| content |
HEADER OXIDOREDUCTASE, HYDRLOASE 26-JUL-11 3T52
TITLE L29I MUTATION IN AN ARYL ESTERASE FROM PSEUDOMONAS FLUORESCENS LEADS
TITLE 2 TO UNIQUE PEPTIDE FLIP AND INCREASED ACTIVITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARYLESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: ARYL-ESTER HYDROLASE, PFE, BROMOPEROXIDASE;
COMPND 5 EC: 3.1.1.2, 1.-.-.-;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS FLUORESCENS;
SOURCE 3 ORGANISM_TAXID: 294;
SOURCE 4 STRAIN: SIK WI;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5 ALPHA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PL29I
KEYWDS PEPTIDE FLIP, OXIDOREDUCTASE, HYDRLOASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.J.KAZLAUSKAS,T.YIN,V.M.PURPERO
REVDAT 1 01-AUG-12 3T52 0
JRNL AUTH T.YIN,R.J.KAZLAUSKAS,V.M.PURPERO
JRNL TITL L29I MUTATION IN AN ARYL ESTERASE FROM PSEUDOMONAS
JRNL TITL 2 FLUORESCENS LEADS TO UNIQUE PEPTIDE FLIP AND INCREASED
JRNL TITL 3 ACTIVITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 207522
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) : 0.185
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.211
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 10433
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 14540
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 762
REMARK 3 BIN FREE R VALUE : 0.2790
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12719
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 409
REMARK 3 SOLVENT ATOMS : 1166
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.03000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : 0.05000
REMARK 3 B12 (A**2) : -0.02000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.781
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.965
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13786 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18676 ; 1.368 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1723 ; 5.291 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 649 ;32.455 ;24.114
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2189 ;13.581 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 77 ;19.499 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2000 ; 0.104 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10597 ; 0.007 ; 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): 8336 ; 0.744 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 13352 ; 1.339 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5450 ; 2.214 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5279 ; 3.535 ; 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 : 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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3T52 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-11.
REMARK 100 THE RCSB ID CODE IS RCSB067046.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-MAY-08
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 : ALS
REMARK 200 BEAMLINE : 4.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : ROSENBAUM-ROCK SI(111) SAGITALLY
REMARK 200 FOCUSED MONOCHROMATOR
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NOIR-1
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 207756
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 48.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.460
REMARK 200 R MERGE (I) : 0.11100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.26
REMARK 200 R MERGE FOR SHELL (I) : 0.42700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.900
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 IVA4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.11
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.41
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1% PEG 400, 1.65M (NH4)2SO4, 0.1M
REMARK 280 HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 85.96667
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 42.98333
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27940 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.0 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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 14650 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27420 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.0 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 LEU A 30 -166.62 -119.11
REMARK 500 SER A 94 -124.63 58.08
REMARK 500 TYR A 131 57.02 -142.33
REMARK 500 ASP A 150 85.91 -156.80
REMARK 500 THR A 230 -96.81 -123.16
REMARK 500 LEU B 30 -164.92 -115.83
REMARK 500 GLN B 62 76.57 -119.60
REMARK 500 SER B 94 -123.85 59.41
REMARK 500 LEU B 124 136.27 -171.45
REMARK 500 TYR B 131 58.84 -140.37
REMARK 500 ASP B 150 86.96 -156.67
REMARK 500 THR B 230 -91.99 -123.14
REMARK 500 ASP B 248 7.24 57.97
REMARK 500 TRP C 28 -85.95 -56.15
REMARK 500 ILE C 29 47.17 -91.51
REMARK 500 LEU C 30 -166.64 -120.86
REMARK 500 GLN C 62 74.82 -116.52
REMARK 500 SER C 94 -125.84 57.63
REMARK 500 LEU C 124 134.40 -171.19
REMARK 500 ASP C 150 87.30 -160.39
REMARK 500 THR C 230 -96.64 -125.51
REMARK 500 TRP D 28 -83.31 -56.91
REMARK 500 ILE D 29 47.78 -95.71
REMARK 500 LEU D 30 -164.37 -120.09
REMARK 500 SER D 94 -122.81 58.40
REMARK 500 TYR D 131 58.05 -141.27
REMARK 500 ASP D 150 84.86 -153.54
REMARK 500 THR D 230 -91.48 -123.54
REMARK 500 LEU E 30 -165.06 -121.11
REMARK 500 GLN E 62 78.03 -119.40
REMARK 500 SER E 94 -126.03 57.17
REMARK 500 TYR E 131 56.34 -144.78
REMARK 500 ASP E 150 89.28 -154.64
REMARK 500 THR E 230 -90.85 -123.86
REMARK 500 TRP F 28 -80.51 -61.59
REMARK 500 ILE F 29 45.04 -95.06
REMARK 500 LEU F 30 -165.14 -118.14
REMARK 500 GLN F 62 74.49 -119.11
REMARK 500 SER F 94 -127.19 60.98
REMARK 500 LEU F 124 133.34 -171.72
REMARK 500 ASP F 150 85.12 -162.33
REMARK 500 THR F 230 -94.13 -123.97
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ASP A 99 23.4 L L OUTSIDE RANGE
REMARK 500 ASP C 99 23.7 L L OUTSIDE RANGE
REMARK 500 ASP E 99 23.8 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH C1028 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH D 968 DISTANCE = 5.05 ANGSTROMS
REMARK 525 HOH D1026 DISTANCE = 5.98 ANGSTROMS
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 SO4 A 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO A 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO A 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 282
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 283
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO B 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO B 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO B 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO B 282
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 283
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 284
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 285
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 286
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 287
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 288
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 289
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO C 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 282
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 283
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO C 284
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 285
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 286
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 287
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 288
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 289
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO D 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO D 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO D 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 282
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 283
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 284
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 285
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 286
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO E 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO E 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO E 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO E 282
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 283
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 284
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 285
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 286
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 287
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO E 288
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 289
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 290
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO F 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO F 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: JC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO F 279
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 280
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 281
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 282
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 283
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 284
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 285
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 286
REMARK 800
REMARK 800 SITE_IDENTIFIER: KC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 287
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VA4 RELATED DB: PDB
REMARK 900 WT ARYL ESTERASE
REMARK 900 RELATED ID: 3HI4 RELATED DB: PDB
REMARK 900 L29P MUTATION
REMARK 900 RELATED ID: 3T4U RELATED DB: PDB
REMARK 900 L29I RESTING
DBREF 3T52 A 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3T52 B 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3T52 C 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3T52 D 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3T52 E 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3T52 F 1 271 UNP P22862 ESTE_PSEFL 2 272
SEQADV 3T52 ILE A 29 UNP P22862 LEU 30 ENGINEERED MUTATION
SEQADV 3T52 ILE B 29 UNP P22862 LEU 30 ENGINEERED MUTATION
SEQADV 3T52 ILE C 29 UNP P22862 LEU 30 ENGINEERED MUTATION
SEQADV 3T52 ILE D 29 UNP P22862 LEU 30 ENGINEERED MUTATION
SEQADV 3T52 ILE E 29 UNP P22862 LEU 30 ENGINEERED MUTATION
SEQADV 3T52 ILE F 29 UNP P22862 LEU 30 ENGINEERED MUTATION
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 ILE 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 LEU 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 ILE 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 LEU 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 ILE 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 LEU 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 ILE 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 LEU 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 ILE 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 LEU 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 ILE 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 LEU 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 SO4 A 273 5
HET CL A 274 1
HET CL A 275 1
HET PEO A 276 2
HET PEO A 277 2
HET GOL A 278 6
HET ACT A 279 4
HET ACT A 280 4
HET ACT A 281 4
HET ACT A 282 4
HET GOL A 283 6
HET GOL B 272 6
HET GOL B 273 6
HET SO4 B 274 5
HET SO4 B 275 5
HET CL B 276 1
HET GOL B 277 6
HET GOL B 278 6
HET PEO B 279 2
HET PEO B 280 2
HET PEO B 281 2
HET PEO B 282 2
HET ACT B 283 4
HET ACT B 284 4
HET ACT B 285 4
HET ACT B 286 8
HET ACT B 287 4
HET GOL B 288 6
HET GOL B 289 6
HET GOL C 272 6
HET GOL C 273 6
HET SO4 C 274 5
HET SO4 C 275 5
HET SO4 C 276 5
HET CL C 277 1
HET CL C 278 1
HET GOL C 279 6
HET PEO C 280 2
HET ACT C 281 4
HET ACT C 282 4
HET ACT C 283 4
HET PEO C 284 2
HET ACT C 285 4
HET ACT C 286 4
HET ACT C 287 4
HET GOL C 288 6
HET GOL C 289 6
HET GOL D 272 6
HET GOL D 273 6
HET SO4 D 274 5
HET CL D 275 1
HET ACT D 276 4
HET GOL D 277 6
HET PEO D 278 2
HET PEO D 279 2
HET GOL D 280 12
HET PEO D 281 2
HET ACT D 282 4
HET ACT D 283 4
HET GOL D 284 6
HET GOL D 285 6
HET GOL D 286 6
HET GOL E 272 6
HET GOL E 273 6
HET SO4 E 274 5
HET SO4 E 275 5
HET CL E 276 1
HET GOL E 277 6
HET PEO E 278 2
HET PEO E 279 2
HET PEO E 280 2
HET GOL E 281 6
HET PEO E 282 2
HET ACT E 283 4
HET ACT E 284 4
HET ACT E 285 4
HET ACT E 286 8
HET ACT E 287 4
HET PEO E 288 2
HET GOL E 289 6
HET ACT E 290 4
HET GOL F 272 6
HET SO4 F 273 5
HET SO4 F 274 5
HET SO4 F 275 5
HET GOL F 276 6
HET PEO F 277 2
HET PEO F 278 2
HET PEO F 279 2
HET GOL F 280 6
HET ACT F 281 4
HET ACT F 282 4
HET ACT F 283 4
HET GOL F 284 6
HET GOL F 285 12
HET ACT F 286 4
HET GOL F 287 6
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM PEO HYDROGEN PEROXIDE
HETNAM ACT ACETATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 7 GOL 32(C3 H8 O3)
FORMUL 8 SO4 12(O4 S 2-)
FORMUL 9 CL 7(CL 1-)
FORMUL 11 PEO 19(H2 O2)
FORMUL 14 ACT 28(C2 H3 O2 1-)
FORMUL 05 HOH *1166(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 LEU A 83 1 16
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 ARG A 271 1 15
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 LEU B 83 1 16
HELIX 17 17 MET B 95 GLY B 108 1 14
HELIX 18 18 PRO B 136 TYR B 163 1 28
HELIX 19 19 GLY B 164 GLY B 168 5 5
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 ILE B 210 1 8
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 LEU C 83 1 16
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 LYS C 209 1 7
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 ASP D 84 1 17
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 ILE D 210 1 8
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 ARG D 271 1 15
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 ARG E 271 1 15
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 SER A 25
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 GLU A 242 N THR A 214
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 ARG B 48 PHE B 52 -1 O THR B 49 N TRP B 16
SHEET 4 B 8 PRO B 21 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 LEU C 23
SHEET 6 C 8 VAL C 112 LEU C 118 1 O LEU C 118 N GLY C 92
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 THR E 49 N TRP E 16
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 ILE E 217 N LEU E 117
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 GLY F 17 -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 LEU F 118 N GLY F 92
SHEET 7 F 8 THR F 214 GLY F 219 1 O ILE F 217 N LEU F 117
SHEET 8 F 8 GLU F 242 TYR F 246 1 O GLU F 242 N VAL F 216
CISPEP 1 THR A 122 PRO A 123 0 6.11
CISPEP 2 THR B 122 PRO B 123 0 3.12
CISPEP 3 THR C 122 PRO C 123 0 3.60
CISPEP 4 THR D 122 PRO D 123 0 3.59
CISPEP 5 THR E 122 PRO E 123 0 3.44
CISPEP 6 THR F 122 PRO F 123 0 4.77
SITE 1 AC1 7 SER A 1 TYR A 12 LYS A 14 ASP A 15
SITE 2 AC1 7 HOH A 540 ASP C 61 GLN C 62
SITE 1 AC2 1 ARG A 106
SITE 1 AC3 2 LYS A 247 GLN A 260
SITE 1 AC4 1 HOH A 871
SITE 1 AC5 3 VAL A 212 PRO A 213 HOH A 980
SITE 1 AC6 2 LYS A 128 HOH A 723
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 3 SER A 156 ASN A 159 GLN A 173
SITE 1 AC9 6 ASP A 7 PRO A 63 TRP A 64 THR A 65
SITE 2 AC9 6 HOH A 389 HOH A1076
SITE 1 BC1 9 GLY A 27 TRP A 28 ILE A 29 LEU A 30
SITE 2 BC1 9 PHE A 93 SER A 94 PHE A 162 HIS A 251
SITE 3 BC1 9 ACT A 282
SITE 1 BC2 7 TRP A 28 SER A 94 MET A 95 VAL A 121
SITE 2 BC2 7 PHE A 125 ILE A 224 ACT A 281
SITE 1 BC3 3 GLN A 223 ILE A 224 HOH A1073
SITE 1 BC4 5 LEU B 137 ALA B 141 LYS B 144 GLU B 200
SITE 2 BC4 5 PEO B 281
SITE 1 BC5 8 ASP A 61 GLN A 62 SER B 1 TYR B 12
SITE 2 BC5 8 PHE B 13 LYS B 14 ASP B 15 HOH B 311
SITE 1 BC6 1 ARG B 106
SITE 1 BC7 4 VAL B 245 TYR B 246 LYS B 247 GLN B 260
SITE 1 BC8 1 GLY B 240
SITE 1 BC9 4 GLN B 223 ILE B 224 ACT B 286 ACT B 287
SITE 1 CC1 6 SER B 1 THR B 2 LYS B 167 GLY B 168
SITE 2 CC1 6 HOH B 303 HOH B 311
SITE 1 CC2 3 ARG B 102 ASP B 202 HOH B 909
SITE 1 CC3 2 GLY B 17 SER B 18
SITE 1 CC4 3 ASP B 138 ALA B 141 GOL B 272
SITE 1 CC5 3 HOH A 292 HOH B 297 HOH B 875
SITE 1 CC6 7 GLY B 27 TRP B 28 PHE B 93 SER B 94
SITE 2 CC6 7 PHE B 162 HIS B 251 ACT B 284
SITE 1 CC7 8 TRP B 28 SER B 94 MET B 95 VAL B 121
SITE 2 CC7 8 PHE B 125 PHE B 198 ILE B 224 ACT B 283
SITE 1 CC8 6 ASP B 7 PRO B 63 TRP B 64 THR B 65
SITE 2 CC8 6 HOH B 359 HOH B1096
SITE 1 CC9 4 ILE B 224 GOL B 277 ACT B 287 HOH B 797
SITE 1 DC1 6 TRP B 28 PHE B 143 PHE B 158 ILE B 224
SITE 2 DC1 6 GOL B 277 ACT B 286
SITE 1 DC2 2 TRP B 64 SER C 18
SITE 1 DC3 2 ARG B 45 HOH B1146
SITE 1 DC4 7 ASP B 61 GLN B 62 SER C 1 TYR C 12
SITE 2 DC4 7 LYS C 14 ASP C 15 HOH C 297
SITE 1 DC5 4 LEU C 137 ALA C 141 LYS C 144 GLU C 200
SITE 1 DC6 5 VAL C 245 TYR C 246 LYS C 247 GLN C 260
SITE 2 DC6 5 HOH C 736
SITE 1 DC7 5 HIS B 107 GLN C 173 HOH C 310 HOH C 372
SITE 2 DC7 5 HOH C 712
SITE 1 DC8 2 ARG C 106 ACT C 281
SITE 1 DC9 1 GLY C 240
SITE 1 EC1 1 ARG C 45
SITE 1 EC2 6 PHE C 143 GLN C 223 ILE C 224 PRO C 226
SITE 2 EC2 6 ACT C 286 ACT C 287
SITE 1 EC3 4 ARG C 102 ASP C 202 GOL C 289 HOH C 669
SITE 1 EC4 5 THR C 71 ASP C 74 SO4 C 276 HOH C 847
SITE 2 EC4 5 HOH C1072
SITE 1 EC5 10 GLY C 27 TRP C 28 ILE C 29 LEU C 30
SITE 2 EC5 10 PHE C 93 SER C 94 PHE C 158 PHE C 162
SITE 3 EC5 10 HIS C 251 ACT C 283
SITE 1 EC6 9 TRP C 28 SER C 94 MET C 95 VAL C 121
SITE 2 EC6 9 PHE C 125 PHE C 198 ILE C 224 HIS C 251
SITE 3 EC6 9 ACT C 282
SITE 1 EC7 2 GLN C 259 GLU C 263
SITE 1 EC8 7 ASP C 7 PRO C 63 TRP C 64 THR C 65
SITE 2 EC8 7 HOH C 337 HOH C1094 HOH C1095
SITE 1 EC9 4 ILE C 224 GOL C 279 ACT C 287 HOH C 895
SITE 1 FC1 5 TRP C 28 PHE C 143 PHE C 158 GOL C 279
SITE 2 FC1 5 ACT C 286
SITE 1 FC2 4 ASN A 166 SER C 18 GLY C 19 HOH C 870
SITE 1 FC3 3 LYS C 128 ASP C 202 PEO C 280
SITE 1 FC4 5 LEU D 137 ALA D 141 LYS D 144 GLU D 200
SITE 2 FC4 5 HOH D 628
SITE 1 FC5 7 SER D 1 TYR D 12 LYS D 14 ASP D 15
SITE 2 FC5 7 HOH D 401 ASP E 61 GLN E 62
SITE 1 FC6 1 ARG D 106
SITE 1 FC7 1 HOH D 573
SITE 1 FC8 4 VAL D 245 LYS D 247 GLN D 260 HOH D 374
SITE 1 FC9 7 PHE D 125 VAL D 139 GLN D 223 ILE D 224
SITE 2 FC9 7 GOL D 284 HOH D 359 HOH D1080
SITE 1 GC1 1 ASP D 202
SITE 1 GC2 2 THR D 214 GLY D 240
SITE 1 GC3 4 LYS D 239 GLY D 240 HOH D 500 HOH D 657
SITE 1 GC4 2 GLU D 40 ARG D 45
SITE 1 GC5 9 GLY D 27 TRP D 28 ILE D 29 PHE D 93
SITE 2 GC5 9 SER D 94 PHE D 158 PHE D 162 HIS D 251
SITE 3 GC5 9 ACT D 283
SITE 1 GC6 10 TRP D 28 SER D 94 MET D 95 VAL D 121
SITE 2 GC6 10 PHE D 125 PHE D 198 ILE D 224 HIS D 251
SITE 3 GC6 10 ACT D 282 GOL D 284
SITE 1 GC7 9 TRP D 28 PHE D 140 PHE D 143 PHE D 158
SITE 2 GC7 9 PHE D 198 ILE D 224 GOL D 277 ACT D 283
SITE 3 GC7 9 HOH D1080
SITE 1 GC8 5 ALA D 235 GLU D 236 ALA D 241 HOH D 423
SITE 2 GC8 5 HOH D 887
SITE 1 GC9 5 GLN D 127 LYS D 128 PRO D 129 PRO D 132
SITE 2 GC9 5 HOH D 779
SITE 1 HC1 7 SER E 1 TYR E 12 LYS E 14 ASP E 15
SITE 2 HC1 7 HOH E 859 ASP F 61 GLN F 62
SITE 1 HC2 5 LEU E 137 ALA E 141 LYS E 144 GLU E 200
SITE 2 HC2 5 HOH E 814
SITE 1 HC3 1 ARG E 106
SITE 1 HC4 3 LYS E 239 GLY E 240 HOH E 794
SITE 1 HC5 2 LYS E 247 GLN E 260
SITE 1 HC6 6 PHE E 143 GLN E 223 ILE E 224 PRO E 226
SITE 2 HC6 6 ACT E 286 ACT E 287
SITE 1 HC7 5 GLN E 173 GLY E 174 THR E 177 SER F 156
SITE 2 HC7 5 LEU F 180
SITE 1 HC8 2 SER E 18 GLY E 19
SITE 1 HC9 2 THR E 65 GLY E 66
SITE 1 IC1 10 LEU E 30 MET E 34 TYR E 163 GLN E 178
SITE 2 IC1 10 THR E 179 ILE E 182 VAL E 255 HOH E 326
SITE 3 IC1 10 HOH E 929 HOH E1125
SITE 1 IC2 4 TYR D 37 VAL D 175 LYS E 149 HOH E1115
SITE 1 IC3 8 GLY E 27 TRP E 28 LEU E 30 PHE E 93
SITE 2 IC3 8 SER E 94 PHE E 162 HIS E 251 ACT E 284
SITE 1 IC4 8 TRP E 28 SER E 94 MET E 95 VAL E 121
SITE 2 IC4 8 PHE E 125 PHE E 198 ILE E 224 ACT E 283
SITE 1 IC5 6 ASP E 7 PRO E 63 TRP E 64 THR E 65
SITE 2 IC5 6 HOH E 315 HOH E 335
SITE 1 IC6 4 ILE E 224 GOL E 277 ACT E 287 ACT E 290
SITE 1 IC7 7 TRP E 28 PHE E 140 PHE E 143 PHE E 158
SITE 2 IC7 7 ILE E 224 GOL E 277 ACT E 286
SITE 1 IC8 2 THR E 201 ASP E 202
SITE 1 IC9 5 LYS E 6 ASP E 74 GLU E 81 HIS E 107
SITE 2 IC9 5 HOH E1150
SITE 1 JC1 4 PHE E 154 PHE E 158 ACT E 286 HOH E1123
SITE 1 JC2 7 ASP D 61 GLN D 62 SER F 1 TYR F 12
SITE 2 JC2 7 LYS F 14 ASP F 15 HOH F 322
SITE 1 JC3 5 VAL F 245 TYR F 246 LYS F 247 GLN F 260
SITE 2 JC3 5 HOH F 548
SITE 1 JC4 5 ILE F 238 LYS F 239 GLY F 240 HOH F 535
SITE 2 JC4 5 HOH F 646
SITE 1 JC5 1 ARG F 106
SITE 1 JC6 5 PHE F 143 GLN F 223 ILE F 224 PRO F 226
SITE 2 JC6 5 ACT F 286
SITE 1 JC7 2 LYS F 144 GLU F 200
SITE 1 JC8 1 TRP F 64
SITE 1 JC9 3 SER F 156 ASN F 159 GLN F 173
SITE 1 KC1 3 PHE F 143 ACT F 286 HOH F 818
SITE 1 KC2 8 TRP F 28 SER F 94 MET F 95 VAL F 121
SITE 2 KC2 8 PHE F 125 PHE F 198 ILE F 224 ACT F 282
SITE 1 KC3 6 GLY F 27 TRP F 28 SER F 94 PHE F 162
SITE 2 KC3 6 HIS F 251 ACT F 281
SITE 1 KC4 6 ASP F 7 PRO F 63 TRP F 64 THR F 65
SITE 2 KC4 6 HOH F 320 HOH F1092
SITE 1 KC5 7 LEU D 148 TYR F 37 GLU F 40 ALA F 258
SITE 2 KC5 7 ASN F 262 HOH F 619 HOH F 620
SITE 1 KC6 12 LEU F 30 ASP F 31 MET F 34 TYR F 163
SITE 2 KC6 12 GLN F 178 THR F 179 ILE F 182 VAL F 255
SITE 3 KC6 12 HOH F 325 HOH F 436 HOH F 810 HOH F 828
SITE 1 KC7 7 TRP F 28 PHE F 140 PHE F 143 PHE F 158
SITE 2 KC7 7 ILE F 224 GOL F 276 GOL F 280
SITE 1 KC8 1 ARG F 45
CRYST1 146.020 146.020 128.950 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 0.006848 0.003954 0.000000 0.00000
SCALE2 0.000000 0.007908 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007755 0.00000
TER 2181 ARG A 271
TER 4379 ARG B 271
TER 6553 ARG C 271
TER 8713 ARG D 271
TER 10911 ARG E 271
TER 13106 ARG F 271
MASTER 737 0 98 78 48 0 155 614294 6 422 126
END |