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HEADER HYDROLASE 18-JAN-09 3FWH
TITLE STRUCTURE OF HALOALKANE DEHALOGENASE MUTANT DHA15
TITLE 2 (I135F/C176Y) FROM RHODOCOCCUS RHODOCHROUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HALOALKANE DEHALOGENASE;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.8.1.5;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS SP.;
SOURCE 3 ORGANISM_TAXID: 1831;
SOURCE 4 STRAIN: NCIMB 13064;
SOURCE 5 GENE: DHAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAQN
KEYWDS ALPHA/BETA HYDROLASE CORE, HELICAL CAP DOMAIN, CATALYTIC
KEYWDS 2 TRIAD (ASP106, HIS272, GLU130), MUTANT, I135F, C176Y,
KEYWDS 3 HALOALKANES, DETOXIFICATION, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.GAVIRA,A STSIAPANAVA,M.KUTY,J.DOHNALEK,M.LAPKOUSKI,I
AUTHOR 2 KUTA SMATANOVA
REVDAT 1 02-FEB-10 3FWH 0
JRNL AUTH A.STSIAPANAVA,J.A.GAVIRA,J.DOHNALEK,M.KUTY,
JRNL AUTH 2 T.KOUDELAKOVA,J.DAMBORSKY,I.KUTA SMATANOVA
JRNL TITL ATOMIC RESOLUTION STUDIES OF MUTATED HALOALKANE
JRNL TITL 2 DEHALOGENASE DHAA FROM RHODOCOCCUS RHODOCHROUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.STSIAPANAVA,T.KOUDELAKOVA,M.LAPKOUSKI,M.PAVLOVA,
REMARK 1 AUTH 2 J.DAMBORSKY,I.KUTA SMATANOVA
REMARK 1 TITL CRYSTALS OF DHAA MUTANTS FROM RHODOCOCCUS
REMARK 1 TITL 2 RHODOCHROUS NCIMB 13064 DIFFRACTED TO ULTRAHIGH
REMARK 1 TITL 3 RESOLUTION: CRYSTALLIZATION AND PRELIMINARY
REMARK 1 TITL 4 DIFFRACTION ANALYSIS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. F64 137 2008
REMARK 1 REFN ESSN 1744-3091
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.KLVANA,M.PAVLOVA,T.KOUDELAKOVA,R.CHALOUPKOVA,
REMARK 1 AUTH 2 P.DVORAK,A.STSIAPANAVA,M.KUTY,I.KUTA SMATANOVA,
REMARK 1 AUTH 3 J.DOHNALEK,P.KULHANEK,R.C.WADE,J.DAMBORSKY
REMARK 1 TITL PATHWAYS AND MECHANISMS FOR PRODUCT RELEASE IN
REMARK 1 TITL 2 ENGINEERED HALOALKANE DEHALOGENASE DHAA EXPLORED
REMARK 1 TITL 3 USING CLASSICAL AND RANDOM ACCELERATION MOLECULAR
REMARK 1 TITL 4 DYNAMICS SIMULATIONS
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 1.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 1.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.4
REMARK 3 NUMBER OF REFLECTIONS : 77113
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) : 0.132
REMARK 3 R VALUE (WORKING SET) : 0.130
REMARK 3 FREE R VALUE : 0.162
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3872
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) : 1.22
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.25
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4551
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.57
REMARK 3 BIN R VALUE (WORKING SET) : 0.2670
REMARK 3 BIN FREE R VALUE SET COUNT : 224
REMARK 3 BIN FREE R VALUE : 0.2630
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2725
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 10
REMARK 3 SOLVENT ATOMS : 632
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 11.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.66000
REMARK 3 B22 (A**2) : -0.19000
REMARK 3 B33 (A**2) : -0.07000
REMARK 3 B12 (A**2) : 0.44000
REMARK 3 B13 (A**2) : 0.45000
REMARK 3 B23 (A**2) : -0.04000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.042
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.044
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.016
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.769
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2866 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 1996 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3973 ; 1.605 ; 1.957
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4872 ; 0.974 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 377 ; 5.863 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 156 ;30.902 ;23.462
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 463 ;14.245 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 25 ;21.933 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 402 ; 0.102 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3353 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 627 ; 0.003 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 565 ; 0.168 ; 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): 50 ; 0.204 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 99 ; 0.242 ; 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): 1684 ; 1.433 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 645 ; 2.025 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2788 ; 2.058 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1182 ; 2.731 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1159 ; 3.789 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 2866 ; 1.517 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 168 ; 8.381 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2733 ; 4.293 ; 3.000
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 : 1.40
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
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3FWH COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-09.
REMARK 100 THE RCSB ID CODE IS RCSB051128.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.15
REMARK 200 MONOCHROMATOR : MONOCHROMATOR: GE(111)
REMARK 200 TRIANGULAR BENT COMPRESSING 7
REMARK 200 FANKUCHEN CUT
REMARK 200 OPTICS : MIRROR: ELLIPTICALLY BENT 12
REMARK 200 QUARTZ SEGMENTS
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MAR SCANNER 345 MM PLATE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 77114
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.7
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 29.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 45.0
REMARK 200 DATA REDUNDANCY IN SHELL : 2.10
REMARK 200 R MERGE FOR SHELL (I) : 0.17900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 6.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1BN6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 % PEG 4 000, 8 % ISO-PROPANOL
REMARK 280 AND 100 MM NA-ACETATE, PH 7.5, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,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
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: 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 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 HIS A 298
REMARK 465 HIS A 299
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 OE2 GLU A 223 O HOH A 871 1545 2.06
REMARK 500 O HOH A 820 O HOH A 869 1655 2.11
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 PRO A 42 48.49 -105.39
REMARK 500 THR A 43 -159.83 -102.04
REMARK 500 GLU A 98 -93.35 -106.89
REMARK 500 ASP A 106 -126.93 54.39
REMARK 500 ARG A 153 47.87 -84.68
REMARK 500 ASP A 156 -73.95 -102.40
REMARK 500 VAL A 245 -73.09 -133.32
REMARK 500 LEU A 271 -97.06 -118.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FBW RELATED DB: PDB
REMARK 900 RELATED ID: 3G9X RELATED DB: PDB
DBREF 3FWH A 1 293 UNP P0A3G3 DHAA_RHOSO 1 293
SEQADV 3FWH PHE A 135 UNP P0A3G3 ILE 135 ENGINEERED
SEQADV 3FWH TYR A 176 UNP P0A3G3 CYS 176 ENGINEERED
SEQADV 3FWH HIS A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 3FWH HIS A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 3FWH HIS A 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 3FWH HIS A 297 UNP P0A3G3 EXPRESSION TAG
SEQADV 3FWH HIS A 298 UNP P0A3G3 EXPRESSION TAG
SEQADV 3FWH HIS A 299 UNP P0A3G3 EXPRESSION TAG
SEQRES 1 A 299 MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS
SEQRES 2 A 299 TYR VAL GLU VAL LEU GLY GLU ARG MET HIS TYR VAL ASP
SEQRES 3 A 299 VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS
SEQRES 4 A 299 GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE
SEQRES 5 A 299 PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP
SEQRES 6 A 299 LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP
SEQRES 7 A 299 TYR PHE PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE
SEQRES 8 A 299 ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE
SEQRES 9 A 299 HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS
SEQRES 10 A 299 ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA CYS MET GLU
SEQRES 11 A 299 PHE ILE ARG PRO PHE PRO THR TRP ASP GLU TRP PRO GLU
SEQRES 12 A 299 PHE ALA ARG GLU THR PHE GLN ALA PHE ARG THR ALA ASP
SEQRES 13 A 299 VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE
SEQRES 14 A 299 GLU GLY ALA LEU PRO LYS TYR VAL VAL ARG PRO LEU THR
SEQRES 15 A 299 GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS
SEQRES 16 A 299 PRO VAL ASP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU
SEQRES 17 A 299 LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE VAL ALA LEU
SEQRES 18 A 299 VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL
SEQRES 19 A 299 PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE
SEQRES 20 A 299 PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO
SEQRES 21 A 299 ASN CYS LYS THR VAL ASP ILE GLY PRO GLY LEU HIS TYR
SEQRES 22 A 299 LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE
SEQRES 23 A 299 ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS
HET ACT A 300 4
HET CL A 301 1
HET IPA A 302 4
HET CL A 303 1
HETNAM ACT ACETATE ION
HETNAM CL CHLORIDE ION
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 2 ACT C2 H3 O2 1-
FORMUL 3 CL 2(CL 1-)
FORMUL 4 IPA C3 H8 O
FORMUL 6 HOH *617(H2 O)
HELIX 1 1 SER A 44 ARG A 49 5 6
HELIX 2 2 ILE A 51 ALA A 56 1 6
HELIX 3 3 PHE A 80 LEU A 95 1 16
HELIX 4 4 ASP A 106 ASN A 119 1 14
HELIX 5 5 THR A 137 TRP A 141 5 5
HELIX 6 6 PRO A 142 PHE A 144 5 3
HELIX 7 7 ALA A 145 ARG A 153 1 9
HELIX 8 8 ASP A 156 ILE A 163 1 8
HELIX 9 9 ASN A 166 GLY A 171 1 6
HELIX 10 10 GLY A 171 TYR A 176 1 6
HELIX 11 11 THR A 182 GLU A 191 1 10
HELIX 12 12 PRO A 192 LEU A 194 5 3
HELIX 13 13 LYS A 195 ASP A 198 5 4
HELIX 14 14 ARG A 199 LEU A 209 1 11
HELIX 15 15 PRO A 215 SER A 232 1 18
HELIX 16 16 PRO A 248 LEU A 259 1 12
HELIX 17 17 TYR A 273 ASN A 278 1 6
HELIX 18 18 ASN A 278 LEU A 290 1 13
HELIX 19 19 PRO A 291 HIS A 294 5 4
SHEET 1 A 8 HIS A 13 VAL A 17 0
SHEET 2 A 8 GLU A 20 VAL A 27 -1 O GLU A 20 N VAL A 17
SHEET 3 A 8 CYS A 61 PRO A 64 -1 O CYS A 61 N VAL A 27
SHEET 4 A 8 VAL A 35 LEU A 38 1 N VAL A 35 O ILE A 62
SHEET 5 A 8 VAL A 100 HIS A 105 1 O VAL A 101 N LEU A 36
SHEET 6 A 8 VAL A 123 MET A 129 1 O ALA A 127 N LEU A 102
SHEET 7 A 8 LYS A 236 PRO A 243 1 O LEU A 237 N CYS A 128
SHEET 8 A 8 CYS A 262 GLY A 270 1 O ILE A 267 N TRP A 240
CISPEP 1 ASN A 41 PRO A 42 0 -3.38
CISPEP 2 GLU A 214 PRO A 215 0 -5.91
CISPEP 3 THR A 242 PRO A 243 0 5.20
SITE 1 AC1 7 THR A 33 HIS A 59 LYS A 124 LEU A 290
SITE 2 AC1 7 HIS A 294 HOH A 664 HOH A 809
SITE 1 AC2 4 ASN A 41 TRP A 107 PRO A 206 IPA A 302
SITE 1 AC3 5 ASN A 41 ASP A 106 HIS A 272 TYR A 273
SITE 2 AC3 5 CL A 301
SITE 1 AC4 4 GLU A 3 ILE A 4 GLY A 5 ASN A 50
CRYST1 42.524 44.370 46.541 115.48 98.41 109.60 P 1 1
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 0.023516 0.008374 0.009075 0.00000
SCALE2 0.000000 0.023924 0.014346 0.00000
SCALE3 0.000000 0.000000 0.025326 0.00000
END |