| content |
HEADER HYDROLASE 21-NOV-05 2C7B
TITLE THE CRYSTAL STRUCTURE OF ESTE1, A NEW THERMOPHILIC AND
TITLE 2 THERMOSTABLE CARBOXYLESTERASE CLONED FROM A METAGENOMIC
TITLE 3 LIBRARY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 SYNONYM: ESTE1;
COMPND 4 CHAIN: A, B;
COMPND 5 FRAGMENT: ALPHA-BETA HYDROLASE FOLD, RESIDUES 1-311;
COMPND 6 EC: 3.1.1.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 3 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)B834;
SOURCE 4 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 5 ORGANISM_SCIENTIFIC: UNCULTURED ARCHAEON;
SOURCE 6 OTHER_DETAILS: METAGENOMES FROM THERMAL ENVIRONMENTAL
SOURCE 7 SAMPLES
KEYWDS CARBOXYESTERASE, THERMOPHILIC ENZYME, HYDROLASE, HSL,
KEYWDS 2 ALPHA/BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR J.-S.BYUN,J.-K.RHEE,D.-U.KIM,J.-W.OH,H.-S.CHO
REVDAT 1 01-DEC-05 2C7B 0
JRNL AUTH J.-S.BYUN,J.-K.RHEE,D.-U.KIM,J.-W.OH,H.-S.CHO
JRNL TITL THE CRYSTAL STRUCTURE OF ESTE1, A NEW THERMOPHILIC
JRNL TITL 2 AND THERMOSTABLE CARBOXYLESTERASE CLONED FROM A
JRNL TITL 3 METAGENOMIC LIBRARY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.3 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,
REMARK 3 GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,
REMARK 3 PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.3
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.0
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.0
REMARK 3 OUTLIER CUTOFF HIGH (RMS(ABS(F))) : 10000
REMARK 3 COMPLETENESS FOR RANGE (%) : 76.1
REMARK 3 NUMBER OF REFLECTIONS : 54674
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.2338
REMARK 3 FREE R VALUE : 0.2613
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.8
REMARK 3 FREE R VALUE TEST SET COUNT : 2721
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.01
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4405
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 138
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.777
REMARK 3 B22 (A**2) : -2.777
REMARK 3 B33 (A**2) : 5.554
REMARK 3 B12 (A**2) : 0.000
REMARK 3 B13 (A**2) : 0.000
REMARK 3 B23 (A**2) : 0.000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.7
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : N/A
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : 0.363934
REMARK 3 BSOL : 40.3777
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 2 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 2 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 3 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 3 B-FACTOR (A**2) : NULL ; NULL
REMARK 3 GROUP 4 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 4 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2C7B COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI ON 21-NOV-2005.
REMARK 100 THE EBI ID CODE IS EBI-26498.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUL-2005
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 BEAMLINE 6B
REMARK 200 BEAMLINE : 6B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD (PROTEUM)
REMARK 200 DETECTOR MANUFACTURER : BRUKER AXS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29848
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.30
REMARK 200 RESOLUTION RANGE LOW (A) : 20.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 4.1
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 2
REMARK 200 R MERGE (I) : 0.12
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.60
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) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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 : 4.10
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.74
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH6.5, 0.2M
REMARK 280 AMMONIUM SULFATE, 35%(W/V) PEG 3350
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,1/2+Z
REMARK 290 3555 1/2-Y,1/2+X,1/4+Z
REMARK 290 4555 1/2+Y,1/2-X,3/4+Z
REMARK 290 5555 1/2-X,1/2+Y,1/4-Z
REMARK 290 6555 1/2+X,1/2-Y,3/4-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,1/2-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -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 117.11500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 36.85500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 36.85500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 58.55750
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 36.85500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 36.85500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 175.67250
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 36.85500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 36.85500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 58.55750
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 36.85500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 36.85500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 175.67250
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 117.11500
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 300
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: TETRAMERIC
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 234.23000
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 MSE A 1
REMARK 465 PRO A 2
REMARK 465 LEU A 3
REMARK 465 ASP A 4
REMARK 465 PRO A 5
REMARK 465 GLN A 6
REMARK 465 ILE A 7
REMARK 465 LYS A 8
REMARK 465 PRO A 9
REMARK 465 ILE A 10
REMARK 465 LEU A 11
REMARK 465 GLU A 12
REMARK 465 ARG A 13
REMARK 465 ILE A 14
REMARK 465 ARG A 15
REMARK 465 ALA A 16
REMARK 465 MSE B 1
REMARK 465 PRO B 2
REMARK 465 LEU B 3
REMARK 465 ASP B 4
REMARK 465 PRO B 5
REMARK 465 GLN B 6
REMARK 465 ILE B 7
REMARK 465 LYS B 8
REMARK 465 PRO B 9
REMARK 465 ILE B 10
REMARK 465 LEU B 11
REMARK 465 GLU B 12
REMARK 465 ARG B 13
REMARK 465 ILE B 14
REMARK 465 ARG B 15
REMARK 465 ALA B 16
REMARK 465 LEU B 17
REMARK 465 SER B 18
REMARK 465 ILE B 19
REMARK 465 ALA B 20
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 311 CA C O CB OG
REMARK 470 SER B 311 CA C O CB OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 121 C - N - CA ANGL. DEV. = 54.7 DEGREES
REMARK 500 VAL B 41 N - CA - C ANGL. DEV. = -20.0 DEGREES
REMARK 500 ALA B 46 C - N - CA ANGL. DEV. = 17.9 DEGREES
REMARK 500 ALA B 46 CA - C - N ANGL. DEV. = 17.9 DEGREES
REMARK 500 ALA B 46 O - C - N ANGL. DEV. = -15.4 DEGREES
REMARK 500 ALA B 115 C - N - CA ANGL. DEV. = -18.5 DEGREES
REMARK 500 ALA B 115 CA - C - N ANGL. DEV. = -32.6 DEGREES
REMARK 500 ALA B 115 O - C - N ANGL. DEV. = 21.9 DEGREES
REMARK 500 PRO B 116 C - N - CA ANGL. DEV. = 43.0 DEGREES
REMARK 500 PRO B 116 CA - N - CD ANGL. DEV. = -47.9 DEGREES
REMARK 500 PRO B 116 CB - CG - CD ANGL. DEV. = -17.6 DEGREES
REMARK 500 PRO B 121 CA - N - CD ANGL. DEV. = -45.9 DEGREES
REMARK 500 THR B 203 CA - C - N ANGL. DEV. = 19.6 DEGREES
REMARK 500 THR B 203 O - C - N ANGL. DEV. = -23.4 DEGREES
REMARK 500 THR B 204 CA - C - N ANGL. DEV. = -17.3 DEGREES
REMARK 500 THR B 204 O - C - N ANGL. DEV. = 16.4 DEGREES
REMARK 500 SER B 205 C - N - CA ANGL. DEV. = 18.0 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD AND BY MORE THAN 0.150 ANGSTROMS (M=MODEL
REMARK 500 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 500 NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,1X,2(A4,A1,3X),12X,F5.3)
REMARK 500
REMARK 500 EXPECTED VALUESS: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG B 98 C LEU B 99 N -0.216
REMARK 500 LEU B 114 C ALA B 115 N 0.236
REMARK 500 ALA B 115 C PRO B 116 N 0.411
REMARK 500 THR B 203 C THR B 204 N -0.266
REMARK 500
REMARK 500 REMARK: NULL
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 ND1 HIS A 52 O HOH Z 18 2.11
REMARK 500 NH1 ARG A 216 O HOH Z 62 1.33
REMARK 500 CG GLN B 29 NE2 GLN B 33 1.59
REMARK 500 OE2 GLU B 43 OH TYR B 287 2.11
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 N ASP B 139 NH2 ARG B 221 6455 1.63
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY
REMARK 525 ASSOCIATED WITH:
REMARK 525 PROTEIN CHAIN SOLVENT CHAIN
REMARK 525 A Z
REMARK 525 B Y
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BZQ RELATED DB: PDB
REMARK 900 ANALYSIS OF THE THERMOSTABILITY DETERMINANTS
REMARK 900 OF HYPERTHERMOPHILIC ESTERASE, ESTE1, BASED ON
REMARK 900 THE PREDICTED THREE-DIMENSIONAL STRUCTURE
DBREF 2C7B A 1 311 UNP Q5G935 Q5G935_9ARCH 1 311
DBREF 2C7B B 1 311 UNP Q5G935 Q5G935_9ARCH 1 311
SEQRES 1 A 311 MSE PRO LEU ASP PRO GLN ILE LYS PRO ILE LEU GLU ARG
SEQRES 2 A 311 ILE ARG ALA LEU SER ILE ALA ALA SER PRO GLN GLU LEU
SEQRES 3 A 311 ARG ARG GLN VAL GLU GLU GLN SER ARG LEU LEU THR ALA
SEQRES 4 A 311 ALA VAL GLN GLU PRO ILE ALA GLU THR ARG ASP VAL HIS
SEQRES 5 A 311 ILE PRO VAL SER GLY GLY SER ILE ARG ALA ARG VAL TYR
SEQRES 6 A 311 PHE PRO LYS LYS ALA ALA GLY LEU PRO ALA VAL LEU TYR
SEQRES 7 A 311 TYR HIS GLY GLY GLY PHE VAL PHE GLY SER ILE GLU THR
SEQRES 8 A 311 HIS ASP HIS ILE CYS ARG ARG LEU SER ARG LEU SER ASP
SEQRES 9 A 311 SER VAL VAL VAL SER VAL ASP TYR ARG LEU ALA PRO GLU
SEQRES 10 A 311 TYR LYS PHE PRO THR ALA VAL GLU ASP ALA TYR ALA ALA
SEQRES 11 A 311 LEU LYS TRP VAL ALA ASP ARG ALA ASP GLU LEU GLY VAL
SEQRES 12 A 311 ASP PRO ASP ARG ILE ALA VAL ALA GLY ASP SER ALA GLY
SEQRES 13 A 311 GLY ASN LEU ALA ALA VAL VAL SER ILE LEU ASP ARG ASN
SEQRES 14 A 311 SER GLY GLU LYS LEU VAL LYS LYS GLN VAL LEU ILE TYR
SEQRES 15 A 311 PRO VAL VAL ASN MSE THR GLY VAL PRO THR ALA SER LEU
SEQRES 16 A 311 VAL GLU PHE GLY VAL ALA GLU THR THR SER LEU PRO ILE
SEQRES 17 A 311 GLU LEU MSE VAL TRP PHE GLY ARG GLN TYR LEU LYS ARG
SEQRES 18 A 311 PRO GLU GLU ALA TYR ASP PHE LYS ALA SER PRO LEU LEU
SEQRES 19 A 311 ALA ASP LEU GLY GLY LEU PRO PRO ALA LEU VAL VAL THR
SEQRES 20 A 311 ALA GLU TYR ASP PRO LEU ARG ASP GLU GLY GLU LEU TYR
SEQRES 21 A 311 ALA TYR LYS MSE LYS ALA SER GLY SER ARG ALA VAL ALA
SEQRES 22 A 311 VAL ARG PHE ALA GLY MSE VAL HIS GLY PHE VAL SER PHE
SEQRES 23 A 311 TYR PRO PHE VAL ASP ALA GLY ARG GLU ALA LEU ASP LEU
SEQRES 24 A 311 ALA ALA ALA SER ILE ARG SER GLY LEU GLN PRO SER
SEQRES 1 B 311 MSE PRO LEU ASP PRO GLN ILE LYS PRO ILE LEU GLU ARG
SEQRES 2 B 311 ILE ARG ALA LEU SER ILE ALA ALA SER PRO GLN GLU LEU
SEQRES 3 B 311 ARG ARG GLN VAL GLU GLU GLN SER ARG LEU LEU THR ALA
SEQRES 4 B 311 ALA VAL GLN GLU PRO ILE ALA GLU THR ARG ASP VAL HIS
SEQRES 5 B 311 ILE PRO VAL SER GLY GLY SER ILE ARG ALA ARG VAL TYR
SEQRES 6 B 311 PHE PRO LYS LYS ALA ALA GLY LEU PRO ALA VAL LEU TYR
SEQRES 7 B 311 TYR HIS GLY GLY GLY PHE VAL PHE GLY SER ILE GLU THR
SEQRES 8 B 311 HIS ASP HIS ILE CYS ARG ARG LEU SER ARG LEU SER ASP
SEQRES 9 B 311 SER VAL VAL VAL SER VAL ASP TYR ARG LEU ALA PRO GLU
SEQRES 10 B 311 TYR LYS PHE PRO THR ALA VAL GLU ASP ALA TYR ALA ALA
SEQRES 11 B 311 LEU LYS TRP VAL ALA ASP ARG ALA ASP GLU LEU GLY VAL
SEQRES 12 B 311 ASP PRO ASP ARG ILE ALA VAL ALA GLY ASP SER ALA GLY
SEQRES 13 B 311 GLY ASN LEU ALA ALA VAL VAL SER ILE LEU ASP ARG ASN
SEQRES 14 B 311 SER GLY GLU LYS LEU VAL LYS LYS GLN VAL LEU ILE TYR
SEQRES 15 B 311 PRO VAL VAL ASN MSE THR GLY VAL PRO THR ALA SER LEU
SEQRES 16 B 311 VAL GLU PHE GLY VAL ALA GLU THR THR SER LEU PRO ILE
SEQRES 17 B 311 GLU LEU MSE VAL TRP PHE GLY ARG GLN TYR LEU LYS ARG
SEQRES 18 B 311 PRO GLU GLU ALA TYR ASP PHE LYS ALA SER PRO LEU LEU
SEQRES 19 B 311 ALA ASP LEU GLY GLY LEU PRO PRO ALA LEU VAL VAL THR
SEQRES 20 B 311 ALA GLU TYR ASP PRO LEU ARG ASP GLU GLY GLU LEU TYR
SEQRES 21 B 311 ALA TYR LYS MSE LYS ALA SER GLY SER ARG ALA VAL ALA
SEQRES 22 B 311 VAL ARG PHE ALA GLY MSE VAL HIS GLY PHE VAL SER PHE
SEQRES 23 B 311 TYR PRO PHE VAL ASP ALA GLY ARG GLU ALA LEU ASP LEU
SEQRES 24 B 311 ALA ALA ALA SER ILE ARG SER GLY LEU GLN PRO SER
MODRES 2C7B MSE A 187 MET SELENOMETHIONINE
MODRES 2C7B MSE A 211 MET SELENOMETHIONINE
MODRES 2C7B MSE A 264 MET SELENOMETHIONINE
MODRES 2C7B MSE A 279 MET SELENOMETHIONINE
MODRES 2C7B MSE B 187 MET SELENOMETHIONINE
MODRES 2C7B MSE B 211 MET SELENOMETHIONINE
MODRES 2C7B MSE B 264 MET SELENOMETHIONINE
MODRES 2C7B MSE B 279 MET SELENOMETHIONINE
HET MSE A 187 8
HET MSE A 211 8
HET MSE A 264 8
HET MSE A 279 8
HET MSE B 187 8
HET MSE B 211 8
HET MSE B 264 8
HET MSE B 279 8
HETNAM MSE SELENOMETHIONINE
FORMUL 3 MSE 8(C5 H11 N1 O2 SE1)
FORMUL 4 HOH *138(H2 O1)
HELIX 1 1 SER A 22 ALA A 40 1 19
HELIX 2 2 ILE A 89 THR A 91 5 3
HELIX 3 3 HIS A 92 ASP A 104 1 13
HELIX 4 4 PRO A 121 ARG A 137 1 17
HELIX 5 5 ARG A 137 GLY A 142 1 6
HELIX 6 6 SER A 154 SER A 170 1 17
HELIX 7 7 THR A 192 ALA A 201 1 10
HELIX 8 8 PRO A 207 LEU A 219 1 13
HELIX 9 9 GLU A 223 ASP A 227 5 5
HELIX 10 10 SER A 231 ALA A 235 5 5
HELIX 11 11 LEU A 253 SER A 267 1 15
HELIX 12 12 GLY A 282 TYR A 287 5 6
HELIX 13 13 VAL A 290 LEU A 308 1 19
HELIX 14 14 SER B 22 THR B 38 1 17
HELIX 15 15 ILE B 89 THR B 91 5 3
HELIX 16 16 HIS B 92 ASP B 104 1 13
HELIX 17 17 PRO B 121 ARG B 137 1 17
HELIX 18 18 ARG B 137 GLY B 142 1 6
HELIX 19 19 SER B 154 GLY B 171 1 18
HELIX 20 20 THR B 192 ALA B 201 1 10
HELIX 21 21 PRO B 207 LEU B 219 1 13
HELIX 22 22 PRO B 222 ASP B 227 5 6
HELIX 23 23 SER B 231 ALA B 235 5 5
HELIX 24 24 LEU B 253 SER B 267 1 15
HELIX 25 25 GLY B 282 PHE B 289 5 8
HELIX 26 26 VAL B 290 LEU B 308 1 19
SHEET 1 AA 8 GLU A 47 VAL A 55 0
SHEET 2 AA 8 GLY A 58 PHE A 66 -1 O GLY A 58 N VAL A 55
SHEET 3 AA 8 VAL A 106 VAL A 110 -1 O VAL A 107 N TYR A 65
SHEET 4 AA 8 LEU A 73 TYR A 79 1 O PRO A 74 N VAL A 106
SHEET 5 AA 8 VAL A 143 ASP A 153 1 N ASP A 144 O LEU A 73
SHEET 6 AA 8 LYS A 177 ILE A 181 1 O LYS A 177 N VAL A 150
SHEET 7 AA 8 ALA A 243 ALA A 248 1 O LEU A 244 N LEU A 180
SHEET 8 AA 8 ALA A 271 PHE A 276 1 O VAL A 272 N VAL A 245
SHEET 1 BA 8 GLU B 47 VAL B 55 0
SHEET 2 BA 8 GLY B 58 PHE B 66 -1 O GLY B 58 N VAL B 55
SHEET 3 BA 8 VAL B 106 ASP B 111 -1 O VAL B 107 N TYR B 65
SHEET 4 BA 8 LEU B 73 TYR B 79 1 O PRO B 74 N VAL B 106
SHEET 5 BA 8 VAL B 143 ASP B 153 1 N ASP B 144 O LEU B 73
SHEET 6 BA 8 LYS B 177 ILE B 181 1 O LYS B 177 N VAL B 150
SHEET 7 BA 8 ALA B 243 TYR B 250 1 O LEU B 244 N LEU B 180
SHEET 8 BA 8 ALA B 271 VAL B 280 1 O VAL B 272 N VAL B 245
LINK C ASN A 186 N MSE A 187 1555 1555
LINK C MSE A 187 N THR A 188 1555 1555
LINK C LEU A 210 N MSE A 211 1555 1555
LINK C MSE A 211 N VAL A 212 1555 1555
LINK C LYS A 263 N MSE A 264 1555 1555
LINK C MSE A 264 N LYS A 265 1555 1555
LINK C GLY A 278 N MSE A 279 1555 1555
LINK C MSE A 279 N VAL A 280 1555 1555
LINK C ASN B 186 N MSE B 187 1555 1555
LINK C MSE B 187 N THR B 188 1555 1555
LINK C LEU B 210 N MSE B 211 1555 1555
LINK C MSE B 211 N VAL B 212 1555 1555
LINK C LYS B 263 N MSE B 264 1555 1555
LINK C MSE B 264 N LYS B 265 1555 1555
LINK C GLY B 278 N MSE B 279 1555 1555
LINK C MSE B 279 N VAL B 280 1555 1555
CISPEP 1 ALA A 115 PRO A 116 0 -0.30
CISPEP 2 PRO B 310 SER B 311 0 2.75
CRYST1 73.710 73.710 234.230 90.00 90.00 90.00 P 41 21 2 16
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 0.013567 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013567 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004269 0.00000
TER 2249 SER A 311
TER 4471 SER B 311
MASTER 384 0 8 26 16 0 0 6 4607 2 80 48
END |