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HEADER HYDROLASE 20-NOV-08 3FBW
TITLE STRUCTURE OF RHODOCOCCUS RHODOCHROUS HALOALKANE DEHALOGENASE
TITLE 2 DHAA MUTANT C176Y
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;
COMPND 7 OTHER_DETAILS: THE ACTIVE SITE PARTIALLY OCCUPIED BY A
COMPND 8 SMALL LIGAND AND BY A CHLORIDE ION
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS RHODOCHROUS;
SOURCE 3 ORGANISM_TAXID: 1829;
SOURCE 4 STRAIN: NCIMB 13064;
SOURCE 5 GENE: DHAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PAQN
KEYWDS DETOXIFICATION, HYDROLASE, ALPHA/BETA-HYDROLASE, CATALYTIC
KEYWDS 2 TRIAD, HALIDE-BINDING SITE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.DOHNALEK,A.STSIAPANAVA,J.A.GAVIRA,I.KUTA SMATANOVA,M.KUTY
REVDAT 1 24-NOV-09 3FBW 0
JRNL AUTH A.STSIAPANAVA,J.DOHNALEK,M.KUTY,J.A.GAVIRA,
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 RHOODOCHROUS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.23 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) : 1.23
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 100.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
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) : 0.137
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : 0.137
REMARK 3 FREE R VALUE (NO CUTOFF) : 0.167
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 3.860
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : 3425
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 88731
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).
REMARK 3 R VALUE (WORKING + TEST SET, F>4SIG(F)) : 0.114
REMARK 3 R VALUE (WORKING SET, F>4SIG(F)) : 0.114
REMARK 3 FREE R VALUE (F>4SIG(F)) : 0.141
REMARK 3 FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 3.880
REMARK 3 FREE R VALUE TEST SET COUNT (F>4SIG(F)) : 2632
REMARK 3 TOTAL NUMBER OF REFLECTIONS (F>4SIG(F)) : 67869
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2692
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 454
REMARK 3
REMARK 3 MODEL REFINEMENT.
REMARK 3 OCCUPANCY SUM OF NON-HYDROGEN ATOMS : 2738.52
REMARK 3 OCCUPANCY SUM OF HYDROGEN ATOMS : 2267.90
REMARK 3 NUMBER OF DISCRETELY DISORDERED RESIDUES : 61
REMARK 3 NUMBER OF LEAST-SQUARES PARAMETERS : 26510
REMARK 3 NUMBER OF RESTRAINTS : 37060
REMARK 3
REMARK 3 RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 ANGLE DISTANCES (A) : 0.028
REMARK 3 SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000
REMARK 3 DISTANCES FROM RESTRAINT PLANES (A) : 0.027
REMARK 3 ZERO CHIRAL VOLUMES (A**3) : 0.080
REMARK 3 NON-ZERO CHIRAL VOLUMES (A**3) : 0.076
REMARK 3 ANTI-BUMPING DISTANCE RESTRAINTS (A) : 0.024
REMARK 3 RIGID-BOND ADP COMPONENTS (A**2) : 0.004
REMARK 3 SIMILAR ADP COMPONENTS (A**2) : 0.036
REMARK 3 APPROXIMATELY ISOTROPIC ADPS (A**2) : 0.031
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED: BABINET, SHELXL97 IMPLEMENTATION, G=1.007, U=
REMARK 3 4.133
REMARK 3
REMARK 3 STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER, LIGAND TARGET
REMARK 3 VALUES BASED ON AVERAGED BEST
REMARK 3 CAMBRIDGE STRUCTURAL DATABASE
REMARK 3 VALUES
REMARK 3 SPECIAL CASE: NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CONJUGATE GRADIENT LEAST SQUARES
REMARK 3 REFINEMENT IN SHELXL97 WITH ANISOTROPIC ADPS FOR ALL ATOMS
REMARK 3 EXCEPT FOR WATER MOLECULES ABOVE A CERTAIN ADP CUTTOF
REMARK 4
REMARK 4 3FBW COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-08.
REMARK 100 THE RCSB ID CODE IS RCSB050398.
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88814
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.230
REMARK 200 RESOLUTION RANGE LOW (A) : 100.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -999.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : 0.05600
REMARK 200 FOR THE DATA SET : 25.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.23
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.25
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.58100
REMARK 200 R SYM FOR SHELL (I) : 0.58100
REMARK 200 FOR SHELL : 4.200
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 (%): 44.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.08M BICINE, 8% PEG 8000, 0.08M
REMARK 280 MAGNESIUM CHLORIDE, PH 9.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 294K
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 21.33900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 46.54900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.14700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 46.54900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.33900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.14700
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: 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 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 HIS A 299
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 HIS A 295 CA C O CB CG ND1 CD2
REMARK 470 HIS A 295 CE1 NE2
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 30 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 30 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 PHE A 37 CB - CG - CD1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG A 60 NE - CZ - NH2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 ASP A 139 CB - CG - OD1 ANGL. DEV. = 7.5 DEGREES
REMARK 500 ASP A 139 CB - CG - OD2 ANGL. DEV. = -6.0 DEGREES
REMARK 500 ARG A 146 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 159 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 190 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 TYR A 225 CB - CG - CD1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH1 ANGL. DEV. = -5.1 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 TYR A 273 CB - CG - CD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 288 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 288 NE - CZ - NH2 ANGL. DEV. = -3.5 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 29 153.49 -49.40
REMARK 500 PRO A 42 47.44 -102.51
REMARK 500 THR A 43 -160.77 -103.22
REMARK 500 GLU A 98 -92.76 -109.45
REMARK 500 ASP A 106 -129.05 51.73
REMARK 500 ASP A 156 -54.00 68.19
REMARK 500 VAL A 245 -71.52 -135.75
REMARK 500 LEU A 271 -97.31 -118.23
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 A 527 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 19 O
REMARK 620 2 HOH A 741 O 82.6
REMARK 620 3 HOH A 672 O 95.5 176.5
REMARK 620 4 HOH A 732 O 176.3 94.3 87.5
REMARK 620 5 HOH A 648 O 91.2 93.2 89.8 90.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 528 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ARG A 153 O
REMARK 620 2 HOH A 857 O 91.0
REMARK 620 3 HOH A 907 O 87.1 95.8
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 BEZ A 501
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 521
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 522
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 523
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 524
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 525
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 526
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 527
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 528
DBREF 3FBW A 1 293 UNP P0A3G2 DHAA_RHORH 1 293
SEQADV 3FBW TYR A 176 UNP P0A3G2 CYS 176 ENGINEERED
SEQADV 3FBW HIS A 294 UNP P0A3G2 EXPRESSION TAG
SEQADV 3FBW HIS A 295 UNP P0A3G2 EXPRESSION TAG
SEQADV 3FBW HIS A 296 UNP P0A3G2 EXPRESSION TAG
SEQADV 3FBW HIS A 297 UNP P0A3G2 EXPRESSION TAG
SEQADV 3FBW HIS A 298 UNP P0A3G2 EXPRESSION TAG
SEQADV 3FBW HIS A 299 UNP P0A3G2 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 ILE 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 BEZ A 501 9
HET CL A 521 1
HET CL A 522 1
HET CL A 523 1
HET CL A 524 1
HET CL A 525 1
HET CL A 526 1
HET MG A 527 1
HET MG A 528 1
HETNAM BEZ BENZOIC ACID
HETNAM CL CHLORIDE ION
HETNAM MG MAGNESIUM ION
FORMUL 2 BEZ C7 H6 O2
FORMUL 3 CL 6(CL 1-)
FORMUL 9 MG 2(MG 2+)
FORMUL 11 HOH *454(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 LYS A 263 N LEU A 238
LINK O GLY A 19 MG MG A 527 1555 1555 2.25
LINK O AARG A 153 MG MG A 528 1555 1555 2.39
LINK MG MG A 527 O HOH A 741 1555 1555 2.13
LINK MG MG A 527 O HOH A 672 1555 1555 2.05
LINK MG MG A 527 O HOH A 732 1555 1555 2.41
LINK MG MG A 527 O HOH A 648 1555 1555 2.40
LINK MG MG A 528 O HOH A 857 1555 1555 2.43
LINK MG MG A 528 O HOH A 907 1555 1555 2.29
CISPEP 1 ASN A 41 PRO A 42 0 -7.29
CISPEP 2 GLU A 214 PRO A 215 0 -5.53
CISPEP 3 THR A 242 PRO A 243 0 3.27
SITE 1 AC1 12 ASN A 41 ASP A 106 TRP A 107 PHE A 168
SITE 2 AC1 12 TYR A 176 LEU A 209 HIS A 272 TYR A 273
SITE 3 AC1 12 CL A 521 HOH A 662 HOH A 699 HOH A 727
SITE 1 AC2 6 ASN A 41 TRP A 107 PHE A 205 PRO A 206
SITE 2 AC2 6 BEZ A 501 HOH A 662
SITE 1 AC3 3 ALA A 155 ASP A 156 ARG A 159
SITE 1 AC4 4 LEU A 77 ARG A 86 TYR A 87 PRO A 269
SITE 1 AC5 4 PHE A 8 HOH A 678 HOH A 974 HOH A 978
SITE 1 AC6 3 ASN A 119 PRO A 120 GLU A 121
SITE 1 AC7 4 ILE A 4 GLY A 5 ASN A 50 HOH A 814
SITE 1 AC8 7 GLY A 19 ASP A 277 HOH A 648 HOH A 672
SITE 2 AC8 7 HOH A 732 HOH A 741 HOH A 831
SITE 1 AC9 5 ARG A 153 HOH A 798 HOH A 857 HOH A 906
SITE 2 AC9 5 HOH A 907
CRYST1 42.678 76.294 93.098 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 0.023431 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013107 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010741 0.00000
END |