| content |
HEADER HYDROLASE 11-APR-09 3H19
TITLE CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY METHYL ALCOHOL
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 GENE: ESTE5;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-21A;
SOURCE 10 OTHER_DETAILS: SOIL METAGENOME LIBRARY
KEYWDS HSL, ESTE5, ESTERASE, LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.Y.HWANG,K.H.NAM
REVDAT 1 28-APR-09 3H19 0
JRNL AUTH K.Y.HWANG,K.H.NAM
JRNL TITL CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY ORGANIC
JRNL TITL 2 SOLVENT
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.5
REMARK 3 NUMBER OF REFLECTIONS : 11817
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) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.171
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 601
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 575
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 61.04
REMARK 3 BIN R VALUE (WORKING SET) : 0.2210
REMARK 3 BIN FREE R VALUE SET COUNT : 25
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2214
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 59
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.33
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.42000
REMARK 3 B22 (A**2) : 0.42000
REMARK 3 B33 (A**2) : -0.83000
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): 0.379
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.260
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.178
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.657
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.893
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2266 ; 0.023 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3074 ; 2.113 ; 1.966
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 291 ; 7.534 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 90 ;36.757 ;24.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 373 ;19.970 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;22.537 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 337 ; 0.139 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1716 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1077 ; 0.230 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1491 ; 0.310 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 103 ; 0.162 ; 0.200
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): 34 ; 0.254 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.325 ; 0.200
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): 1500 ; 1.009 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2323 ; 1.563 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 888 ; 2.773 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 751 ; 4.152 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 297
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1309 15.4148 0.0147
REMARK 3 T TENSOR
REMARK 3 T11: -0.0189 T22: -0.0141
REMARK 3 T33: -0.0173 T12: -0.0205
REMARK 3 T13: -0.0048 T23: -0.0029
REMARK 3 L TENSOR
REMARK 3 L11: 0.3145 L22: 0.2822
REMARK 3 L33: 0.5897 L12: 0.0426
REMARK 3 L13: 0.1550 L23: -0.0897
REMARK 3 S TENSOR
REMARK 3 S11: 0.0313 S12: 0.0012 S13: -0.0198
REMARK 3 S21: 0.0134 S22: 0.0051 S23: -0.0041
REMARK 3 S31: 0.0308 S32: 0.0221 S33: -0.0364
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3H19 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-APR-09.
REMARK 100 THE RCSB ID CODE IS RCSB052564.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-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-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12422
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
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 (%) : 92.1
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) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 65.3
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: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3FAK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
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 75.28750
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 30.61850
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 30.61850
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.64375
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 30.61850
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 30.61850
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 112.93125
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 30.61850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 30.61850
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 37.64375
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 30.61850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 30.61850
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 112.93125
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 75.28750
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 MET A 1
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 LYS A 252 CD - CE - NZ ANGL. DEV. = 13.9 DEGREES
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 ASP A 105 75.68 -105.66
REMARK 500 SER A 144 -127.07 65.88
REMARK 500 ASP A 176 95.38 -162.30
REMARK 500 ASP A 237 50.11 -105.22
REMARK 500 LYS A 257 92.85 -69.79
REMARK 500 ASP A 265 -0.55 69.04
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 192 MET A 193 -145.84
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 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: (11X,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 THR A 50 24.5 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
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: 3G9U RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY P-NITROPHENYL
REMARK 900 BUTYRATE FOR 5MIN
REMARK 900 RELATED ID: 3G9V RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY P-NITROPHENYL
REMARK 900 BUTYRATE FOR 5SEC
REMARK 900 RELATED ID: 3G9Z RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ESTE5, WAS SOAKED BY P-NITROPHENYL
REMARK 900 CAPRYLATE
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: 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
DBREF 3H19 A 1 297 UNP Q0GMU2 Q0GMU2_9BACT 1 297
SEQADV 3H19 MET A -12 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 ALA A -11 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 SER A -10 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 MET A -9 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 THR A -8 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 GLY A -7 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 GLY A -6 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 GLN A -5 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 GLN A -4 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 MET A -3 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 GLY A -2 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 ARG A -1 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 GLY A 0 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 LEU A 298 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 ALA A 299 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 ALA A 300 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 ALA A 301 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 LEU A 302 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 GLU A 303 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 HIS A 304 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 HIS A 305 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 HIS A 306 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 HIS A 307 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 HIS A 308 UNP Q0GMU2 EXPRESSION TAG
SEQADV 3H19 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 *59(H2 O)
HELIX 1 1 GLY A 3 ALA A 17 1 15
HELIX 2 2 PRO A 25 ALA A 37 1 13
HELIX 3 3 SER A 82 GLN A 98 1 17
HELIX 4 4 PRO A 115 GLN A 131 1 17
HELIX 5 5 LYS A 134 GLN A 136 5 3
HELIX 6 6 ALA A 145 GLN A 160 1 16
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 GLY A 255 1 16
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 ARG A 60 N GLN A 45
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 THR A 259 N ILE A 232
CISPEP 1 ALA A 109 PRO A 110 0 0.73
CISPEP 2 PHE A 114 PRO A 115 0 5.47
CRYST1 61.237 61.237 150.575 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 0.016330 0.000000 0.000000 0.00000
SCALE2 0.000000 0.016330 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006641 0.00000
TER 2215 ALA A 297
MASTER 393 0 0 12 8 0 0 6 2273 1 0 25
END |