 1.61
REMARK 500 ND1 HIS A 121 O HOH Z 157 2.12
REMARK 500 CE1 HIS A 121 O HOH Z 157 1.15
REMARK 500 NE2 GLN A 165 O HOH Z 203 2.20
REMARK 500 CG ASP A 166 O HOH Z 206 1.66
REMARK 500 OD1 ASP A 166 O HOH Z 206 0.92
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 CE1 HIS A 121 CA CA A 1299 3655 1.72
REMARK 500 O HOH Z 84 O HOH Z 130 3645 2.16
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 FOR METAL ATOM CA CA A1299 THE COORDINATION ANGLES ARE:
REMARK 600 1 HIS 121A NE2
REMARK 600 2 ASP 166A OD1 136.0
REMARK 600 3 ASP 166A OD2 108.9 52.3
REMARK 600 4 HOH 157Z O 62.7 128.7 77.1
REMARK 600 5 HOH 206Z O 116.3 20.9 58.6 133.4
REMARK 600 6 GLN 165A OE1 130.3 93.6 102.8 89.4 112.6
REMARK 600 7 HIS 121A ND1 57.8 166.1 127.6 51.1 171.7 72.7
REMARK 600 1 2 3 4 5 6
REMARK 600
REMARK 600 FOR METAL ATOM CA CA A1300 THE COORDINATION ANGLES ARE:
REMARK 600 1 ASP 149A OD1
REMARK 600 2 ASP 149A OD1 24.6
REMARK 600 3 HOH 186Z O 92.6 115.7
REMARK 600 4 GLN 152A OE1 93.5 100.0 92.4
REMARK 600 5 HOH 185Z O 107.0 87.2 153.0 68.6
REMARK 600 6 HOH 274Z O 93.3 81.5 99.5 166.0 97.7
REMARK 600 7 HOH 273Z O 175.4 151.8 89.6 90.5 72.3 82.3
REMARK 600 1 2 3 4 5 6
REMARK 600
REMARK 600 FOR METAL ATOM CA CA A1301 THE COORDINATION ANGLES ARE:
REMARK 600 1 HOH 18Z O
REMARK 600 2 HOH 39Z O 64.8
REMARK 600 3 HOH 36Z O 143.3 78.9
REMARK 600 4 HOH 37Z O 84.9 73.0 79.5
REMARK 600 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 SITE_DESCRIPTION: D2P BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 SITE_DESCRIPTION: CL BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE FOR CHAIN A
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 SITE_DESCRIPTION: CA BINDING SITE FOR CHAIN A
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CV2 RELATED DB: PDB
REMARK 900 HYDROLYTIC HALOALKANE DEHALOGENASE LINB FROM
REMARK 900 SPHINGOMONAS PAUCIMOBILIS UT26 AT 1.6 A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1D07 RELATED DB: PDB
REMARK 900 HYDROLYTIC HALOALKANE DEHALOGENASE LINB FROM
REMARK 900 SPHINGOMONAS PAUCIMOBILIS UT26 WITH 1,3-
REMARK 900 PROPANEDIOL, A PRODUCT OF DEBROMIDATION OF
REMARK 900 DIBROMPROPANE, AT 2.0A RESOLUTION
REMARK 900 RELATED ID: 1G42 RELATED DB: PDB
REMARK 900 STRUCTURE OF 1,3,4,6-TETRACHLORO-1,4-
REMARK 900 CYCLOHEXADIENEHYDROLASE (LINB) FROM SPHINGOMONAS
REMARK 900 PAUCIMOBILIS COMPLEXEDWITH 1,2-DICHLOROPROPANE
REMARK 900 RELATED ID: 1G4H RELATED DB: PDB
REMARK 900 LINB COMPLEXED WITH BUTAN-1-OL
REMARK 900 RELATED ID: 1G5F RELATED DB: PDB
REMARK 900 STRUCTURE OF LINB COMPLEXED WITH 1,2-
REMARK 900 DICHLOROETHANE
REMARK 900 RELATED ID: 1IZ7 RELATED DB: PDB
REMARK 900 RE-REFINEMENT OF THE STRUCTURE OF HYDROLYTIC
REMARK 900 HALOALKANEDEHALOGENASE LINB FROM SPHINGOMONAS
REMARK 900 PAUCIMOBILIS UT26 AT1.6 A RESOLUTION
REMARK 900 RELATED ID: 1IZ8 RELATED DB: PDB
REMARK 900 RE-REFINEMENT OF THE STRUCTURE OF HYDROLYTIC
REMARK 900 HALOALKANEDEHALOGENASE LINB FROM SPHINGOMONAS
REMARK 900 PAUCIMOBILIS UT26 WITH1,3-PROPANEDIOL, A
REMARK 900 PRODUCT OF DEBROMIDATION OFDIBROMPROPANE, AT 2
REMARK 900 .0A RESOLUTION
REMARK 900 RELATED ID: 1K5P RELATED DB: PDB
REMARK 900 HYDROLYTIC HALOALKANE DEHALOGENASE LINB FROM
REMARK 900 SPHINGOMONASPAUCIMOBILIS UT26 AT 1.8A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1K63 RELATED DB: PDB
REMARK 900 COMPLEX OF HYDROLYTIC HALOALKANE DEHALOGENASE
REMARK 900 LINB FROMSPHINGOMONAS PAUCIMOBILIS WITH UT26 2
REMARK 900 -BROMO-2-PROPENE-1-OLAT 1.8A RESOLUTION
REMARK 900 RELATED ID: 1K6E RELATED DB: PDB
REMARK 900 COMPLEX OF HYDROLYTIC HALOALKANE DEHALOGENASE
REMARK 900 LINB FROMSPHINGOMONAS PAUCIMOBILIS UT26 WITH 1
REMARK 900 ,2-PROPANEDIOL(PRODUCT OF DEHALOGENATION OF
REMARK 900 1,2-DIBROMOPROPANE) AT 1.85A
REMARK 900 RELATED ID: 1MJ5 RELATED DB: PDB
REMARK 900 LINB (HALOALKANE DEHALOGENASE) FROM
REMARK 900 SPHINGOMONASPAUCIMOBILIS UT26 AT ATOMIC
REMARK 900 RESOLUTION
DBREF 2BFN A 1 1 PDB 2BFN 2BFN 1 1
DBREF 2BFN A 2 296 UNP P51698 LINB_PSEPA 1 295
SEQRES 1 A 296 MET SER LEU GLY ALA LYS PRO PHE GLY GLU LYS LYS PHE
SEQRES 2 A 296 ILE GLU ILE LYS GLY ARG ARG MET ALA TYR ILE ASP GLU
SEQRES 3 A 296 GLY THR GLY ASP PRO ILE LEU PHE GLN HIS GLY ASN PRO
SEQRES 4 A 296 THR SER SER TYR LEU TRP ARG ASN ILE MET PRO HIS CYS
SEQRES 5 A 296 ALA GLY LEU GLY ARG LEU ILE ALA CYS ASP LEU ILE GLY
SEQRES 6 A 296 MET GLY ASP SER ASP LYS LEU ASP PRO SER GLY PRO GLU
SEQRES 7 A 296 ARG TYR ALA TYR ALA GLU HIS ARG ASP TYR LEU ASP ALA
SEQRES 8 A 296 LEU TRP GLU ALA LEU ASP LEU GLY ASP ARG VAL VAL LEU
SEQRES 9 A 296 VAL VAL HIS ASP TRP GLY SER ALA LEU GLY PHE ASP TRP
SEQRES 10 A 296 ALA ARG ARG HIS ARG GLU ARG VAL GLN GLY ILE ALA TYR
SEQRES 11 A 296 MET GLU ALA ILE ALA MET PRO ILE GLU TRP ALA ASP PHE
SEQRES 12 A 296 PRO GLU GLN ASP ARG ASP LEU PHE GLN ALA PHE ARG SER
SEQRES 13 A 296 GLN ALA GLY GLU GLU LEU VAL LEU GLN ASP ASN VAL PHE
SEQRES 14 A 296 VAL GLU GLN VAL LEU PRO GLY LEU ILE LEU ARG PRO LEU
SEQRES 15 A 296 SER GLU ALA GLU MET ALA ALA TYR ARG GLU PRO PHE LEU
SEQRES 16 A 296 ALA ALA GLY GLU ALA ARG ARG PRO THR LEU SER TRP PRO
SEQRES 17 A 296 ARG GLN ILE PRO ILE ALA GLY THR PRO ALA ASP VAL VAL
SEQRES 18 A 296 ALA ILE ALA ARG ASP TYR ALA GLY TRP LEU SER GLU SER
SEQRES 19 A 296 PRO ILE PRO LYS LEU PHE ILE ASN ALA GLU PRO GLY ALA
SEQRES 20 A 296 LEU THR THR GLY ARG MET ARG ASP PHE CYS ARG THR TRP
SEQRES 21 A 296 PRO ASN GLN THR GLU ILE THR VAL ALA GLY ALA HIS PHE
SEQRES 22 A 296 ILE GLN GLU ASP SER PRO ASP GLU ILE GLY ALA ALA ILE
SEQRES 23 A 296 ALA ALA PHE VAL ARG ARG LEU ARG PRO ALA
HET D2P A1297 6
HET CL A1298 1
HET CA A1299 1
HET CA A1300 1
HET CA A1301 1
HETNAM CA CALCIUM ION
HETNAM CL CHLORIDE ION
HETNAM D2P (2S)-2,3-DICHLOROPROPAN-1-OL
FORMUL 2 CA 3(CA1 2+)
FORMUL 3 CL CL1 1-
FORMUL 4 D2P C3 H6 O1 CL2
FORMUL 5 HOH *337(H2 O1)
HELIX 1 1 SER A 41 ARG A 46 5 6
HELIX 2 2 ILE A 48 ALA A 53 5 6
HELIX 3 3 ALA A 81 LEU A 96 1 16
HELIX 4 4 ASP A 108 HIS A 121 1 14
HELIX 5 5 GLU A 139 PHE A 143 5 5
HELIX 6 6 PRO A 144 GLN A 146 5 3
HELIX 7 7 ASP A 147 ARG A 155 1 9
HELIX 8 8 ALA A 158 LEU A 164 1 7
HELIX 9 9 ASN A 167 GLN A 172 1 6
HELIX 10 10 GLN A 172 LEU A 177 1 6
HELIX 11 11 SER A 183 GLU A 192 1 10
HELIX 12 12 PRO A 193 LEU A 195 5 3
HELIX 13 13 GLY A 198 ALA A 200 5 3
HELIX 14 14 ARG A 201 ILE A 211 1 11
HELIX 15 15 PRO A 217 SER A 232 1 16
HELIX 16 16 THR A 250 ARG A 258 1 9
HELIX 17 17 PHE A 273 ASP A 277 5 5
HELIX 18 18 SER A 278 ARG A 294 1 17
SHEET 1 AA 8 LYS A 12 ILE A 16 0
SHEET 2 AA 8 ARG A 19 GLU A 26 -1 O ARG A 19 N ILE A 16
SHEET 3 AA 8 ARG A 57 CYS A 61 -1 O LEU A 58 N GLU A 26
SHEET 4 AA 8 PRO A 31 GLN A 35 1 O ILE A 32 N ILE A 59
SHEET 5 AA 8 VAL A 102 HIS A 107 1 O VAL A 103 N LEU A 33
SHEET 6 AA 8 VAL A 125 MET A 131 1 N GLN A 126 O VAL A 102
SHEET 7 AA 8 LYS A 238 PRO A 245 1 O LEU A 239 N TYR A 130
SHEET 8 AA 8 GLN A 263 GLY A 270 1 O THR A 264 N PHE A 240
LINK CA CA A1299 NE2 HIS A 121 1555 3645
LINK CA CA A1299 OD1 ASP A 166 1555 1555
LINK CA CA A1299 OD2 ASP A 166 1555 1555
LINK CA CA A1299 O HOH Z 157 1555 3645
LINK CA CA A1299 O HOH Z 206 1555 1555
LINK CA CA A1299 OE1 GLN A 165 1555 1555
LINK CA CA A1299 ND1 HIS A 121 1555 3645
LINK CA CA A1300 O HOH Z 185 1555 1555
LINK CA CA A1300 OD1BASP A 149 1555 1555
LINK CA CA A1300 O HOH Z 186 1555 1555
LINK CA CA A1300 OE1 GLN A 152 1555 1555
LINK CA CA A1300 O HOH Z 274 1555 4556
LINK CA CA A1300 O HOH Z 273 1555 4556
LINK CA CA A1300 OD1AASP A 149 1555 1555
LINK CA CA A1301 O HOH Z 39 1555 1555
LINK CA CA A1301 O HOH Z 36 1555 1555
LINK CA CA A1301 O HOH Z 37 1555 1555
LINK CA CA A1301 O HOH Z 18 1555 1555
CISPEP 1 ASN A 38 PRO A 39 0 -2.31
CISPEP 2 ASP A 73 PRO A 74 0 0.29
CISPEP 3 THR A 216 PRO A 217 0 -4.00
CISPEP 4 GLU A 244 PRO A 245 0 2.16
SITE 1 AC1 7 ASP A 108 PRO A 144 PHE A 151 ALA A 247
SITE 2 AC1 7 HIS A 272 HOH Z 152 HOH Z 337
SITE 1 AC2 4 ASN A 38 TRP A 109 PRO A 208 HOH Z 337
SITE 1 AC3 5 HIS A 121 GLN A 165 ASP A 166 HOH Z 157
SITE 2 AC3 5 HOH Z 206
SITE 1 AC4 6 ASP A 149 GLN A 152 HOH Z 185 HOH Z 186
SITE 2 AC4 6 HOH Z 273 HOH Z 274
SITE 1 AC5 4 HOH Z 18 HOH Z 36 HOH Z 37 HOH Z 39
CRYST1 50.571 72.142 73.311 90.00 90.00 90.00 P 21 21 21 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 0.019774 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013862 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013641 0.00000
TER 2397 ALA A 296
MASTER 365 0 5 18 8 0 8 6 2743 1 23 23
END |