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HEADER HYDROLASE 04-JAN-07 2OG1
TITLE CRYSTAL STRUCTURE OF BPHD, A C-C HYDROLASE FROM
TITLE 2 BURKHOLDERIA XENOVORANS LB400
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE
COMPND 3 HYDROLASE;
COMPND 4 CHAIN: A, B;
COMPND 5 EC: 3.7.1.8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BURKHOLDERIA XENOVORANS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 STRAIN: LB400;
SOURCE 5 GENE: BPHD;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PSS314
KEYWDS BPHD, ALPHA/BETA HYDROLASE, PCB DEGRADATION, META CLEAVAGE
KEYWDS 2 PRODUCT HYDROLASE, MCP HYDROLASE, 2-HYDROXY-6-OXO-6-
KEYWDS 3 PHENYLHEXA-2,4-DIENOATE HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.DAI,J.KE,J.T.BOLIN
REVDAT 1 16-JAN-07 2OG1 0
JRNL AUTH G.P.HORSMAN,J.KE,S.DAI,S.Y.SEAH,J.T.BOLIN,L.D.ELTIS
JRNL TITL KINETIC AND STRUCTURAL INSIGHT INTO THE MECHANISM
JRNL TITL 2 OF BPHD, A C-C BOND HYDROLASE FROM THE BIPHENYL
JRNL TITL 3 DEGRADATION PATHWAY
JRNL REF BIOCHEMISTRY V. 45 11071 2006
JRNL REFN ASTM BICHAW US ISSN 0006-2960
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 2428265.500
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.6
REMARK 3 NUMBER OF REFLECTIONS : 88125
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 SET) : 0.208
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 8856
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.002
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.70
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 81.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 11071
REMARK 3 BIN R VALUE (WORKING SET) : 0.2690
REMARK 3 BIN FREE R VALUE : 0.2920
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.20
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1262
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.008
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4532
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 469
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.32000
REMARK 3 B22 (A**2) : 0.32000
REMARK 3 B33 (A**2) : -0.64000
REMARK 3 B12 (A**2) : 1.25000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.20
REMARK 3 ESD FROM SIGMAA (A) : 0.15
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.22
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.16
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 23.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.70
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.120 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.770 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.760 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.720 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 50.25
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : LIGAND.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : LIGAND.TOP
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2OG1 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-2007.
REMARK 100 THE RCSB ID CODE IS RCSB041089.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-SEP-1998; 05-DEC-1998
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.20
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; APS
REMARK 200 BEAMLINE : 14-BM-D; 14-BM-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795; 0.9537,0.9793,0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 1; ADSC QUANTUM 1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88125
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
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 (%) : 96.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.63
REMARK 200 COMPLETENESS FOR SHELL (%) : 74.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.90
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0-2.4 M AMMONIUM SULFATE, 6-10%
REMARK 280 ETHANOL, 0.1M TRIS-HCL, PH 8.2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,1/3+Z
REMARK 290 3555 -X+Y,-X,2/3+Z
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,1/3+Z
REMARK 290 6555 X-Y,X,2/3+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 -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 22.24167
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 44.48333
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 0.00000
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 22.24167
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 44.48333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 67.50000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 116.91343
REMARK 350 BIOMT3 2 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 MET B 1
REMARK 465 THR B 2
REMARK 465 ALA B 3
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 52 CD1 TYR A 52 CE1 0.030
REMARK 500 MET A 171 SD MET A 171 CE 0.031
REMARK 500 ARG A 190 CB ARG A 190 CG -0.030
REMARK 500 MET B 98 SD MET B 98 CE -0.044
REMARK 500 MET B 135 SD MET B 135 CE -0.031
REMARK 500 MET B 135 SD MET B 135 CE -0.043
REMARK 500 PRO B 163 CG PRO B 163 CD 0.034
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: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY A 42 N - CA - C ANGL. DEV. = 7.1 DEGREES
REMARK 500 TYR A 52 N - CA - C ANGL. DEV. = 10.5 DEGREES
REMARK 500 ARG A 65 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 LEU A 68 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 ASP A 70 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 VAL A 81 N - CA - C ANGL. DEV. =-10.4 DEGREES
REMARK 500 HIS A 107 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 VAL A 109 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 GLY A 130 N - CA - C ANGL. DEV. = -7.6 DEGREES
REMARK 500 TYR A 177 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 LYS A 228 N - CA - C ANGL. DEV. = -7.5 DEGREES
REMARK 500 PRO A 241 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 HIS A 285 N - CA - C ANGL. DEV. = 9.1 DEGREES
REMARK 500 GLY B 234 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 HIS B 285 N - CA - C ANGL. DEV. = 7.5 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 112 -114.13 52.85
REMARK 500 SER B 112 -113.24 50.64
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 252 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH 266 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH 291 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH 343 DISTANCE = 5.23 ANGSTROMS
DBREF 2OG1 A 1 286 UNP P47229 BPHD_BURXL 1 286
DBREF 2OG1 B 1 286 UNP P47229 BPHD_BURXL 1 286
SEQRES 1 A 286 MET THR ALA LEU THR GLU SER SER THR SER LYS PHE VAL
SEQRES 2 A 286 LYS ILE ASN GLU LYS GLY PHE SER ASP PHE ASN ILE HIS
SEQRES 3 A 286 TYR ASN GLU ALA GLY ASN GLY GLU THR VAL ILE MET LEU
SEQRES 4 A 286 HIS GLY GLY GLY PRO GLY ALA GLY GLY TRP SER ASN TYR
SEQRES 5 A 286 TYR ARG ASN VAL GLY PRO PHE VAL ASP ALA GLY TYR ARG
SEQRES 6 A 286 VAL ILE LEU LYS ASP SER PRO GLY PHE ASN LYS SER ASP
SEQRES 7 A 286 ALA VAL VAL MET ASP GLU GLN ARG GLY LEU VAL ASN ALA
SEQRES 8 A 286 ARG ALA VAL LYS GLY LEU MET ASP ALA LEU ASP ILE ASP
SEQRES 9 A 286 ARG ALA HIS LEU VAL GLY ASN SER MET GLY GLY ALA THR
SEQRES 10 A 286 ALA LEU ASN PHE ALA LEU GLU TYR PRO ASP ARG ILE GLY
SEQRES 11 A 286 LYS LEU ILE LEU MET GLY PRO GLY GLY LEU GLY PRO SER
SEQRES 12 A 286 MET PHE ALA PRO MET PRO MET GLU GLY ILE LYS LEU LEU
SEQRES 13 A 286 PHE LYS LEU TYR ALA GLU PRO SER TYR GLU THR LEU LYS
SEQRES 14 A 286 GLN MET LEU GLN VAL PHE LEU TYR ASP GLN SER LEU ILE
SEQRES 15 A 286 THR GLU GLU LEU LEU GLN GLY ARG TRP GLU ALA ILE GLN
SEQRES 16 A 286 ARG GLN PRO GLU HIS LEU LYS ASN PHE LEU ILE SER ALA
SEQRES 17 A 286 GLN LYS ALA PRO LEU SER THR TRP ASP VAL THR ALA ARG
SEQRES 18 A 286 LEU GLY GLU ILE LYS ALA LYS THR PHE ILE THR TRP GLY
SEQRES 19 A 286 ARG ASP ASP ARG PHE VAL PRO LEU ASP HIS GLY LEU LYS
SEQRES 20 A 286 LEU LEU TRP ASN ILE ASP ASP ALA ARG LEU HIS VAL PHE
SEQRES 21 A 286 SER LYS CYS GLY HIS TRP ALA GLN TRP GLU HIS ALA ASP
SEQRES 22 A 286 GLU PHE ASN ARG LEU VAL ILE ASP PHE LEU ARG HIS ALA
SEQRES 1 B 286 MET THR ALA LEU THR GLU SER SER THR SER LYS PHE VAL
SEQRES 2 B 286 LYS ILE ASN GLU LYS GLY PHE SER ASP PHE ASN ILE HIS
SEQRES 3 B 286 TYR ASN GLU ALA GLY ASN GLY GLU THR VAL ILE MET LEU
SEQRES 4 B 286 HIS GLY GLY GLY PRO GLY ALA GLY GLY TRP SER ASN TYR
SEQRES 5 B 286 TYR ARG ASN VAL GLY PRO PHE VAL ASP ALA GLY TYR ARG
SEQRES 6 B 286 VAL ILE LEU LYS ASP SER PRO GLY PHE ASN LYS SER ASP
SEQRES 7 B 286 ALA VAL VAL MET ASP GLU GLN ARG GLY LEU VAL ASN ALA
SEQRES 8 B 286 ARG ALA VAL LYS GLY LEU MET ASP ALA LEU ASP ILE ASP
SEQRES 9 B 286 ARG ALA HIS LEU VAL GLY ASN SER MET GLY GLY ALA THR
SEQRES 10 B 286 ALA LEU ASN PHE ALA LEU GLU TYR PRO ASP ARG ILE GLY
SEQRES 11 B 286 LYS LEU ILE LEU MET GLY PRO GLY GLY LEU GLY PRO SER
SEQRES 12 B 286 MET PHE ALA PRO MET PRO MET GLU GLY ILE LYS LEU LEU
SEQRES 13 B 286 PHE LYS LEU TYR ALA GLU PRO SER TYR GLU THR LEU LYS
SEQRES 14 B 286 GLN MET LEU GLN VAL PHE LEU TYR ASP GLN SER LEU ILE
SEQRES 15 B 286 THR GLU GLU LEU LEU GLN GLY ARG TRP GLU ALA ILE GLN
SEQRES 16 B 286 ARG GLN PRO GLU HIS LEU LYS ASN PHE LEU ILE SER ALA
SEQRES 17 B 286 GLN LYS ALA PRO LEU SER THR TRP ASP VAL THR ALA ARG
SEQRES 18 B 286 LEU GLY GLU ILE LYS ALA LYS THR PHE ILE THR TRP GLY
SEQRES 19 B 286 ARG ASP ASP ARG PHE VAL PRO LEU ASP HIS GLY LEU LYS
SEQRES 20 B 286 LEU LEU TRP ASN ILE ASP ASP ALA ARG LEU HIS VAL PHE
SEQRES 21 B 286 SER LYS CYS GLY HIS TRP ALA GLN TRP GLU HIS ALA ASP
SEQRES 22 B 286 GLU PHE ASN ARG LEU VAL ILE ASP PHE LEU ARG HIS ALA
HET SO4 501 5
HET SO4 502 5
HET SO4 503 5
HET SO4 504 5
HET GOL 601 6
HET EOH 701 3
HET EOH 702 3
HET EOH 703 3
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETNAM EOH ETHANOL
FORMUL 3 SO4 4(O4 S1 2-)
FORMUL 7 GOL C3 H8 O3
FORMUL 8 EOH 3(C2 H6 O1)
FORMUL 11 HOH *469(H2 O1)
HELIX 1 1 THR A 5 THR A 9 1 5
HELIX 2 2 GLY A 47 TYR A 53 1 7
HELIX 3 3 ASN A 55 ALA A 62 1 8
HELIX 4 4 GLN A 85 LEU A 101 1 17
HELIX 5 5 SER A 112 TYR A 125 1 14
HELIX 6 6 MET A 150 GLU A 162 1 13
HELIX 7 7 SER A 164 PHE A 175 1 12
HELIX 8 8 ASP A 178 ILE A 182 5 5
HELIX 9 9 THR A 183 GLN A 197 1 15
HELIX 10 10 GLN A 197 ALA A 211 1 15
HELIX 11 11 PRO A 212 ASP A 217 5 6
HELIX 12 12 VAL A 218 ILE A 225 5 8
HELIX 13 13 LEU A 242 ILE A 252 1 11
HELIX 14 14 TRP A 266 HIS A 271 1 6
HELIX 15 15 HIS A 271 ALA A 286 1 16
HELIX 16 16 THR B 5 THR B 9 1 5
HELIX 17 17 GLY B 47 TYR B 53 1 7
HELIX 18 18 ASN B 55 ALA B 62 1 8
HELIX 19 19 GLN B 85 LEU B 101 1 17
HELIX 20 20 SER B 112 TYR B 125 1 14
HELIX 21 21 MET B 150 GLU B 162 1 13
HELIX 22 22 SER B 164 LEU B 176 1 13
HELIX 23 23 ASP B 178 ILE B 182 5 5
HELIX 24 24 THR B 183 GLN B 197 1 15
HELIX 25 25 GLN B 197 ALA B 211 1 15
HELIX 26 26 PRO B 212 TRP B 216 5 5
HELIX 27 27 VAL B 218 ILE B 225 5 8
HELIX 28 28 LEU B 242 ILE B 252 1 11
HELIX 29 29 TRP B 266 HIS B 271 1 6
HELIX 30 30 HIS B 271 ALA B 286 1 16
SHEET 1 A16 SER A 10 GLU A 17 0
SHEET 2 A16 PHE A 20 ALA A 30 -1 O TYR A 27 N LYS A 11
SHEET 3 A16 TYR A 64 LYS A 69 -1 O VAL A 66 N ALA A 30
SHEET 4 A16 GLU A 34 LEU A 39 1 N MET A 38 O ILE A 67
SHEET 5 A16 ALA A 106 ASN A 111 1 O VAL A 109 N LEU A 39
SHEET 6 A16 ILE A 129 MET A 135 1 O ILE A 133 N LEU A 108
SHEET 7 A16 THR A 229 GLY A 234 1 O THR A 232 N LEU A 134
SHEET 8 A16 ALA A 255 PHE A 260 1 O ARG A 256 N ILE A 231
SHEET 9 A16 ALA B 255 PHE B 260 -1 O VAL B 259 N LEU A 257
SHEET 10 A16 THR B 229 GLY B 234 1 N ILE B 231 O ARG B 256
SHEET 11 A16 ILE B 129 MET B 135 1 N LEU B 134 O THR B 232
SHEET 12 A16 ALA B 106 ASN B 111 1 N ALA B 106 O GLY B 130
SHEET 13 A16 GLU B 34 LEU B 39 1 N LEU B 39 O VAL B 109
SHEET 14 A16 TYR B 64 LYS B 69 1 O ARG B 65 N GLU B 34
SHEET 15 A16 PHE B 20 ALA B 30 -1 N ASN B 28 O LEU B 68
SHEET 16 A16 SER B 10 GLU B 17 -1 N VAL B 13 O ILE B 25
CISPEP 1 MET A 148 PRO A 149 0 0.95
CISPEP 2 MET B 148 PRO B 149 0 0.09
CRYST1 135.000 135.000 66.725 90.00 90.00 120.00 P 64 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 0.007407 0.004277 0.000000 0.00000
SCALE2 0.000000 0.008553 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014987 0.00000
TER 2285 ALA A 286
TER 4534 ALA B 286
MASTER 317 0 8 30 16 0 0 6 5036 2 35 44
END |