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HEADER HYDROLASE 08-MAY-09 3HEA
TITLE THE L29P/L124I MUTATION OF PSEUDOMONAS FLUORESCENS ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARYLESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: ARYL-ESTER HYDROLASE, PFE, PUTATIVE
COMPND 5 BROMOPEROXIDASE;
COMPND 6 EC: 3.1.1.2, 1.-.-.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS FLUORESCENS;
SOURCE 3 ORGANISM_TAXID: 294;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID
KEYWDS ALPHA/BETA HYDROLASE, ESTERASE, COVALENT ADDUCT, TETRAHEDRAL
KEYWDS 2 INTERMEDIATE, HYDROLASE, OXIDOREDUCTASE, PEROXIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.KAZLAUSKAS,J.D.SCHRAG,J.D.CHEESEMAN,K.L.MORLEY
REVDAT 1 23-MAR-10 3HEA 0
JRNL AUTH L.T.YIN DE,P.BERNHARDT,K.L.MORLEY,Y.JIANG,
JRNL AUTH 2 J.D.CHEESEMAN,V.PURPERO,J.D.SCHRAG,R.J.KAZLAUSKAS
JRNL TITL SWITCHING CATALYSIS FROM HYDROLYSIS TO
JRNL TITL 2 PERHYDROLYSIS IN PSEUDOMONAS FLUORESCENS ESTERASE.
JRNL REF BIOCHEMISTRY V. 49 1931 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20112920
JRNL DOI 10.1021/BI9021268
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.BERNHARDT,K.HULT,R.J.KAZLAUSKAS
REMARK 1 TITL MOLECULAR BASIS OF PERHYDROLASE ACTIVITY IN SERINE
REMARK 1 TITL 2 HYDROLASES.
REMARK 1 REF ANGEW.CHEM.INT.ED.ENGL. V. 44 2742 2005
REMARK 1 REFN ISSN 1433-7851
REMARK 1 PMID 15803517
REMARK 1 DOI 10.1002/ANIE.200463006
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.D.CHEESEMAN,A.TOCILJ,S.PARK,J.D.SCHRAG,
REMARK 1 AUTH 2 R.J.KAZLAUSKAS
REMARK 1 TITL STRUCTURE OF AN ARYL ESTERASE FROM PSEUDOMONAS
REMARK 1 TITL 2 FLUORESCENS.
REMARK 1 REF ACTA CRYSTALLOGR.,SECT.D V. 60 1237 2004
REMARK 1 REFN ISSN 0907-4449
REMARK 1 PMID 15213385
REMARK 1 DOI 10.1107/S0907444904010522
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.4.0069
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 219350
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 11625
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 15794
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.60
REMARK 3 BIN R VALUE (WORKING SET) : 0.2890
REMARK 3 BIN FREE R VALUE SET COUNT : 829
REMARK 3 BIN FREE R VALUE : 0.3080
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12888
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 250
REMARK 3 SOLVENT ATOMS : 1057
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.03000
REMARK 3 B22 (A**2) : -1.03000
REMARK 3 B33 (A**2) : 1.54000
REMARK 3 B12 (A**2) : -0.51000
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): 0.110
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.106
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.664
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.958
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.947
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13448 ; 0.006 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18275 ; 0.930 ; 1.965
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1682 ; 4.684 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 626 ;32.889 ;24.058
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2135 ;11.884 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 74 ;16.819 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1979 ; 0.071 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10271 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 8159 ; 0.361 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13140 ; 0.700 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5289 ; 1.084 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5102 ; 1.881 ; 4.500
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 0
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 1068 ; 0.10 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 1068 ; 0.10 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 C (A): 1068 ; 0.09 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 D (A): 1068 ; 0.07 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 E (A): 1068 ; 0.11 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 F (A): 1068 ; 0.15 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 983 ; 0.37 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 B (A): 983 ; 0.30 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 C (A): 983 ; 0.26 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 D (A): 983 ; 0.27 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 E (A): 983 ; 0.29 ; 5.00
REMARK 3 LOOSE POSITIONAL 1 F (A): 983 ; 0.32 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 1068 ; 0.45 ; 2.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 1068 ; 0.62 ; 2.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 1068 ; 0.34 ; 2.00
REMARK 3 MEDIUM THERMAL 1 D (A**2): 1068 ; 0.29 ; 2.00
REMARK 3 MEDIUM THERMAL 1 E (A**2): 1068 ; 0.41 ; 2.00
REMARK 3 MEDIUM THERMAL 1 F (A**2): 1068 ; 0.42 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 983 ; 0.46 ; 10.00
REMARK 3 LOOSE THERMAL 1 B (A**2): 983 ; 0.60 ; 10.00
REMARK 3 LOOSE THERMAL 1 C (A**2): 983 ; 0.37 ; 10.00
REMARK 3 LOOSE THERMAL 1 D (A**2): 983 ; 0.35 ; 10.00
REMARK 3 LOOSE THERMAL 1 E (A**2): 983 ; 0.47 ; 10.00
REMARK 3 LOOSE THERMAL 1 F (A**2): 983 ; 0.45 ; 10.00
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: NULL
REMARK 4
REMARK 4 3HEA COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAY-09.
REMARK 100 THE RCSB ID CODE IS RCSB053027.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-05
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 : NSLS
REMARK 200 BEAMLINE : X29A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : DOUBLE CRYSTAL MONOCHROMETER
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 231042
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 48.100
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.5
REMARK 200 DATA REDUNDANCY : 2.620
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05600
REMARK 200 FOR THE DATA SET : 10.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.54
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.31300
REMARK 200 FOR SHELL : 3.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: O
REMARK 200 STARTING MODEL: PDB ENTRY 1VA4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.7 M AMMONIUM PHOSPHATE, 0.1 M NA,
REMARK 280 K PHOSPHATE, PH 7.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
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
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 85.46667
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 42.73333
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27760 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 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 62.36 -106.19
REMARK 500 LEU A 30 -147.26 -103.65
REMARK 500 ASP A 31 -168.49 -160.10
REMARK 500 SER A 94 -122.85 58.71
REMARK 500 PHE A 125 -65.44 -104.39
REMARK 500 TYR A 131 57.71 -147.17
REMARK 500 ASP A 150 81.60 -163.00
REMARK 500 THR A 230 -92.44 -126.08
REMARK 500 PRO B 29 61.05 -106.93
REMARK 500 LEU B 30 -147.29 -101.03
REMARK 500 GLN B 62 78.10 -118.59
REMARK 500 SER B 94 -126.10 55.90
REMARK 500 PHE B 125 -61.27 -109.44
REMARK 500 ASP B 150 85.49 -160.02
REMARK 500 GLN B 169 153.46 -48.64
REMARK 500 THR B 230 -95.52 -126.56
REMARK 500 PRO C 29 61.50 -107.02
REMARK 500 LEU C 30 -146.51 -101.44
REMARK 500 SER C 94 -124.84 60.53
REMARK 500 PHE C 125 -60.38 -105.45
REMARK 500 ASP C 150 81.87 -158.60
REMARK 500 THR C 230 -90.97 -121.77
REMARK 500 PRO D 29 60.61 -109.52
REMARK 500 LEU D 30 -145.66 -99.93
REMARK 500 GLN D 62 71.59 -119.78
REMARK 500 SER D 94 -124.93 59.24
REMARK 500 PHE D 125 -64.98 -107.87
REMARK 500 ASP D 150 83.56 -158.57
REMARK 500 THR D 230 -93.90 -125.04
REMARK 500 PRO E 29 60.09 -106.56
REMARK 500 LEU E 30 -150.26 -102.32
REMARK 500 SER E 94 -125.47 61.07
REMARK 500 PHE E 125 -64.26 -107.46
REMARK 500 TYR E 131 59.17 -146.02
REMARK 500 ASP E 150 84.29 -160.18
REMARK 500 THR E 230 -90.53 -125.06
REMARK 500 PRO F 29 61.48 -107.64
REMARK 500 LEU F 30 -146.19 -103.50
REMARK 500 SER F 94 -120.90 60.70
REMARK 500 TYR F 131 58.50 -141.21
REMARK 500 ASP F 150 81.71 -153.21
REMARK 500 THR F 230 -90.68 -125.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 THE C1 CARBON OF EEE BECOMES SP3 RATHER THAN SP2 UPON
REMARK 600 REACTION WITH SER94. O1 BECOMES SINGLE BONDED AND ACQUIRES
REMARK 600 A NEGATIVE CHARGE
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EEE A 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EEE B 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EEE C 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EEE D 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EEE E 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EEE F 300
DBREF 3HEA A 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3HEA B 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3HEA C 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3HEA D 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3HEA E 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3HEA F 1 271 UNP P22862 ESTE_PSEFL 2 272
SEQADV 3HEA PRO A 29 UNP P22862 LEU 30 ENGINEERED
SEQADV 3HEA ILE A 124 UNP P22862 LEU 125 ENGINEERED
SEQADV 3HEA PRO B 29 UNP P22862 LEU 30 ENGINEERED
SEQADV 3HEA ILE B 124 UNP P22862 LEU 125 ENGINEERED
SEQADV 3HEA PRO C 29 UNP P22862 LEU 30 ENGINEERED
SEQADV 3HEA ILE C 124 UNP P22862 LEU 125 ENGINEERED
SEQADV 3HEA PRO D 29 UNP P22862 LEU 30 ENGINEERED
SEQADV 3HEA ILE D 124 UNP P22862 LEU 125 ENGINEERED
SEQADV 3HEA PRO E 29 UNP P22862 LEU 30 ENGINEERED
SEQADV 3HEA ILE E 124 UNP P22862 LEU 125 ENGINEERED
SEQADV 3HEA PRO F 29 UNP P22862 LEU 30 ENGINEERED
SEQADV 3HEA ILE F 124 UNP P22862 LEU 125 ENGINEERED
SEQRES 1 A 271 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 A 271 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 A 271 GLY TRP PRO LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 A 271 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 A 271 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 A 271 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 A 271 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 A 271 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 A 271 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 A 271 LEU GLY ALA VAL THR PRO ILE PHE GLY GLN LYS PRO ASP
SEQRES 11 A 271 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 A 271 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 A 271 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 A 271 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 A 271 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 A 271 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 A 271 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 A 271 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 A 271 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 A 271 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 A 271 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG
SEQRES 1 B 271 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 B 271 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 B 271 GLY TRP PRO LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 B 271 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 B 271 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 B 271 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 B 271 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 B 271 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 B 271 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 B 271 LEU GLY ALA VAL THR PRO ILE PHE GLY GLN LYS PRO ASP
SEQRES 11 B 271 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 B 271 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 B 271 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 B 271 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 B 271 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 B 271 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 B 271 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 B 271 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 B 271 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 B 271 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 B 271 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG
SEQRES 1 C 271 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 C 271 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 C 271 GLY TRP PRO LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 C 271 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 C 271 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 C 271 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 C 271 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 C 271 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 C 271 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 C 271 LEU GLY ALA VAL THR PRO ILE PHE GLY GLN LYS PRO ASP
SEQRES 11 C 271 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 C 271 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 C 271 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 C 271 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 C 271 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 C 271 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 C 271 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 C 271 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 C 271 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 C 271 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 C 271 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG
SEQRES 1 D 271 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 D 271 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 D 271 GLY TRP PRO LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 D 271 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 D 271 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 D 271 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 D 271 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 D 271 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 D 271 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 D 271 LEU GLY ALA VAL THR PRO ILE PHE GLY GLN LYS PRO ASP
SEQRES 11 D 271 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 D 271 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 D 271 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 D 271 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 D 271 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 D 271 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 D 271 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 D 271 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 D 271 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 D 271 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 D 271 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG
SEQRES 1 E 271 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 E 271 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 E 271 GLY TRP PRO LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 E 271 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 E 271 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 E 271 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 E 271 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 E 271 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 E 271 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 E 271 LEU GLY ALA VAL THR PRO ILE PHE GLY GLN LYS PRO ASP
SEQRES 11 E 271 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 E 271 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 E 271 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 E 271 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 E 271 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 E 271 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 E 271 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 E 271 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 E 271 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 E 271 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 E 271 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG
SEQRES 1 F 271 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 F 271 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 F 271 GLY TRP PRO LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 F 271 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 F 271 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 F 271 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 F 271 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 F 271 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 F 271 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 F 271 LEU GLY ALA VAL THR PRO ILE PHE GLY GLN LYS PRO ASP
SEQRES 11 F 271 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 F 271 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 F 271 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 F 271 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 F 271 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 F 271 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 F 271 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 F 271 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 F 271 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 F 271 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 F 271 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG
HET GOL A 272 6
HET GOL A 273 6
HET GOL A 274 6
HET SO4 A 275 5
HET SO4 A 276 5
HET SO4 A 277 5
HET SO4 A 278 5
HET EEE A 300 6
HET GOL B 272 6
HET GOL B 273 6
HET GOL B 274 6
HET GOL B 275 6
HET SO4 B 276 5
HET SO4 B 277 5
HET EEE B 300 6
HET GOL C 272 6
HET GOL C 273 6
HET GOL C 274 6
HET GOL C 275 6
HET SO4 C 276 5
HET SO4 C 277 5
HET SO4 C 278 5
HET EEE C 300 6
HET GOL D 272 6
HET GOL D 273 6
HET GOL D 274 6
HET SO4 D 275 5
HET SO4 D 276 5
HET EEE D 300 6
HET GOL E 272 6
HET GOL E 273 6
HET GOL E 274 6
HET GOL E 275 6
HET GOL E 276 6
HET SO4 E 277 5
HET SO4 E 278 5
HET EEE E 300 6
HET GOL F 272 6
HET GOL F 273 6
HET GOL F 274 6
HET GOL F 275 6
HET GOL F 276 6
HET SO4 F 277 5
HET EEE F 300 6
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM EEE ETHYL ACETATE
FORMUL 7 GOL 24(C3 H8 O3)
FORMUL 10 SO4 14(O4 S 2-)
FORMUL 14 EEE 6(C4 H8 O2)
FORMUL 51 HOH *1057(H2 O)
HELIX 1 1 ASP A 31 MET A 34 5 4
HELIX 2 2 TRP A 35 SER A 44 1 10
HELIX 3 3 ASP A 68 ASP A 84 1 17
HELIX 4 4 MET A 95 GLY A 108 1 14
HELIX 5 5 PRO A 136 GLY A 164 1 29
HELIX 6 6 ILE A 165 GLY A 168 5 4
HELIX 7 7 SER A 172 ALA A 186 1 15
HELIX 8 8 SER A 187 THR A 201 1 15
HELIX 9 9 PHE A 203 ILE A 210 1 8
HELIX 10 10 PRO A 226 THR A 229 5 4
HELIX 11 11 THR A 230 ILE A 238 1 9
HELIX 12 12 GLY A 252 HIS A 257 1 6
HELIX 13 13 HIS A 257 LYS A 270 1 14
HELIX 14 14 ASP B 31 MET B 34 5 4
HELIX 15 15 TRP B 35 SER B 44 1 10
HELIX 16 16 ASP B 68 ASP B 84 1 17
HELIX 17 17 MET B 95 GLY B 108 1 14
HELIX 18 18 PRO B 136 GLY B 164 1 29
HELIX 19 19 ILE B 165 GLY B 168 5 4
HELIX 20 20 SER B 172 ALA B 186 1 15
HELIX 21 21 SER B 187 THR B 201 1 15
HELIX 22 22 PHE B 203 ALA B 208 1 6
HELIX 23 23 PRO B 226 THR B 229 5 4
HELIX 24 24 THR B 230 ILE B 238 1 9
HELIX 25 25 GLY B 252 HIS B 257 1 6
HELIX 26 26 HIS B 257 ARG B 271 1 15
HELIX 27 27 ASP C 31 MET C 34 5 4
HELIX 28 28 TRP C 35 SER C 44 1 10
HELIX 29 29 ASP C 68 ASP C 84 1 17
HELIX 30 30 MET C 95 GLY C 108 1 14
HELIX 31 31 PRO C 136 GLY C 164 1 29
HELIX 32 32 ILE C 165 GLY C 168 5 4
HELIX 33 33 SER C 172 ALA C 186 1 15
HELIX 34 34 SER C 187 THR C 201 1 15
HELIX 35 35 PHE C 203 ILE C 210 1 8
HELIX 36 36 PRO C 226 THR C 229 5 4
HELIX 37 37 THR C 230 ILE C 238 1 9
HELIX 38 38 GLY C 252 HIS C 257 1 6
HELIX 39 39 HIS C 257 LYS C 270 1 14
HELIX 40 40 ASP D 31 MET D 34 5 4
HELIX 41 41 TRP D 35 SER D 44 1 10
HELIX 42 42 ASP D 68 LEU D 83 1 16
HELIX 43 43 MET D 95 GLY D 108 1 14
HELIX 44 44 PRO D 136 GLY D 164 1 29
HELIX 45 45 ILE D 165 GLY D 168 5 4
HELIX 46 46 SER D 172 ALA D 186 1 15
HELIX 47 47 SER D 187 THR D 201 1 15
HELIX 48 48 PHE D 203 LYS D 209 1 7
HELIX 49 49 PRO D 226 THR D 229 5 4
HELIX 50 50 THR D 230 ILE D 238 1 9
HELIX 51 51 GLY D 252 HIS D 257 1 6
HELIX 52 52 HIS D 257 LYS D 270 1 14
HELIX 53 53 ASP E 31 MET E 34 5 4
HELIX 54 54 TRP E 35 SER E 44 1 10
HELIX 55 55 ASP E 68 LEU E 83 1 16
HELIX 56 56 MET E 95 GLY E 108 1 14
HELIX 57 57 PRO E 136 GLY E 164 1 29
HELIX 58 58 ILE E 165 GLY E 168 5 4
HELIX 59 59 SER E 172 ALA E 186 1 15
HELIX 60 60 SER E 187 THR E 201 1 15
HELIX 61 61 PHE E 203 ILE E 210 1 8
HELIX 62 62 PRO E 226 THR E 229 5 4
HELIX 63 63 THR E 230 ILE E 238 1 9
HELIX 64 64 GLY E 252 HIS E 257 1 6
HELIX 65 65 HIS E 257 LYS E 270 1 14
HELIX 66 66 ASP F 31 MET F 34 5 4
HELIX 67 67 TRP F 35 SER F 44 1 10
HELIX 68 68 ASP F 68 ASP F 84 1 17
HELIX 69 69 MET F 95 GLY F 108 1 14
HELIX 70 70 PRO F 136 GLY F 164 1 29
HELIX 71 71 ILE F 165 GLY F 168 5 4
HELIX 72 72 SER F 172 ALA F 186 1 15
HELIX 73 73 SER F 187 THR F 201 1 15
HELIX 74 74 PHE F 203 LYS F 209 1 7
HELIX 75 75 PRO F 226 THR F 229 5 4
HELIX 76 76 THR F 230 ILE F 238 1 9
HELIX 77 77 GLY F 252 HIS F 257 1 6
HELIX 78 78 HIS F 257 LYS F 270 1 14
SHEET 1 A 8 THR A 2 VAL A 4 0
SHEET 2 A 8 GLN A 10 TRP A 16 -1 O ILE A 11 N PHE A 3
SHEET 3 A 8 ARG A 48 PHE A 52 -1 O THR A 49 N TRP A 16
SHEET 4 A 8 PRO A 21 SER A 25 1 N PHE A 24 O ILE A 50
SHEET 5 A 8 VAL A 88 PHE A 93 1 O VAL A 91 N LEU A 23
SHEET 6 A 8 VAL A 112 LEU A 118 1 O LEU A 118 N GLY A 92
SHEET 7 A 8 THR A 214 GLY A 219 1 O ILE A 217 N LEU A 117
SHEET 8 A 8 GLU A 242 TYR A 246 1 O LYS A 244 N VAL A 216
SHEET 1 B 8 THR B 2 VAL B 4 0
SHEET 2 B 8 GLN B 10 TRP B 16 -1 O ILE B 11 N PHE B 3
SHEET 3 B 8 TYR B 47 PHE B 52 -1 O THR B 49 N TRP B 16
SHEET 4 B 8 LYS B 20 SER B 25 1 N PHE B 24 O ILE B 50
SHEET 5 B 8 VAL B 88 PHE B 93 1 O VAL B 91 N SER B 25
SHEET 6 B 8 VAL B 112 LEU B 118 1 O LEU B 118 N GLY B 92
SHEET 7 B 8 THR B 214 GLY B 219 1 O ILE B 217 N LEU B 117
SHEET 8 B 8 GLU B 242 TYR B 246 1 O GLU B 242 N VAL B 216
SHEET 1 C 8 THR C 2 VAL C 4 0
SHEET 2 C 8 GLN C 10 TRP C 16 -1 O ILE C 11 N PHE C 3
SHEET 3 C 8 ARG C 48 PHE C 52 -1 O THR C 49 N TRP C 16
SHEET 4 C 8 PRO C 21 SER C 25 1 N PHE C 24 O ILE C 50
SHEET 5 C 8 VAL C 88 PHE C 93 1 O VAL C 91 N SER C 25
SHEET 6 C 8 VAL C 112 LEU C 118 1 O VAL C 116 N LEU C 90
SHEET 7 C 8 THR C 214 GLY C 219 1 O ILE C 217 N LEU C 117
SHEET 8 C 8 GLU C 242 TYR C 246 1 O GLU C 242 N VAL C 216
SHEET 1 D 8 THR D 2 VAL D 4 0
SHEET 2 D 8 GLN D 10 TRP D 16 -1 O ILE D 11 N PHE D 3
SHEET 3 D 8 ARG D 48 PHE D 52 -1 O THR D 49 N TRP D 16
SHEET 4 D 8 PRO D 21 SER D 25 1 N PHE D 24 O ILE D 50
SHEET 5 D 8 VAL D 88 PHE D 93 1 O VAL D 91 N SER D 25
SHEET 6 D 8 VAL D 112 LEU D 118 1 O LEU D 118 N GLY D 92
SHEET 7 D 8 THR D 214 GLY D 219 1 O ILE D 217 N LEU D 117
SHEET 8 D 8 GLU D 242 TYR D 246 1 O GLU D 242 N VAL D 216
SHEET 1 E 8 THR E 2 VAL E 4 0
SHEET 2 E 8 GLN E 10 TRP E 16 -1 O ILE E 11 N PHE E 3
SHEET 3 E 8 ARG E 48 PHE E 52 -1 O ALA E 51 N LYS E 14
SHEET 4 E 8 PRO E 21 SER E 25 1 N PHE E 24 O ILE E 50
SHEET 5 E 8 VAL E 88 PHE E 93 1 O VAL E 91 N SER E 25
SHEET 6 E 8 VAL E 112 LEU E 118 1 O LEU E 118 N GLY E 92
SHEET 7 E 8 THR E 214 GLY E 219 1 O LEU E 215 N LEU E 115
SHEET 8 E 8 GLU E 242 TYR E 246 1 O GLU E 242 N VAL E 216
SHEET 1 F 8 THR F 2 VAL F 4 0
SHEET 2 F 8 GLN F 10 TRP F 16 -1 O ILE F 11 N PHE F 3
SHEET 3 F 8 ARG F 48 PHE F 52 -1 O THR F 49 N TRP F 16
SHEET 4 F 8 PRO F 21 SER F 25 1 N PHE F 24 O ILE F 50
SHEET 5 F 8 VAL F 88 PHE F 93 1 O VAL F 91 N SER F 25
SHEET 6 F 8 VAL F 112 LEU F 118 1 O VAL F 116 N LEU F 90
SHEET 7 F 8 THR F 214 GLY F 219 1 O LEU F 215 N LEU F 117
SHEET 8 F 8 GLU F 242 TYR F 246 1 O GLU F 242 N VAL F 216
LINK OG SER A 94 C1 EEE A 300 1555 1555 1.45
LINK OG SER B 94 C1 EEE B 300 1555 1555 1.45
LINK OG SER C 94 C1 EEE C 300 1555 1555 1.44
LINK OG SER D 94 C1 EEE D 300 1555 1555 1.44
LINK OG SER E 94 C1 EEE E 300 1555 1555 1.45
LINK OG SER F 94 C1 EEE F 300 1555 1555 1.45
CISPEP 1 TRP A 28 PRO A 29 0 -7.59
CISPEP 2 THR A 122 PRO A 123 0 3.53
CISPEP 3 TRP B 28 PRO B 29 0 -8.89
CISPEP 4 THR B 122 PRO B 123 0 4.10
CISPEP 5 TRP C 28 PRO C 29 0 -8.36
CISPEP 6 THR C 122 PRO C 123 0 0.74
CISPEP 7 TRP D 28 PRO D 29 0 -7.70
CISPEP 8 THR D 122 PRO D 123 0 1.90
CISPEP 9 TRP E 28 PRO E 29 0 -10.03
CISPEP 10 THR E 122 PRO E 123 0 3.01
CISPEP 11 TRP F 28 PRO F 29 0 -7.41
CISPEP 12 THR F 122 PRO F 123 0 1.26
SITE 1 AC1 5 SER A 1 TYR A 12 ASP A 15 HOH A 377
SITE 2 AC1 5 GLN C 62
SITE 1 AC2 5 LEU D 137 ALA D 141 LYS D 144 THR D 196
SITE 2 AC2 5 GLU D 200
SITE 1 AC3 7 ASP B 61 GLN B 62 SER C 1 TYR C 12
SITE 2 AC3 7 LYS C 14 ASP C 15 HOH C 337
SITE 1 AC4 7 SER D 1 TYR D 12 LYS D 14 ASP D 15
SITE 2 AC4 7 HOH D 343 ASP E 61 GLN E 62
SITE 1 AC5 6 SER E 1 TYR E 12 ASP E 15 HOH E 823
SITE 2 AC5 6 ASP F 61 GLN F 62
SITE 1 AC6 7 ASP D 61 GLN D 62 SER F 1 TYR F 12
SITE 2 AC6 7 LYS F 14 ASP F 15 HOH F 511
SITE 1 AC7 5 LEU A 137 ALA A 141 LYS A 144 THR A 196
SITE 2 AC7 5 GLU A 200
SITE 1 AC8 6 LEU B 137 ALA B 141 LYS B 144 THR B 196
SITE 2 AC8 6 GLU B 200 HOH B 713
SITE 1 AC9 4 LEU C 137 LYS C 144 THR C 196 GLU C 200
SITE 1 BC1 6 LEU E 137 ALA E 141 LYS E 144 THR E 196
SITE 2 BC1 6 GLU E 200 HOH E 779
SITE 1 BC2 4 LEU F 137 ALA F 141 LYS F 144 GLU F 200
SITE 1 BC3 7 ASP A 61 GLN A 62 SER B 1 TYR B 12
SITE 2 BC3 7 LYS B 14 ASP B 15 HOH B 364
SITE 1 BC4 9 LEU D 30 TYR D 163 VAL D 175 GLN D 178
SITE 2 BC4 9 THR D 179 ILE D 182 HOH D 299 HOH D 494
SITE 3 BC4 9 HOH D 975
SITE 1 BC5 7 TYR E 163 VAL E 175 GLN E 178 THR E 179
SITE 2 BC5 7 ILE E 182 HOH E 298 HOH E 615
SITE 1 BC6 7 TYR A 163 VAL A 175 GLN A 178 THR A 179
SITE 2 BC6 7 ILE A 182 HOH A 310 HOH A 587
SITE 1 BC7 9 LEU B 30 TYR B 163 VAL B 175 GLN B 178
SITE 2 BC7 9 THR B 179 ILE B 182 HOH B 294 HOH B 348
SITE 3 BC7 9 HOH B 914
SITE 1 BC8 9 LEU C 30 TYR C 163 VAL C 175 GLN C 178
SITE 2 BC8 9 THR C 179 ILE C 182 HOH C 301 HOH C 529
SITE 3 BC8 9 HOH C 552
SITE 1 BC9 7 TYR F 163 VAL F 175 GLN F 178 THR F 179
SITE 2 BC9 7 ILE F 182 HOH F 293 HOH F 521
SITE 1 CC1 7 LYS E 6 ASP E 74 GLN E 78 GLU E 81
SITE 2 CC1 7 HIS E 107 HOH E 281 HOH E 814
SITE 1 CC2 2 GLN C 223 ILE C 224
SITE 1 CC3 2 GLN B 223 ILE B 224
SITE 1 CC4 4 VAL F 245 LYS F 247 GLN F 260 HOH F 438
SITE 1 CC5 4 PHE F 143 GLN F 223 ILE F 224 PRO F 226
SITE 1 CC6 2 GLN E 223 ILE E 224
SITE 1 CC7 5 VAL E 245 TYR E 246 LYS E 247 GLN E 260
SITE 2 CC7 5 HOH E 903
SITE 1 CC8 4 ASN A 166 SER C 18 GLY C 19 HOH C1039
SITE 1 CC9 5 VAL C 245 TYR C 246 LYS C 247 GLN C 260
SITE 2 CC9 5 HOH C 396
SITE 1 DC1 1 ARG A 106
SITE 1 DC2 3 ASP B 70 ARG B 106 HOH B 806
SITE 1 DC3 1 ARG C 106
SITE 1 DC4 5 VAL A 245 TYR A 246 LYS A 247 GLN A 260
SITE 2 DC4 5 HOH A 699
SITE 1 DC5 2 ASP E 70 ARG E 106
SITE 1 DC6 1 ARG D 106
SITE 1 DC7 6 PHE A 3 VAL A 4 HIS A 82 HOH A1004
SITE 2 DC7 6 LYS B 247 ASP B 248
SITE 1 DC8 5 VAL D 245 TYR D 246 LYS D 247 GLN D 260
SITE 2 DC8 5 HOH D1031
SITE 1 DC9 5 VAL B 245 TYR B 246 LYS B 247 GLN B 260
SITE 2 DC9 5 HOH B 822
SITE 1 EC1 2 ARG F 106 HOH F 920
SITE 1 EC2 4 HIS B 107 GLN C 173 HOH C 306 HOH C 780
SITE 1 EC3 7 GLY A 27 TRP A 28 PHE A 93 SER A 94
SITE 2 EC3 7 MET A 95 ILE A 224 HIS A 251
SITE 1 EC4 7 GLY B 27 TRP B 28 PHE B 93 SER B 94
SITE 2 EC4 7 MET B 95 ILE B 224 HIS B 251
SITE 1 EC5 7 GLY C 27 TRP C 28 PHE C 93 SER C 94
SITE 2 EC5 7 MET C 95 ILE C 224 HIS C 251
SITE 1 EC6 8 GLY D 27 TRP D 28 PHE D 93 SER D 94
SITE 2 EC6 8 MET D 95 ILE D 224 HIS D 251 HOH D 645
SITE 1 EC7 7 GLY E 27 TRP E 28 PHE E 93 SER E 94
SITE 2 EC7 7 MET E 95 ILE E 224 HIS E 251
SITE 1 EC8 8 GLY F 27 TRP F 28 PHE F 93 SER F 94
SITE 2 EC8 8 MET F 95 PHE F 198 ILE F 224 HIS F 251
CRYST1 145.586 145.586 128.200 90.00 90.00 120.00 P 32 18
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 0.006869 0.003966 0.000000 0.00000
SCALE2 0.000000 0.007931 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007800 0.00000
TER 2154 ARG A 271
TER 4310 ARG B 271
TER 6454 ARG C 271
TER 8602 ARG D 271
TER 10751 ARG E 271
TER 12894 ARG F 271
MASTER 528 0 44 78 48 0 76 614195 6 256 126
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