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HEADER HYDROLASE 31-JAN-19 6JD9
TITLE PROTEUS MIRABILIS LIPASE MUTANT - I118V/E130G
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PROTEUS MIRABILIS;
SOURCE 3 ORGANISM_TAXID: 584;
SOURCE 4 GENE: LIP, AM402_13560, NCTC10975_00950;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS LIPASE, PROTEUS MIRABILIS LIPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR B.S.HEATER,W.S.CHAN,M.K.CHAN
REVDAT 1 24-JUL-19 6JD9 0
JRNL AUTH B.S.HEATER,W.S.CHAN,M.M.LEE,M.K.CHAN
JRNL TITL DIRECTED EVOLUTION OF A GENETICALLY ENCODED IMMOBILIZED
JRNL TITL 2 LIPASE FOR THE EFFICIENT PRODUCTION OF BIODIESEL FROM WASTE
JRNL TITL 3 COOKING OIL.
JRNL REF BIOTECHNOL BIOFUELS V. 12 165 2019
JRNL REFN ESSN 1754-6834
JRNL PMID 31297153
JRNL DOI 10.1186/S13068-019-1509-5
REMARK 2
REMARK 2 RESOLUTION. 1.58 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.58
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.85
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 39488
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) : 0.140
REMARK 3 R VALUE (WORKING SET) : 0.139
REMARK 3 FREE R VALUE : 0.163
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2089
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) : 1.58
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2913
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.1440
REMARK 3 BIN FREE R VALUE SET COUNT : 160
REMARK 3 BIN FREE R VALUE : 0.1920
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2220
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 215
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.064
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.065
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.038
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.025
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2282 ; 0.026 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2160 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3096 ; 2.353 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4947 ; 1.212 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 285 ; 6.178 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 109 ;38.241 ;24.679
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 366 ;12.269 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 10 ;15.135 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 342 ; 0.157 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2644 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 548 ; 0.002 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
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 6JD9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-FEB-19.
REMARK 100 THE DEPOSITION ID IS D_1300010206.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-AUG-18
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 : NSRRC
REMARK 200 BEAMLINE : TPS 05A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : LN2-COOLED, FIXED-EXIT DOUBLE
REMARK 200 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.17
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41629
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.580
REMARK 200 RESOLUTION RANGE LOW (A) : 63.590
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : 0.08200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.58
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.61
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.13000
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7.5, 70% MPD, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 42.39400
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 21.19700
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 TOTAL BURIED SURFACE AREA: 810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
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 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 OD1 ASN A 17 O HOH A 401 2.12
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 TYR A 26 CG TYR A 26 CD1 -0.081
REMARK 500 GLU A 163 CG GLU A 163 CD 0.096
REMARK 500 GLU A 163 CD GLU A 163 OE1 0.091
REMARK 500 TYR A 172 CE1 TYR A 172 CZ -0.125
REMARK 500 GLU A 183 CB GLU A 183 CG -0.116
REMARK 500 GLU A 183 CD GLU A 183 OE2 -0.093
REMARK 500 VAL A 235 CB VAL A 235 CG1 -0.137
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 30 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 PHE A 47 CB - CG - CD1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 GLU A 51 OE1 - CD - OE2 ANGL. DEV. = -7.9 DEGREES
REMARK 500 PHE A 60 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 MET A 219 CG - SD - CE ANGL. DEV. = -25.5 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 LEU A 13 79.00 99.16
REMARK 500 PHE A 47 50.28 -104.19
REMARK 500 SER A 79 -105.32 67.55
REMARK 500 LYS A 208 -120.36 68.71
REMARK 500 ILE A 246 -66.38 -92.16
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 CA A 301 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A 210 OD1
REMARK 620 2 ASP A 213 OD2 93.4
REMARK 620 3 ASP A 256 OD1 85.8 169.4
REMARK 620 4 GLN A 260 O 163.8 90.5 93.3
REMARK 620 5 LEU A 264 O 84.7 90.2 100.2 79.5
REMARK 620 6 HOH A 423 O 93.3 82.3 87.2 102.9 172.2
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MPD A 303
DBREF1 6JD9 A 2 287 UNP A0A1Z1SX23_PROMI
DBREF2 6JD9 A A0A1Z1SX23 2 287
SEQADV 6JD9 VAL A 118 UNP A0A1Z1SX2 ILE 118 ENGINEERED MUTATION
SEQADV 6JD9 GLY A 130 UNP A0A1Z1SX2 GLU 130 ENGINEERED MUTATION
SEQRES 1 A 286 SER THR LYS TYR PRO ILE VAL LEU VAL HIS GLY LEU ALA
SEQRES 2 A 286 GLY PHE ASN GLU ILE VAL GLY PHE PRO TYR PHE TYR GLY
SEQRES 3 A 286 ILE ALA ASP ALA LEU ARG GLN ASP GLY HIS GLN VAL PHE
SEQRES 4 A 286 THR ALA SER LEU SER ALA PHE ASN SER ASN GLU VAL ARG
SEQRES 5 A 286 GLY LYS GLN LEU TRP GLN PHE VAL GLN THR LEU LEU GLN
SEQRES 6 A 286 GLU THR GLN ALA LYS LYS VAL ASN PHE ILE GLY HIS SER
SEQRES 7 A 286 GLN GLY PRO LEU ALA CYS ARG TYR VAL ALA ALA ASN TYR
SEQRES 8 A 286 PRO ASP SER VAL ALA SER VAL THR SER ILE ASN GLY VAL
SEQRES 9 A 286 ASN HIS GLY SER GLU ILE ALA ASP LEU TYR ARG ARG VAL
SEQRES 10 A 286 MET ARG LYS ASP SER ILE PRO GLU TYR ILE VAL GLY LYS
SEQRES 11 A 286 VAL LEU ASN ALA PHE GLY THR ILE ILE SER THR PHE SER
SEQRES 12 A 286 GLY HIS ARG GLY ASP PRO GLN ASP ALA ILE ALA ALA LEU
SEQRES 13 A 286 GLU SER LEU THR THR GLU GLN VAL THR GLU PHE ASN ASN
SEQRES 14 A 286 LYS TYR PRO GLN ALA LEU PRO LYS THR PRO GLY GLY GLU
SEQRES 15 A 286 GLY ASP GLU ILE VAL ASN GLY VAL HIS TYR TYR CYS PHE
SEQRES 16 A 286 GLY SER TYR ILE GLN GLY LEU ILE ALA GLY GLU LYS GLY
SEQRES 17 A 286 ASN LEU LEU ASP PRO THR HIS ALA ALA MET ARG VAL LEU
SEQRES 18 A 286 ASN THR PHE PHE THR GLU LYS GLN ASN ASP GLY LEU VAL
SEQRES 19 A 286 GLY ARG SER SER MET ARG LEU GLY LYS LEU ILE LYS ASP
SEQRES 20 A 286 ASP TYR ALA GLN ASP HIS ILE ASP MET VAL ASN GLN VAL
SEQRES 21 A 286 ALA GLY LEU VAL GLY TYR ASN GLU ASP ILE VAL ALA ILE
SEQRES 22 A 286 TYR THR GLN HIS ALA LYS TYR LEU ALA SER LYS GLN LEU
HET CA A 301 1
HET MPD A 302 8
HET MPD A 303 8
HETNAM CA CALCIUM ION
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
FORMUL 2 CA CA 2+
FORMUL 3 MPD 2(C6 H14 O2)
FORMUL 5 HOH *215(H2 O)
HELIX 1 AA1 GLY A 15 GLY A 21 1 7
HELIX 2 AA2 GLY A 27 ASP A 35 1 9
HELIX 3 AA3 SER A 49 GLN A 69 1 21
HELIX 4 AA4 GLN A 80 TYR A 92 1 13
HELIX 5 AA5 SER A 109 ARG A 120 1 12
HELIX 6 AA6 PRO A 125 GLY A 145 1 21
HELIX 7 AA7 GLN A 151 LEU A 160 5 10
HELIX 8 AA8 THR A 161 TYR A 172 1 12
HELIX 9 AA9 LEU A 203 LEU A 212 5 10
HELIX 10 AB1 ASP A 213 THR A 224 1 12
HELIX 11 AB2 GLY A 236 ARG A 241 5 6
HELIX 12 AB3 ILE A 255 ASN A 259 5 5
HELIX 13 AB4 ASP A 270 LYS A 285 1 16
SHEET 1 AA1 6 VAL A 39 LEU A 44 0
SHEET 2 AA1 6 ILE A 7 GLY A 12 1 N HIS A 11 O LEU A 44
SHEET 3 AA1 6 VAL A 73 HIS A 78 1 O ILE A 76 N VAL A 8
SHEET 4 AA1 6 VAL A 96 ILE A 102 1 O ILE A 102 N GLY A 77
SHEET 5 AA1 6 VAL A 191 SER A 198 1 O PHE A 196 N SER A 101
SHEET 6 AA1 6 ILE A 187 VAL A 188 -1 N VAL A 188 O VAL A 191
SHEET 1 AA2 6 VAL A 39 LEU A 44 0
SHEET 2 AA2 6 ILE A 7 GLY A 12 1 N HIS A 11 O LEU A 44
SHEET 3 AA2 6 VAL A 73 HIS A 78 1 O ILE A 76 N VAL A 8
SHEET 4 AA2 6 VAL A 96 ILE A 102 1 O ILE A 102 N GLY A 77
SHEET 5 AA2 6 VAL A 191 SER A 198 1 O PHE A 196 N SER A 101
SHEET 6 AA2 6 LYS A 244 TYR A 250 1 O ILE A 246 N CYS A 195
LINK OD1 ASN A 210 CA CA A 301 1555 1555 2.35
LINK OD2 ASP A 213 CA CA A 301 1555 1555 2.34
LINK OD1 ASP A 256 CA CA A 301 1555 1555 2.29
LINK O GLN A 260 CA CA A 301 1555 1555 2.39
LINK O LEU A 264 CA CA A 301 1555 1555 2.26
LINK CA CA A 301 O HOH A 423 1555 1555 2.37
CISPEP 1 GLN A 260 VAL A 261 0 4.76
SITE 1 AC1 7 ASN A 210 ASP A 213 ASP A 256 GLN A 260
SITE 2 AC1 7 VAL A 261 LEU A 264 HOH A 423
SITE 1 AC2 4 PHE A 143 ALA A 153 HOH A 538 HOH A 572
SITE 1 AC3 6 SER A 79 GLN A 80 LEU A 234 HIS A 254
SITE 2 AC3 6 ILE A 255 HOH A 461
CRYST1 65.310 65.310 63.591 90.00 90.00 120.00 P 32 3
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 0.015312 0.008840 0.000000 0.00000
SCALE2 0.000000 0.017680 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015725 0.00000
TER 2221 LEU A 287
MASTER 344 0 3 13 12 0 5 6 2452 1 24 22
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