HEADER LYASE 25-JAN-14 4CNV
TITLE SURFACE RESIDUE ENGINEERING OF BOVINE CARBONIC ANHYDRASE TO AN EXTREME
TITLE 2 HALOPHILIC ENZYME FOR POTENTIAL APPLICATION IN POSTCOMBUSTION CO2
TITLE 3 CAPTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBONIC ANHYDRASE 2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CARBONATE DEHYDRATASE II, CARBONIC ANHYDRASE II, CA-II;
COMPND 5 EC: 4.2.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: STAR;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET
KEYWDS LYASE, PROTEIN ENGINEERING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.WARDEN,J.NEWMAN,T.S.PEAT,S.SEABROOK,M.WILLIAMS,G.DOJCHINOV,
AUTHOR 2 V.HARITOS
REVDAT 3 20-DEC-23 4CNV 1 REMARK LINK
REVDAT 2 13-JAN-16 4CNV 1 JRNL
REVDAT 1 04-FEB-15 4CNV 0
JRNL AUTH A.C.WARDEN,M.WILLIAMS,T.S.PEAT,S.A.SEABROOK,J.NEWMAN,
JRNL AUTH 2 G.DOJCHINOV,V.S.HARITOS
JRNL TITL RATIONAL ENGINEERING OF A MESOHALOPHILIC CARBONIC ANHYDRASE
JRNL TITL 2 TO AN EXTREME HALOTOLERANT BIOCATALYST.
JRNL REF NAT.COMMUN. V. 6 10278 2015
JRNL REFN ESSN 2041-1723
JRNL PMID 26687908
JRNL DOI 10.1038/NCOMMS10278
REMARK 2
REMARK 2 RESOLUTION. 1.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.66
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 29409
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) : 0.145
REMARK 3 R VALUE (WORKING SET) : 0.143
REMARK 3 FREE R VALUE : 0.182
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1552
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.62
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.66
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2145
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2130
REMARK 3 BIN FREE R VALUE SET COUNT : 130
REMARK 3 BIN FREE R VALUE : 0.2370
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2036
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 13
REMARK 3 SOLVENT ATOMS : 249
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.62
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.04000
REMARK 3 B22 (A**2) : -0.35000
REMARK 3 B33 (A**2) : 0.23000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.37000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.081
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.085
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.050
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.432
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.966
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2185 ; 0.023 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2000 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2990 ; 2.104 ; 1.951
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4638 ; 0.953 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 273 ; 6.890 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 104 ;32.960 ;24.904
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 339 ;12.015 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;17.651 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 314 ; 0.137 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2533 ; 0.013 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 501 ; 0.001 ; 0.020
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): 1071 ; 1.465 ; 1.235
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1070 ; 1.464 ; 1.234
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1351 ; 2.177 ; 2.078
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1114 ; 3.138 ; 1.606
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 1.20
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 RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY.
REMARK 4
REMARK 4 4CNV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1290059564.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95370
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30981
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.620
REMARK 200 RESOLUTION RANGE LOW (A) : 42.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.400
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.62
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.64000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3ML2
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS AT 10 MG/ML; THE RESERVOIR
REMARK 280 SOLUTION WAS 5% PEG 1000, 30% PEG 600, 10% GLYCEROL, 100 MM
REMARK 280 SODIUM MES BUFFER AT PH 6. SEEDS OF THE MUT1 FORM WERE USED TO
REMARK 280 OBTAIN THESE CRYSTALS.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
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
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 34.63800
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 -1
REMARK 465 GLY A 0
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 HIS A 3
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 2111 O HOH A 2214 1.85
REMARK 500 O HOH A 2024 O HOH A 2243 1.86
REMARK 500 O HOH A 2025 O HOH A 2239 1.99
REMARK 500 O HOH A 2242 O HOH A 2243 2.15
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 (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 26 CD GLU A 26 OE1 0.108
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 41 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 LYS A 171 CD - CE - NZ ANGL. DEV. = 15.2 DEGREES
REMARK 500 MET A 240 CG - SD - CE ANGL. DEV. = -10.5 DEGREES
REMARK 500 ARG A 245 NE - CZ - NH2 ANGL. DEV. = -3.1 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 57 -61.44 -109.39
REMARK 500 SER A 65 -162.79 -166.85
REMARK 500 SER A 65 -162.79 -168.59
REMARK 500 ASP A 81 -143.35 57.80
REMARK 500 ARG A 111 -0.11 68.59
REMARK 500 PHE A 175 68.23 -151.66
REMARK 500 ASN A 243 38.58 -147.07
REMARK 500 LYS A 251 -132.68 55.47
REMARK 500 ASP A 252 45.79 -94.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 268 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 94 NE2
REMARK 620 2 HIS A 96 NE2 102.0
REMARK 620 3 HIS A 119 ND1 117.1 99.2
REMARK 620 4 HOH A2110 O 103.6 89.7 135.2
REMARK 620 5 HOH A2111 O 89.8 162.4 86.8 74.7
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CNR RELATED DB: PDB
REMARK 900 SURFACE RESIDUE ENGINEERING OF BOVINE CARBONIC ANHYDRASE TO AN
REMARK 900 EXTREME HALOPHILIC ENZYME FOR POTENTIAL APPLICATION IN
REMARK 900 POSTCOMBUSTION CO2 CAPTURE
REMARK 900 RELATED ID: 4CNW RELATED DB: PDB
REMARK 900 SURFACE RESIDUE ENGINEERING OF BOVINE CARBONIC ANHYDRASE TO AN
REMARK 900 EXTREME HALOPHILIC ENZYME FOR POTENTIAL APPLICATION IN
REMARK 900 POSTCOMBUSTION CO2 CAPTURE
REMARK 900 RELATED ID: 4CNX RELATED DB: PDB
REMARK 900 SURFACE RESIDUE ENGINEERING OF BOVINE CARBONIC ANHYDRASE TO AN
REMARK 900 EXTREME HALOPHILIC ENZYME FOR POTENTIAL APPLICATION IN
REMARK 900 POSTCOMBUSTION CO2 CAPTURE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 MUTATED ENZYME
DBREF 4CNV A 1 260 UNP P00921 CAH2_BOVIN 1 260
SEQADV 4CNV MET A -1 UNP P00921 EXPRESSION TAG
SEQADV 4CNV GLY A 0 UNP P00921 EXPRESSION TAG
SEQADV 4CNV ASP A 24 UNP P00921 ASN 24 ENGINEERED MUTATION
SEQADV 4CNV ASP A 39 UNP P00921 VAL 39 ENGINEERED MUTATION
SEQADV 4CNV ASP A 57 UNP P00921 ARG 57 ENGINEERED MUTATION
SEQADV 4CNV GLU A 74 UNP P00921 GLN 74 ENGINEERED MUTATION
SEQADV 4CNV GLU A 169 UNP P00921 LYS 169 ENGINEERED MUTATION
SEQADV 4CNV ASP A 252 UNP P00921 ASN 252 ENGINEERED MUTATION
SEQRES 1 A 262 MET GLY MET SER HIS HIS TRP GLY TYR GLY LYS HIS ASN
SEQRES 2 A 262 GLY PRO GLU HIS TRP HIS LYS ASP PHE PRO ILE ALA ASP
SEQRES 3 A 262 GLY GLU ARG GLN SER PRO VAL ASP ILE ASP THR LYS ALA
SEQRES 4 A 262 VAL ASP GLN ASP PRO ALA LEU LYS PRO LEU ALA LEU VAL
SEQRES 5 A 262 TYR GLY GLU ALA THR SER ASP ARG MET VAL ASN ASN GLY
SEQRES 6 A 262 HIS SER PHE ASN VAL GLU TYR ASP ASP SER GLU ASP LYS
SEQRES 7 A 262 ALA VAL LEU LYS ASP GLY PRO LEU THR GLY THR TYR ARG
SEQRES 8 A 262 LEU VAL GLN PHE HIS PHE HIS TRP GLY SER SER ASP ASP
SEQRES 9 A 262 GLN GLY SER GLU HIS THR VAL ASP ARG LYS LYS TYR ALA
SEQRES 10 A 262 ALA GLU LEU HIS LEU VAL HIS TRP ASN THR LYS TYR GLY
SEQRES 11 A 262 ASP PHE GLY THR ALA ALA GLN GLN PRO ASP GLY LEU ALA
SEQRES 12 A 262 VAL VAL GLY VAL PHE LEU LYS VAL GLY ASP ALA ASN PRO
SEQRES 13 A 262 ALA LEU GLN LYS VAL LEU ASP ALA LEU ASP SER ILE LYS
SEQRES 14 A 262 THR GLU GLY LYS SER THR ASP PHE PRO ASN PHE ASP PRO
SEQRES 15 A 262 GLY SER LEU LEU PRO ASN VAL LEU ASP TYR TRP THR TYR
SEQRES 16 A 262 PRO GLY SER LEU THR THR PRO PRO LEU LEU GLU SER VAL
SEQRES 17 A 262 THR TRP ILE VAL LEU LYS GLU PRO ILE SER VAL SER SER
SEQRES 18 A 262 GLN GLN MET LEU LYS PHE ARG THR LEU ASN PHE ASN ALA
SEQRES 19 A 262 GLU GLY GLU PRO GLU LEU LEU MET LEU ALA ASN TRP ARG
SEQRES 20 A 262 PRO ALA GLN PRO LEU LYS ASP ARG GLN VAL ARG GLY PHE
SEQRES 21 A 262 PRO LYS
HET ZN A 268 1
HET GOL A1001 6
HET GOL A1002 6
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ZN ZN 2+
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 5 HOH *249(H2 O)
HELIX 1 1 GLY A 12 TRP A 16 5 5
HELIX 2 2 PHE A 20 GLY A 25 5 6
HELIX 3 3 ASP A 34 VAL A 38 5 5
HELIX 4 4 LYS A 126 GLY A 128 5 3
HELIX 5 5 ASP A 129 ALA A 134 1 6
HELIX 6 6 ASN A 153 ASP A 161 1 9
HELIX 7 7 ALA A 162 LYS A 167 5 6
HELIX 8 8 ASP A 179 LEU A 184 5 6
HELIX 9 9 SER A 218 ARG A 226 1 9
SHEET 1 AA 2 ASP A 32 ILE A 33 0
SHEET 2 AA 2 THR A 108 VAL A 109 1 O THR A 108 N ILE A 33
SHEET 1 AB 6 LEU A 47 VAL A 50 0
SHEET 2 AB 6 VAL A 78 ASP A 81 -1 O VAL A 78 N VAL A 50
SHEET 3 AB 6 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79
SHEET 4 AB 6 ALA A 116 ASN A 124 -1 O GLU A 117 N HIS A 96
SHEET 5 AB 6 LEU A 140 VAL A 149 -1 O ALA A 141 N HIS A 122
SHEET 6 AB 6 ILE A 215 VAL A 217 1 O ILE A 215 N LYS A 148
SHEET 1 AC 6 LEU A 47 VAL A 50 0
SHEET 2 AC 6 VAL A 78 ASP A 81 -1 O VAL A 78 N VAL A 50
SHEET 3 AC 6 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79
SHEET 4 AC 6 PHE A 66 TYR A 70 -1 O PHE A 66 N PHE A 95
SHEET 5 AC 6 SER A 56 ASN A 61 -1 N ASP A 57 O GLU A 69
SHEET 6 AC 6 SER A 172 ASP A 174 -1 O THR A 173 N MET A 59
SHEET 1 AD 8 LEU A 47 VAL A 50 0
SHEET 2 AD 8 VAL A 78 ASP A 81 -1 O VAL A 78 N VAL A 50
SHEET 3 AD 8 TYR A 88 TRP A 97 -1 O TYR A 88 N LEU A 79
SHEET 4 AD 8 ALA A 116 ASN A 124 -1 O GLU A 117 N HIS A 96
SHEET 5 AD 8 LEU A 140 VAL A 149 -1 O ALA A 141 N HIS A 122
SHEET 6 AD 8 VAL A 206 LEU A 211 1 O THR A 207 N VAL A 142
SHEET 7 AD 8 TYR A 190 GLY A 195 -1 O TRP A 191 N VAL A 210
SHEET 8 AD 8 ARG A 256 PHE A 258 -1 O ARG A 256 N THR A 192
SHEET 1 AE 2 ILE A 215 VAL A 217 0
SHEET 2 AE 2 LEU A 140 VAL A 149 1 O PHE A 146 N ILE A 215
LINK NE2 HIS A 94 ZN ZN A 268 1555 1555 2.11
LINK NE2 HIS A 96 ZN ZN A 268 1555 1555 2.21
LINK ND1 HIS A 119 ZN ZN A 268 1555 1555 2.07
LINK ZN ZN A 268 O HOH A2110 1555 1555 1.92
LINK ZN ZN A 268 O HOH A2111 1555 1555 2.41
CISPEP 1 SER A 29 PRO A 30 0 -5.57
CISPEP 2 PRO A 200 PRO A 201 0 15.43
CISPEP 3 PHE A 258 PRO A 259 0 -1.54
SITE 1 AC1 5 HIS A 94 HIS A 96 HIS A 119 HOH A2110
SITE 2 AC1 5 HOH A2111
SITE 1 AC2 5 ASP A 32 ASP A 34 ASP A 110 ARG A 111
SITE 2 AC2 5 HOH A2249
SITE 1 AC3 2 ASP A 34 LYS A 36
CRYST1 41.757 69.276 44.578 90.00 107.76 90.00 P 1 21 1 2
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 0.023948 0.000000 0.007670 0.00000
SCALE2 0.000000 0.014435 0.000000 0.00000
SCALE3 0.000000 0.000000 0.023555 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
