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HEADER HYDROLASE 11-DEC-09 3L1J
TITLE CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY ZNSO4
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE/LIPASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ESTE5;
COMPND 5 EC: 3.1.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 OTHER_DETAILS: SOIL METAGENOME LIBRARY
KEYWDS HSL, ESTE5, ESTERASE, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.H.NAM,K.Y.HWANG
REVDAT 1 19-JAN-10 3L1J 0
JRNL AUTH K.H.NAM,K.Y.HWANG
JRNL TITL STRUCTURAL INSIGHTS INTO THE NONINVASIVE INHIBITION
JRNL TITL 2 OF HSL-HOMOLOG ESTE5 BY ORGANIC SOLVENTS AND METAL
JRNL TITL 3 IONS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
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) : 43.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.5
REMARK 3 NUMBER OF REFLECTIONS : 18597
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1898
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) : 606
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 46.27
REMARK 3 BIN R VALUE (WORKING SET) : 0.2680
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3540
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2222
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 97
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.27000
REMARK 3 B22 (A**2) : 0.27000
REMARK 3 B33 (A**2) : -0.53000
REMARK 3 B12 (A**2) : 0.00000
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): 0.219
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.196
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.123
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.441
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2274 ; 0.021 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3084 ; 1.806 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 292 ; 6.490 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 90 ;35.112 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 376 ;17.665 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;19.735 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 338 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1720 ; 0.009 ; 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): 1462 ; 0.996 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2331 ; 1.703 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 812 ; 3.018 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 753 ; 4.442 ; 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 : 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
REMARK 3 RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3L1J COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-DEC-09.
REMARK 100 THE RCSB ID CODE IS RCSB056715.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-FEB-09
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 : PAL/PLS
REMARK 200 BEAMLINE : 6C1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.23
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18624
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
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 (%) : 52.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 3FAK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 7.5, 2.2M AMMONIUM
REMARK 280 SULFATE, 0.2M LITHIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.33700
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.55700
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.55700
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.66850
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.55700
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.55700
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 113.00550
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.55700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.55700
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.66850
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.55700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.55700
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 113.00550
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 75.33700
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -12
REMARK 465 ALA A -11
REMARK 465 SER A -10
REMARK 465 MET A -9
REMARK 465 THR A -8
REMARK 465 GLY A -7
REMARK 465 GLY A -6
REMARK 465 GLN A -5
REMARK 465 GLN A -4
REMARK 465 MET A -3
REMARK 465 GLY A -2
REMARK 465 ARG A -1
REMARK 465 GLY A 0
REMARK 465 VAL A 194
REMARK 465 ALA A 195
REMARK 465 PRO A 196
REMARK 465 LEU A 298
REMARK 465 ALA A 299
REMARK 465 ALA A 300
REMARK 465 ALA A 301
REMARK 465 LEU A 302
REMARK 465 GLU A 303
REMARK 465 HIS A 304
REMARK 465 HIS A 305
REMARK 465 HIS A 306
REMARK 465 HIS A 307
REMARK 465 HIS A 308
REMARK 465 HIS A 309
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 349 O HOH A 399 2.00
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 361 O HOH A 380 7455 1.52
REMARK 500 O HOH A 362 O HOH A 374 7455 1.93
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 115 30.72 -98.13
REMARK 500 SER A 144 -127.41 67.48
REMARK 500 ASP A 237 56.51 -104.19
REMARK 500 ASP A 265 -1.73 65.88
REMARK 500 HIS A 268 117.14 -36.48
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 A 326 DISTANCE = 5.36 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3FAK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTE5 (NATIVE)
REMARK 900 RELATED ID: 3H17 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTE5-PMSF (I)
REMARK 900 RELATED ID: 3H18 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTE5-PMSF (II)
REMARK 900 RELATED ID: 3H19 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY METHYL ALCOHOL
REMARK 900 RELATED ID: 3H1A RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY ETHYL ALCOHOL
REMARK 900 RELATED ID: 3H1B RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY ISOPROPYL ALCOHOL
REMARK 900 RELATED ID: 3L1H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY FECL3
REMARK 900 RELATED ID: 3L1I RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY CUSO4
DBREF 3L1J A 1 297 UNP Q0GMU2 Q0GMU2_9BACT 1 297
SEQADV 3L1J MET A -12 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J ALA A -11 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J SER A -10 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J MET A -9 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J THR A -8 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J GLY A -7 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J GLY A -6 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J GLN A -5 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J GLN A -4 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J MET A -3 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J GLY A -2 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J ARG A -1 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J GLY A 0 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J LEU A 298 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J ALA A 299 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J ALA A 300 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J ALA A 301 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J LEU A 302 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J GLU A 303 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J HIS A 304 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J HIS A 305 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J HIS A 306 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J HIS A 307 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J HIS A 308 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3L1J HIS A 309 UNP Q0GMU2 EXPRESSION TAG
SEQRES 1 A 322 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY
SEQRES 2 A 322 MET ALA GLY PRO GLU ILE VAL LYS LEU LYS LYS ILE LEU
SEQRES 3 A 322 ARG GLU LYS ALA VAL PRO PRO GLY THR GLU VAL PRO LEU
SEQRES 4 A 322 ASP VAL MET ARG LYS GLY MET GLU LYS VAL ALA PHE LYS
SEQRES 5 A 322 ALA ALA ASP ASP ILE GLN VAL GLU GLN VAL THR VAL ALA
SEQRES 6 A 322 GLY CYS ALA ALA GLU TRP VAL ARG ALA PRO GLY CYS GLN
SEQRES 7 A 322 ALA GLY LYS ALA ILE LEU TYR LEU HIS GLY GLY GLY TYR
SEQRES 8 A 322 VAL MET GLY SER ILE ASN THR HIS ARG SER MET VAL GLY
SEQRES 9 A 322 GLU ILE SER ARG ALA SER GLN ALA ALA ALA LEU LEU LEU
SEQRES 10 A 322 ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA
SEQRES 11 A 322 VAL GLU ASP GLY VAL ALA ALA TYR ARG TRP LEU LEU ASP
SEQRES 12 A 322 GLN GLY PHE LYS PRO GLN HIS LEU SER ILE SER GLY ASP
SEQRES 13 A 322 SER ALA GLY GLY GLY LEU VAL LEU ALA VAL LEU VAL SER
SEQRES 14 A 322 ALA ARG ASP GLN GLY LEU PRO MET PRO ALA SER ALA ILE
SEQRES 15 A 322 PRO ILE SER PRO TRP ALA ASP MET THR CYS THR ASN ASP
SEQRES 16 A 322 SER PHE LYS THR ARG ALA GLU ALA ASP PRO MET VAL ALA
SEQRES 17 A 322 PRO GLY GLY ILE ASN LYS MET ALA ALA ARG TYR LEU ASN
SEQRES 18 A 322 GLY ALA ASP ALA LYS HIS PRO TYR ALA SER PRO ASN PHE
SEQRES 19 A 322 ALA ASN LEU LYS GLY LEU PRO PRO LEU LEU ILE HIS VAL
SEQRES 20 A 322 GLY ARG ASP GLU VAL LEU LEU ASP ASP SER ILE LYS LEU
SEQRES 21 A 322 ASP ALA LYS ALA LYS ALA ASP GLY VAL LYS SER THR LEU
SEQRES 22 A 322 GLU ILE TRP ASP ASP MET ILE HIS VAL TRP HIS ALA PHE
SEQRES 23 A 322 HIS PRO MET LEU PRO GLU GLY LYS GLN ALA ILE VAL ARG
SEQRES 24 A 322 VAL GLY GLU PHE MET ARG GLU GLN TRP ALA ALA LEU ALA
SEQRES 25 A 322 ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
FORMUL 2 HOH *97(H2 O)
HELIX 1 1 GLY A 3 ALA A 17 1 15
HELIX 2 2 PRO A 25 VAL A 36 1 12
HELIX 3 3 SER A 82 GLN A 98 1 17
HELIX 4 4 PRO A 115 GLY A 132 1 18
HELIX 5 5 LYS A 134 GLN A 136 5 3
HELIX 6 6 SER A 144 GLN A 160 1 17
HELIX 7 7 ASP A 182 ARG A 187 1 6
HELIX 8 8 GLY A 197 ASN A 208 1 12
HELIX 9 9 SER A 218 ALA A 222 5 5
HELIX 10 10 LEU A 240 ASP A 254 1 15
HELIX 11 11 VAL A 269 HIS A 274 5 6
HELIX 12 12 LEU A 277 ALA A 297 1 21
SHEET 1 A 6 GLN A 45 VAL A 51 0
SHEET 2 A 6 CYS A 54 ARG A 60 -1 O CYS A 54 N VAL A 51
SHEET 3 A 6 ALA A 100 LEU A 104 -1 O LEU A 103 N GLU A 57
SHEET 4 A 6 ALA A 69 LEU A 73 1 N ILE A 70 O LEU A 102
SHEET 5 A 6 LEU A 138 ASP A 143 1 O SER A 141 N LEU A 73
SHEET 6 A 6 SER A 167 ILE A 171 1 O ILE A 171 N GLY A 142
SHEET 1 B 2 LEU A 230 GLY A 235 0
SHEET 2 B 2 SER A 258 TRP A 263 1 O GLU A 261 N ILE A 232
CISPEP 1 ALA A 109 PRO A 110 0 2.67
CISPEP 2 PHE A 114 PRO A 115 0 3.84
CRYST1 61.114 61.114 150.674 90.00 90.00 90.00 P 41 21 2 8
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 0.016363 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016363 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006637 0.00000
TER 2223 ALA A 297
MASTER 366 0 0 12 8 0 0 6 2319 1 0 25
END |