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HEADER HYDROLASE 15-FEB-09 3G9X
TITLE STRUCTURE OF HALOALKANE DEHALOGENASE DHAA14 MUTANT I135F FROM
TITLE 2 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: PUC18
KEYWDS ALPHA/BETA HYDROLASE, HELICAL CAP DOMAIN, CATALYTIC TRIAD (ASP106,
KEYWDS 2 HIS272, GLU130), MUTANT, I135F, HALOALKANES, DETOXIFICATION,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.GAVIRA,A.STSIAPANAVA,M.KUTY,M.LAPKOUSKI,J.DOHNALEK,I.KUTA
AUTHOR 2 SMATANOVA
REVDAT 1 28-APR-10 3G9X 0
JRNL AUTH A.STSIAPANAVA,J.A.GAVIRA,J.DOHNALEK,M.KUTY,T.KOUDELAKOVA,
JRNL AUTH 2 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 RHODOCHROUS NCIMB
REMARK 1 TITL 2 13064 DIFFRACTED TO ULTRAHIGH RESOLUTION: CRYSTALLIZATION
REMARK 1 TITL 3 AND PRELIMINARY DIFFRACTION ANALYSIS
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.F V. 64 137 2008
REMARK 1 REFN ESSN 1744-3091
REMARK 1 PMID 18259069
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.KLVANA,M.PAVLOVA,T.KOUDELAKOVA,R.CHALOUPKOVA,P.DVORAK,
REMARK 1 AUTH 2 A.STSIAPANAVA,M.KUTY,I.KUTA SMATANOVA,J.DOHNALEK,
REMARK 1 AUTH 3 P.KULHANEK,R.C.WADE,J.DAMBORSKY
REMARK 1 TITL PATHWAYS AND MECHANISMS FOR PRODUCT RELEASE IN ENGINEERED
REMARK 1 TITL 2 HALOALKANE DEHALOGENASE DHAA EXPLORED USING CLASSICAL AND
REMARK 1 TITL 3 RANDOM ACCELERATION MOLECULAR DYNAMICS SIMULATIONS
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 0.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : SHELXL-97
REMARK 3 AUTHORS : G.M.SHELDRICK
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 0.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 10.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 3 CROSS-VALIDATION METHOD : FREE R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (NO CUTOFF).
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : 0.115
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.115
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.137
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.006
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 8179
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 163371
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.111
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.111
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.133
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.023
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 7281
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 144939
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2372
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 520
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2881.55
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2132.70
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 64
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 25397
REMARK 3 NUMBER OF RESTRAINTS : 32628
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.015
REMARK 3 ANGLE DISTANCES (A) : 0.031
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.028
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.104
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.100
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.036
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.005
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.033
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: MASK
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT IN SHELXL97 WITH ANISOTROPIC
REMARK 3 ADPS FOR ALL PROTEIN ATOMS
REMARK 4
REMARK 4 3G9X COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-09.
REMARK 100 THE RCSB ID CODE IS RCSB051607.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-AUG-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
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) : 0.8158
REMARK 200 MONOCHROMATOR : GE(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 163495
REMARK 200 RESOLUTION RANGE HIGH (A) : 0.950
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.2
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.05900
REMARK 200 R SYM (I) : 0.05900
REMARK 200 FOR THE DATA SET : 26.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 0.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : 0.41800
REMARK 200 R SYM FOR SHELL (I) : 0.41800
REMARK 200 FOR SHELL : 4.400
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 (%): 40.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: [PROTEIN]=7-10 MG/ML IN 50MM TRIS-HCL
REMARK 280 BUFFER PH 7.5; [PRECIPITANT]=25% PEG 4000, 8% 2-PROPANOL IN 100MM
REMARK 280 SODIUM ACETATE., VAPOR DIFFUSION, SITTING DROP, 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 SER A 2
REMARK 465 GLU A 3
REMARK 465 HIS A 298
REMARK 465 HIS A 299
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 NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 21 CD - NE - CZ ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 30 NE - CZ - NH1 ANGL. DEV. = 11.6 DEGREES
REMARK 500 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -7.2 DEGREES
REMARK 500 ARG A 86 CD - NE - CZ ANGL. DEV. = 10.1 DEGREES
REMARK 500 ARG A 86 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 146 NH1 - CZ - NH2 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ARG A 146 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ASP A 156 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 ASP A 164 CB - CG - OD1 ANGL. DEV. = 14.4 DEGREES
REMARK 500 ASP A 164 CB - CG - OD2 ANGL. DEV. = -9.6 DEGREES
REMARK 500 ARG A 190 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG A 204 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH1 ANGL. DEV. = -3.4 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 PRO A 42 46.40 -104.99
REMARK 500 THR A 43 -160.53 -101.07
REMARK 500 GLU A 98 -95.84 -109.58
REMARK 500 ASP A 106 -129.59 55.67
REMARK 500 ARG A 153 47.85 -87.66
REMARK 500 ASP A 156 -73.20 -104.28
REMARK 500 VAL A 245 -73.76 -135.69
REMARK 500 LEU A 271 -99.52 -113.47
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 IPA A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1003
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FBW RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE MUTANT DHAA-04 (C176Y)
REMARK 900 RELATED ID: 3FWH RELATED DB: PDB
REMARK 900 HALOALKANE DEHALOGENASE MUTANT DHAA-15(I135F/C176Y)
DBREF 3G9X A 1 293 UNP P0A3G3 DHAA_RHOSO 1 293
SEQADV 3G9X PHE A 135 UNP P0A3G3 ILE 135 ENGINEERED
SEQADV 3G9X HIS A 294 UNP P0A3G3 EXPRESSION TAG
SEQADV 3G9X HIS A 295 UNP P0A3G3 EXPRESSION TAG
SEQADV 3G9X HIS A 296 UNP P0A3G3 EXPRESSION TAG
SEQADV 3G9X HIS A 297 UNP P0A3G3 EXPRESSION TAG
SEQADV 3G9X HIS A 298 UNP P0A3G3 EXPRESSION TAG
SEQADV 3G9X 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 CYS 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 IPA A1001 4
HET ACT A1002 4
HET CL A1003 1
HETNAM IPA ISOPROPYL ALCOHOL
HETNAM ACT ACETATE ION
HETNAM CL CHLORIDE ION
HETSYN IPA 2-PROPANOL
FORMUL 2 IPA C3 H8 O
FORMUL 3 ACT C2 H3 O2 1-
FORMUL 4 CL CL 1-
FORMUL 5 HOH *520(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 CYS 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 -3.66
CISPEP 2 GLU A 214 PRO A 215 0 -12.04
CISPEP 3 THR A 242 PRO A 243 0 8.27
SITE 1 AC1 6 ASN A 41 ASP A 106 HIS A 272 TYR A 273
SITE 2 AC1 6 CL A1003 HOH A2453
SITE 1 AC2 9 THR A 33 HIS A 59 LYS A 124 LEU A 290
SITE 2 AC2 9 HIS A 294 HOH A2067 HOH A2130 HOH A2438
SITE 3 AC2 9 HOH A2452
SITE 1 AC3 5 ASN A 41 TRP A 107 PHE A 205 PRO A 206
SITE 2 AC3 5 IPA A1001
CRYST1 42.730 44.440 46.630 115.50 97.87 109.52 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 0.023403 0.008297 0.008682 0.00000
SCALE2 0.000000 0.023874 0.014159 0.00000
SCALE3 0.000000 0.000000 0.025170 0.00000
MASTER 273 0 3 19 8 0 7 6 2901 1 8 23
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