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HEADER HYDROLASE 31-JUL-13 4LYE
TITLE CRYSTAL STRUCTURE OF THE S105A MUTANT OF A C-C HYDROLASE, DXNB2 FROM
TITLE 2 SPHINGOMONAS WITTICHII RW1, IN COMPLEX WITH SUBSTRATE HOPDA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MCP HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA/BETA HYDROLASE FOLD;
COMPND 5 EC: 3.7.1.8;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SPHINGOMONAS WITTICHII;
SOURCE 3 ORGANISM_TAXID: 392499;
SOURCE 4 STRAIN: RW1;
SOURCE 5 GENE: DXNB2, SWIT_3055;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 668369;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5A;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PEMDXN1
KEYWDS META-CLEAVAGE PRODUCT HYDROLASE, C-C BOND HYDROLASE, ALPHA-BETA
KEYWDS 2 HYDROLASE, DIBENZO-P-DIOXIN DEGRADATION, DIBENZOFURAN DEGRADATION,
KEYWDS 3 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GHOSH,J.T.BOLIN
REVDAT 1 09-OCT-13 4LYE 0
JRNL AUTH A.C.RUZZINI,S.BHOWMIK,S.GHOSH,K.C.YAM,J.T.BOLIN,L.D.ELTIS
JRNL TITL A SUBSTRATE-ASSISTED MECHANISM OF NUCLEOPHILE ACTIVATION IN
JRNL TITL 2 A SER-HIS-ASP CONTAINING C-C BOND HYDROLASE.
JRNL REF BIOCHEMISTRY 2013
JRNL REFN ISSN 0006-2960
JRNL PMID 24067021
JRNL DOI 10.1021/BI401156A
REMARK 2
REMARK 2 RESOLUTION. 2.33 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
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) : 2.33
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 19693
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.234
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1006
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) : 2.33
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1331
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2900
REMARK 3 BIN FREE R VALUE SET COUNT : 73
REMARK 3 BIN FREE R VALUE : 0.3710
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2108
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 16
REMARK 3 SOLVENT ATOMS : 72
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.58000
REMARK 3 B22 (A**2) : 0.58000
REMARK 3 B33 (A**2) : -1.88000
REMARK 3 B12 (A**2) : 0.58000
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): 0.207
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.143
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.332
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2174 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2044 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2947 ; 1.415 ; 1.959
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4699 ; 0.764 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 275 ; 5.895 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 94 ;34.462 ;23.936
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 344 ;15.924 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;16.502 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 322 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2494 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 504 ; 0.001 ; 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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 1103 ; 2.916 ; 4.598
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1102 ; 2.915 ; 4.594
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1377 ; 4.312 ; 6.890
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 4LYE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-13.
REMARK 100 THE RCSB ID CODE IS RCSB081241.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 14-BM-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9787
REMARK 200 MONOCHROMATOR : GE(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19800
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.330
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 10.700
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.41
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 10.20
REMARK 200 R MERGE FOR SHELL (I) : 0.45900
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M SODIUM MALONATE, PH 6.8, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 226.16800
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 113.08400
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 169.62600
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 56.54200
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 282.71000
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 226.16800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 113.08400
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 56.54200
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 169.62600
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 282.71000
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 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 350 BIOMT1 2 0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 -0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 56.54200
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 ASP A 277
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 ASP A 13 59.94 32.41
REMARK 500 ALA A 70 79.19 -118.18
REMARK 500 ALA A 105 -121.75 51.11
REMARK 500 ASN A 133 32.89 -146.41
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 HPK A 301
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4LXG RELATED DB: PDB
REMARK 900 DXNB2 WILD TYPE
REMARK 900 RELATED ID: 4LYD RELATED DB: PDB
REMARK 900 DXNB2 S105A
REMARK 900 RELATED ID: 4LXH RELATED DB: PDB
REMARK 900 DXNB2 S105A IN COMPLEX WITH 3-CL-HOPDA
REMARK 900 RELATED ID: 4LXI RELATED DB: PDB
REMARK 900 DXNB2 S105A IN COMPLEX WITH 5,8-DIF-HOPDA
DBREF 4LYE A 1 277 UNP A5VAT9 A5VAT9_SPHWW 1 277
SEQADV 4LYE ALA A 105 UNP A5VAT9 SER 105 ENGINEERED MUTATION
SEQRES 1 A 277 MET PHE GLU GLN PHE GLU SER LYS PHE ILE ASP CYS ASP
SEQRES 2 A 277 GLY ILE ARG THR HIS TYR ILE GLU MET GLY GLU GLY ASP
SEQRES 3 A 277 PRO LEU VAL LEU VAL HIS GLY GLY GLY ALA GLY ALA ASP
SEQRES 4 A 277 GLY ARG SER ASN PHE ALA ASP ASN PHE PRO ILE PHE ALA
SEQRES 5 A 277 ARG HIS MET ARG VAL ILE ALA TYR ASP MET VAL GLY PHE
SEQRES 6 A 277 GLY GLN THR ASP ALA PRO ASP PRO ALA GLY PHE ALA TYR
SEQRES 7 A 277 THR GLN ALA ALA ARG THR ASP HIS LEU ILE SER PHE ILE
SEQRES 8 A 277 LYS ALA LEU GLY LEU SER LYS ILE CYS LEU ILE GLY ASN
SEQRES 9 A 277 ALA MET GLY GLY THR THR ALA CYS GLY ALA ALA LEU LYS
SEQRES 10 A 277 ALA PRO GLU LEU ILE ASP ARG LEU VAL LEU MET GLY ALA
SEQRES 11 A 277 ALA VAL ASN ILE SER PRO ASP ASP MET VAL ALA ASN ARG
SEQRES 12 A 277 ASP ASP LEU ALA ALA VAL MET SER TYR ASP GLY SER GLU
SEQRES 13 A 277 GLU GLY MET ARG LYS ILE ILE ALA ALA LEU THR HIS SER
SEQRES 14 A 277 TYR GLN PRO THR ASP ASP ILE VAL HIS TYR ARG HIS GLU
SEQRES 15 A 277 ALA SER LEU ARG PRO THR THR THR ALA ALA TYR LYS ALA
SEQRES 16 A 277 THR MET GLY TRP ALA LYS GLN ASN GLY LEU TYR TYR SER
SEQRES 17 A 277 PRO GLU GLN LEU ALA SER LEU THR MET PRO VAL LEU VAL
SEQRES 18 A 277 LEU GLY GLY LYS ASN ASP VAL MET VAL PRO VAL ARG LYS
SEQRES 19 A 277 VAL ILE ASP GLN ILE LEU ALA ILE PRO GLN ALA ILE GLY
SEQRES 20 A 277 HIS VAL PHE PRO ASN CYS GLY HIS TRP VAL MET ILE GLU
SEQRES 21 A 277 TYR PRO GLU GLU PHE CYS THR GLN THR LEU HIS PHE PHE
SEQRES 22 A 277 GLY LYS LEU ASP
HET HPK A 301 16
HETNAM HPK (3E)-2,6-DIOXO-6-PHENYLHEX-3-ENOATE
FORMUL 2 HPK C12 H9 O4 1-
FORMUL 3 HOH *72(H2 O)
HELIX 1 1 ASP A 39 ALA A 45 1 7
HELIX 2 2 ASN A 47 ARG A 53 1 7
HELIX 3 3 THR A 79 LEU A 94 1 16
HELIX 4 4 ALA A 105 ALA A 118 1 14
HELIX 5 5 SER A 135 ASN A 142 1 8
HELIX 6 6 ASN A 142 SER A 151 1 10
HELIX 7 7 SER A 155 THR A 167 1 13
HELIX 8 8 THR A 173 LEU A 185 1 13
HELIX 9 9 ARG A 186 GLY A 204 1 19
HELIX 10 10 SER A 208 SER A 214 1 7
HELIX 11 11 PRO A 231 ILE A 242 1 12
HELIX 12 12 TRP A 256 TYR A 261 1 6
HELIX 13 13 TYR A 261 PHE A 273 1 13
SHEET 1 A 8 LYS A 8 CYS A 12 0
SHEET 2 A 8 ILE A 15 MET A 22 -1 O ILE A 15 N CYS A 12
SHEET 3 A 8 ARG A 56 TYR A 60 -1 O VAL A 57 N MET A 22
SHEET 4 A 8 PRO A 27 VAL A 31 1 N LEU A 30 O ILE A 58
SHEET 5 A 8 ILE A 99 ASN A 104 1 O ILE A 102 N VAL A 31
SHEET 6 A 8 ILE A 122 MET A 128 1 O MET A 128 N GLY A 103
SHEET 7 A 8 VAL A 219 GLY A 224 1 O LEU A 222 N LEU A 127
SHEET 8 A 8 ILE A 246 PHE A 250 1 O ILE A 246 N VAL A 219
SHEET 1 B 2 ASN A 133 ILE A 134 0
SHEET 2 B 2 LEU A 205 TYR A 206 -1 O LEU A 205 N ILE A 134
SITE 1 AC1 16 GLY A 33 GLY A 34 GLY A 35 ALA A 38
SITE 2 AC1 16 ASN A 43 ASN A 104 ALA A 105 MET A 106
SITE 3 AC1 16 LEU A 146 MET A 150 LEU A 166 ARG A 180
SITE 4 AC1 16 MET A 229 HIS A 255 TRP A 256 HOH A 469
CRYST1 65.715 65.715 339.252 90.00 90.00 120.00 P 65 2 2 12
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 0.015217 0.008786 0.000000 0.00000
SCALE2 0.000000 0.017571 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002948 0.00000
TER 2109 LEU A 276
MASTER 312 0 1 13 10 0 4 6 2196 1 16 22
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