| 3B12-pdb | HEADER HYDROLASE 19-JUN-11 3B12
TITLE CRYSTAL STRUCTURE OF THE FLUOROACETATE DEHALOGENASE D104 MUTANT FROM
TITLE 2 BURKHOLDERIA SP. FA1 IN COMPLEX WITH FLUOROACETATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLUOROACETATE DEHALOGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.8.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA SP.;
SOURCE 3 ORGANISM_TAXID: 36773;
SOURCE 4 STRAIN: FA1;
SOURCE 5 GENE: FAC-DEX;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS DEHALOGEASE, FLUOROACETATE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.OMI,K.HIROTSU
REVDAT 1 20-JUN-12 3B12 0
JRNL AUTH T.NAKAYAMA,T.KAMACHI,K.JITSUMORI,R.OMI,K.HIROTSU,N.ESAKI,
JRNL AUTH 2 T.KURIHARA,K.YOSHIZAWA
JRNL TITL SUBSTRATE SPECIFICITY OF FLUOROACETATE DEHALOGENASE: AN
JRNL TITL 2 INSIGHT FROM CRYSTALLOGRAPHIC ANALYSIS, FLUORESCENCE
JRNL TITL 3 SPECTROSCOPY, AND THEORETICAL COMPUTATIONS
JRNL REF CHEMISTRY 2012
JRNL REFN ISSN 0947-6539
JRNL PMID 22674735
JRNL DOI 10.1002/CHEM.201103369
REMARK 2
REMARK 2 RESOLUTION. 1.20 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
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 174938
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.185
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.900
REMARK 3 FREE R VALUE TEST SET COUNT : 19301
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) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 12802
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.1950
REMARK 3 BIN FREE R VALUE SET COUNT : 1448
REMARK 3 BIN FREE R VALUE : 0.1980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4634
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 561
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 8.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : 0.13000
REMARK 3 B33 (A**2) : -0.29000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.040
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.021
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.434
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.963
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4819 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6542 ; 1.142 ; 1.939
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 592 ; 5.050 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 247 ;33.993 ;22.227
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 708 ;10.430 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 47 ;16.000 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 662 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3873 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2417 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3289 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 438 ; 0.107 ; 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): 49 ; 0.177 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 21 ; 0.053 ; 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): 2978 ; 0.508 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4663 ; 0.840 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2085 ; 1.316 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1876 ; 1.992 ; 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 : 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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3B12 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUL-11.
REMARK 100 THE RCSB ID CODE IS RCSB029944.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-MAY-05
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 219357
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 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: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1Y37
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%(W/V) PEG 8000, 100MM TRIS-HCL
REMARK 280 BUFFER PH 8.5, 40MM MGCL2, 100MM FLUOROACETATE , VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 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 26.74850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.17700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.53250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.17700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 26.74850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.53250
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2240 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 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 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 GLY A 295
REMARK 465 ILE A 296
REMARK 465 HIS A 297
REMARK 465 GLN A 298
REMARK 465 THR A 299
REMARK 465 GLU A 300
REMARK 465 ARG A 301
REMARK 465 ARG A 302
REMARK 465 GLU A 303
REMARK 465 SER A 304
REMARK 465 GLY B 295
REMARK 465 ILE B 296
REMARK 465 HIS B 297
REMARK 465 GLN B 298
REMARK 465 THR B 299
REMARK 465 GLU B 300
REMARK 465 ARG B 301
REMARK 465 ARG B 302
REMARK 465 GLU B 303
REMARK 465 SER B 304
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 O HOH A 449 O HOH A 542 2.04
REMARK 500 O HOH B 474 O HOH B 540 2.06
REMARK 500 O HOH A 447 O HOH A 553 2.14
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 ALA A 104 -118.70 54.83
REMARK 500 TYR A 147 58.95 -106.84
REMARK 500 ASP A 167 77.21 -161.07
REMARK 500 THR A 217 -91.30 -126.62
REMARK 500 PHE A 272 36.23 -96.33
REMARK 500 ALA B 104 -118.83 55.29
REMARK 500 TYR B 147 59.10 -107.68
REMARK 500 ASP B 167 76.67 -163.39
REMARK 500 THR B 217 -92.47 -126.39
REMARK 500 PHE B 272 36.26 -94.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 219 OD2
REMARK 620 2 TYR B 77 O 110.7
REMARK 620 3 ASP B 211 OD1 135.6 104.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 219 OD2
REMARK 620 2 ASP A 211 OD1 139.4
REMARK 620 3 TYR A 77 O 109.1 104.3
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAH A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAH B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAH B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y37 RELATED DB: PDB
DBREF 3B12 A 1 304 UNP Q1JU72 DEHA_BURSP 1 304
DBREF 3B12 B 1 304 UNP Q1JU72 DEHA_BURSP 1 304
SEQADV 3B12 ALA A 104 UNP Q1JU72 ASP 104 ENGINEERED MUTATION
SEQADV 3B12 ALA B 104 UNP Q1JU72 ASP 104 ENGINEERED MUTATION
SEQRES 1 A 304 MET PHE GLU GLY PHE GLU ARG ARG LEU VAL ASP VAL GLY
SEQRES 2 A 304 ASP VAL THR ILE ASN CYS VAL VAL GLY GLY SER GLY PRO
SEQRES 3 A 304 ALA LEU LEU LEU LEU HIS GLY PHE PRO GLN ASN LEU HIS
SEQRES 4 A 304 MET TRP ALA ARG VAL ALA PRO LEU LEU ALA ASN GLU TYR
SEQRES 5 A 304 THR VAL VAL CYS ALA ASP LEU ARG GLY TYR GLY GLY SER
SEQRES 6 A 304 SER LYS PRO VAL GLY ALA PRO ASP HIS ALA ASN TYR SER
SEQRES 7 A 304 PHE ARG ALA MET ALA SER ASP GLN ARG GLU LEU MET ARG
SEQRES 8 A 304 THR LEU GLY PHE GLU ARG PHE HIS LEU VAL GLY HIS ALA
SEQRES 9 A 304 ARG GLY GLY ARG THR GLY HIS ARG MET ALA LEU ASP HIS
SEQRES 10 A 304 PRO ASP SER VAL LEU SER LEU ALA VAL LEU ASP ILE ILE
SEQRES 11 A 304 PRO THR TYR VAL MET PHE GLU GLU VAL ASP ARG PHE VAL
SEQRES 12 A 304 ALA ARG ALA TYR TRP HIS TRP TYR PHE LEU GLN GLN PRO
SEQRES 13 A 304 ALA PRO TYR PRO GLU LYS VAL ILE GLY ALA ASP PRO ASP
SEQRES 14 A 304 THR PHE TYR GLU GLY CYS LEU PHE GLY TRP GLY ALA THR
SEQRES 15 A 304 GLY ALA ASP GLY PHE ASP PRO GLU GLN LEU GLU GLU TYR
SEQRES 16 A 304 ARG LYS GLN TRP ARG ASP PRO ALA ALA ILE HIS GLY SER
SEQRES 17 A 304 CYS CYS ASP TYR ARG ALA GLY GLY THR ILE ASP PHE GLU
SEQRES 18 A 304 LEU ASP HIS GLY ASP LEU GLY ARG GLN VAL GLN CYS PRO
SEQRES 19 A 304 ALA LEU VAL PHE SER GLY SER ALA GLY LEU MET HIS SER
SEQRES 20 A 304 LEU PHE GLU MET GLN VAL VAL TRP ALA PRO ARG LEU ALA
SEQRES 21 A 304 ASN MET ARG PHE ALA SER LEU PRO GLY GLY HIS PHE PHE
SEQRES 22 A 304 VAL ASP ARG PHE PRO ASP ASP THR ALA ARG ILE LEU ARG
SEQRES 23 A 304 GLU PHE LEU SER ASP ALA ARG SER GLY ILE HIS GLN THR
SEQRES 24 A 304 GLU ARG ARG GLU SER
SEQRES 1 B 304 MET PHE GLU GLY PHE GLU ARG ARG LEU VAL ASP VAL GLY
SEQRES 2 B 304 ASP VAL THR ILE ASN CYS VAL VAL GLY GLY SER GLY PRO
SEQRES 3 B 304 ALA LEU LEU LEU LEU HIS GLY PHE PRO GLN ASN LEU HIS
SEQRES 4 B 304 MET TRP ALA ARG VAL ALA PRO LEU LEU ALA ASN GLU TYR
SEQRES 5 B 304 THR VAL VAL CYS ALA ASP LEU ARG GLY TYR GLY GLY SER
SEQRES 6 B 304 SER LYS PRO VAL GLY ALA PRO ASP HIS ALA ASN TYR SER
SEQRES 7 B 304 PHE ARG ALA MET ALA SER ASP GLN ARG GLU LEU MET ARG
SEQRES 8 B 304 THR LEU GLY PHE GLU ARG PHE HIS LEU VAL GLY HIS ALA
SEQRES 9 B 304 ARG GLY GLY ARG THR GLY HIS ARG MET ALA LEU ASP HIS
SEQRES 10 B 304 PRO ASP SER VAL LEU SER LEU ALA VAL LEU ASP ILE ILE
SEQRES 11 B 304 PRO THR TYR VAL MET PHE GLU GLU VAL ASP ARG PHE VAL
SEQRES 12 B 304 ALA ARG ALA TYR TRP HIS TRP TYR PHE LEU GLN GLN PRO
SEQRES 13 B 304 ALA PRO TYR PRO GLU LYS VAL ILE GLY ALA ASP PRO ASP
SEQRES 14 B 304 THR PHE TYR GLU GLY CYS LEU PHE GLY TRP GLY ALA THR
SEQRES 15 B 304 GLY ALA ASP GLY PHE ASP PRO GLU GLN LEU GLU GLU TYR
SEQRES 16 B 304 ARG LYS GLN TRP ARG ASP PRO ALA ALA ILE HIS GLY SER
SEQRES 17 B 304 CYS CYS ASP TYR ARG ALA GLY GLY THR ILE ASP PHE GLU
SEQRES 18 B 304 LEU ASP HIS GLY ASP LEU GLY ARG GLN VAL GLN CYS PRO
SEQRES 19 B 304 ALA LEU VAL PHE SER GLY SER ALA GLY LEU MET HIS SER
SEQRES 20 B 304 LEU PHE GLU MET GLN VAL VAL TRP ALA PRO ARG LEU ALA
SEQRES 21 B 304 ASN MET ARG PHE ALA SER LEU PRO GLY GLY HIS PHE PHE
SEQRES 22 B 304 VAL ASP ARG PHE PRO ASP ASP THR ALA ARG ILE LEU ARG
SEQRES 23 B 304 GLU PHE LEU SER ASP ALA ARG SER GLY ILE HIS GLN THR
SEQRES 24 B 304 GLU ARG ARG GLU SER
HET FAH A 501 5
HET MG A 503 1
HET FAH B 501 5
HET FAH B 502 5
HET MG B 503 1
HETNAM FAH FLUOROACETIC ACID
HETNAM MG MAGNESIUM ION
FORMUL 3 FAH 3(C2 H3 F O2)
FORMUL 4 MG 2(MG 2+)
FORMUL 8 HOH *561(H2 O)
HELIX 1 1 ASN A 37 ALA A 42 5 6
HELIX 2 2 ARG A 43 ALA A 49 1 7
HELIX 3 3 HIS A 74 TYR A 77 5 4
HELIX 4 4 SER A 78 LEU A 93 1 16
HELIX 5 5 ALA A 104 HIS A 117 1 14
HELIX 6 6 PRO A 131 GLU A 138 1 8
HELIX 7 7 ASP A 140 TYR A 147 1 8
HELIX 8 8 TRP A 148 LEU A 153 1 6
HELIX 9 9 PRO A 158 ASP A 167 1 10
HELIX 10 10 ASP A 167 GLY A 178 1 12
HELIX 11 11 GLY A 183 PHE A 187 5 5
HELIX 12 12 ASP A 188 ARG A 200 1 13
HELIX 13 13 ASP A 201 GLY A 216 1 16
HELIX 14 14 THR A 217 ASP A 226 1 10
HELIX 15 15 GLY A 243 PHE A 249 1 7
HELIX 16 16 GLU A 250 ALA A 256 1 7
HELIX 17 17 PRO A 257 LEU A 259 5 3
HELIX 18 18 PHE A 272 PHE A 277 1 6
HELIX 19 19 PHE A 277 SER A 294 1 18
HELIX 20 20 ASN B 37 ALA B 42 5 6
HELIX 21 21 ARG B 43 ALA B 49 1 7
HELIX 22 22 HIS B 74 TYR B 77 5 4
HELIX 23 23 SER B 78 LEU B 93 1 16
HELIX 24 24 ALA B 104 HIS B 117 1 14
HELIX 25 25 PRO B 131 GLU B 138 1 8
HELIX 26 26 ASP B 140 TYR B 147 1 8
HELIX 27 27 TRP B 148 LEU B 153 1 6
HELIX 28 28 PRO B 158 ALA B 166 1 9
HELIX 29 29 ASP B 167 GLY B 178 1 12
HELIX 30 30 GLY B 183 PHE B 187 5 5
HELIX 31 31 ASP B 188 ARG B 200 1 13
HELIX 32 32 ASP B 201 GLY B 216 1 16
HELIX 33 33 THR B 217 ASP B 226 1 10
HELIX 34 34 GLY B 243 PHE B 249 1 7
HELIX 35 35 GLU B 250 ALA B 256 1 7
HELIX 36 36 PRO B 257 LEU B 259 5 3
HELIX 37 37 PHE B 272 PHE B 277 1 6
HELIX 38 38 PHE B 277 SER B 294 1 18
SHEET 1 A 8 GLU A 6 ASP A 11 0
SHEET 2 A 8 THR A 16 GLY A 23 -1 O VAL A 21 N GLU A 6
SHEET 3 A 8 THR A 53 ALA A 57 -1 O VAL A 54 N GLY A 22
SHEET 4 A 8 ALA A 27 LEU A 31 1 N LEU A 28 O VAL A 55
SHEET 5 A 8 PHE A 98 HIS A 103 1 O HIS A 99 N LEU A 29
SHEET 6 A 8 VAL A 121 LEU A 127 1 O LEU A 127 N GLY A 102
SHEET 7 A 8 ALA A 235 GLY A 240 1 O LEU A 236 N VAL A 126
SHEET 8 A 8 MET A 262 LEU A 267 1 O ARG A 263 N VAL A 237
SHEET 1 B 8 GLU B 6 ASP B 11 0
SHEET 2 B 8 THR B 16 GLY B 23 -1 O VAL B 21 N GLU B 6
SHEET 3 B 8 THR B 53 ALA B 57 -1 O VAL B 54 N GLY B 22
SHEET 4 B 8 ALA B 27 LEU B 31 1 N LEU B 30 O VAL B 55
SHEET 5 B 8 PHE B 98 HIS B 103 1 O HIS B 99 N LEU B 29
SHEET 6 B 8 VAL B 121 LEU B 127 1 O LEU B 127 N GLY B 102
SHEET 7 B 8 ALA B 235 GLY B 240 1 O LEU B 236 N VAL B 126
SHEET 8 B 8 MET B 262 LEU B 267 1 O ARG B 263 N VAL B 237
LINK OD2 ASP B 219 MG MG B 503 1555 1555 2.59
LINK OD2 ASP A 219 MG MG A 503 1555 1555 2.62
LINK O TYR B 77 MG MG B 503 1555 1555 2.71
LINK OD1 ASP B 211 MG MG B 503 1555 1555 2.74
LINK OD1 ASP A 211 MG MG A 503 1555 1555 2.74
LINK O TYR A 77 MG MG A 503 1555 1555 2.74
CISPEP 1 PHE A 34 PRO A 35 0 -4.18
CISPEP 2 ALA A 157 PRO A 158 0 2.12
CISPEP 3 PHE B 34 PRO B 35 0 -5.02
CISPEP 4 ALA B 157 PRO B 158 0 1.97
SITE 1 AC1 9 ALA A 104 ARG A 105 ARG A 108 ILE A 129
SITE 2 AC1 9 HIS A 149 TRP A 150 TYR A 212 HIS A 271
SITE 3 AC1 9 HOH A 544
SITE 1 AC2 4 TYR A 77 PHE A 79 ASP A 211 ASP A 219
SITE 1 AC3 9 ALA B 104 ARG B 105 ARG B 108 ILE B 129
SITE 2 AC3 9 HIS B 149 TRP B 150 TYR B 212 HIS B 271
SITE 3 AC3 9 HOH B 440
SITE 1 AC4 7 HIS B 111 ASP B 223 LEU B 227 ARG B 258
SITE 2 AC4 7 HOH B 358 HOH B 459 HOH B 496
SITE 1 AC5 4 TYR B 77 PHE B 79 ASP B 211 ASP B 219
CRYST1 53.497 85.065 136.354 90.00 90.00 90.00 P 21 21 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 0.018693 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011756 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007334 0.00000
TER 2326 SER A 294
TER 4655 SER B 294
MASTER 344 0 5 38 16 0 10 6 5212 2 23 48
END
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