| 7buk-pdb | HEADER HYDROLASE 07-APR-20 7BUK
TITLE T1 LIPASE MUTANT - 5M (D43E/T118N/E226D/E250L/N304E)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 3.1.1.3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GEOBACILLUS ZALIHAE;
SOURCE 3 ORGANISM_TAXID: 213419;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PLYSS
KEYWDS LIPASE, MUTATION, TRIGLYCERIDES, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.N.H.ISHAK,R.N.Z.R.A.RAHMAN,M.S.M.ALI,A.T.C.LEOW,N.H.A.KAMARUDIN
REVDAT 1 07-APR-21 7BUK 0
JRNL AUTH S.N.H.ISHAK,M.S.M.ALI,A.T.C.LEOW,N.H.A.KAMARUDIN,
JRNL AUTH 2 R.N.Z.R.A.RAHMAN
JRNL TITL CRYSTALLIZATION AND STRUCTURE ELUCIDATION OF 5M MUTANT OF T1
JRNL TITL 2 LIPASE GEOBACILLUS ZALIHAE.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0238
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) : 2.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.10
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 3 NUMBER OF REFLECTIONS : 23631
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1188
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) : 2.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.71
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1505
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 78.32
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 77
REMARK 3 BIN FREE R VALUE : 0.4020
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6112
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 183
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.22000
REMARK 3 B22 (A**2) : -1.83000
REMARK 3 B33 (A**2) : 0.36000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.90000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.376
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.241
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.524
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.856
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6280 ; 0.009 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 5564 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8540 ; 1.587 ; 1.642
REMARK 3 BOND ANGLES OTHERS (DEGREES): 12848 ; 1.247 ; 1.573
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 772 ; 7.324 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 366 ;30.584 ;21.148
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 954 ;16.499 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;18.431 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 768 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7230 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1478 ; 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): 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 7BUK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-APR-20.
REMARK 100 THE DEPOSITION ID IS D_1300015947.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-JUN-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : CU
REMARK 200 OPTICS : DEXTRIS 200K
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24822
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.9
REMARK 200 DATA REDUNDANCY : 2.100
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.70
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.12900
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: 2DSN
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.91
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.5 M SODIUM CACODYLATE TRIHYDRATE,
REMARK 280 0.4 M SODIUM CITRATE TRIBASIC PH 6.5, 0.2 M NACL, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 58.79600
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.63450
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 58.79600
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 40.63450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 90 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 578 LIES ON A SPECIAL POSITION.
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 -17
REMARK 465 SER A -16
REMARK 465 PRO A -15
REMARK 465 ILE A -14
REMARK 465 SER A -13
REMARK 465 ARG A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 LEU A -5
REMARK 465 VAL A -4
REMARK 465 PRO A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 ALA A 1
REMARK 465 MET B -17
REMARK 465 SER B -16
REMARK 465 PRO B -15
REMARK 465 ILE B -14
REMARK 465 SER B -13
REMARK 465 ARG B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 LEU B -5
REMARK 465 VAL B -4
REMARK 465 PRO B -3
REMARK 465 ARG B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 ALA B 1
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 NH2 ARG A 92 OD2 ASP A 205 2.05
REMARK 500 NH2 ARG B 92 OD2 ASP B 205 2.19
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 SER A 113 -144.51 64.76
REMARK 500 PHE A 154 8.29 -150.43
REMARK 500 VAL A 203 -59.24 70.38
REMARK 500 LEU A 208 33.24 -99.87
REMARK 500 ARG A 214 136.50 -170.92
REMARK 500 PRO A 217 125.84 -34.28
REMARK 500 ARG A 271 43.02 -145.69
REMARK 500 ASN A 288 131.64 -38.65
REMARK 500 ASP A 310 -148.15 -116.01
REMARK 500 ILE A 319 -40.20 -137.19
REMARK 500 LYS A 329 -56.91 -137.17
REMARK 500 ASN A 367 94.69 -160.29
REMARK 500 LEU B 98 58.97 -147.19
REMARK 500 SER B 113 -137.44 60.61
REMARK 500 ASP B 175 51.67 -108.04
REMARK 500 ALA B 192 -12.20 81.66
REMARK 500 VAL B 203 -70.60 68.60
REMARK 500 ARG B 271 42.63 -148.23
REMARK 500 LEU B 277 -80.21 -70.95
REMARK 500 LEU B 285 128.40 -39.55
REMARK 500 ASP B 310 -156.10 -139.74
REMARK 500 LYS B 329 -53.71 -122.66
REMARK 500 ASN B 367 93.96 -172.68
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 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 61 OD1
REMARK 620 2 ASP A 61 OD2 54.5
REMARK 620 3 HIS A 81 NE2 95.9 150.3
REMARK 620 4 HIS A 87 NE2 115.9 89.3 107.1
REMARK 620 5 ASP A 238 OD2 128.7 102.0 96.6 107.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 286 O
REMARK 620 2 GLU A 360 OE2 84.0
REMARK 620 3 ASP A 365 OD2 99.8 113.0
REMARK 620 4 PRO A 366 O 166.2 95.5 93.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 401 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 61 OD1
REMARK 620 2 HIS B 81 NE2 102.9
REMARK 620 3 HIS B 87 NE2 115.1 103.3
REMARK 620 4 ASP B 238 OD2 132.5 95.4 102.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 286 O
REMARK 620 2 GLU B 360 OE2 81.4
REMARK 620 3 ASP B 365 OD2 110.5 120.0
REMARK 620 4 PRO B 366 O 165.1 96.2 83.5
REMARK 620 N 1 2 3
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 402
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS IS D43E/T118N/E226D/E250L/N304E MUTANT.
REMARK 999 AND 18 N-TERMINAL RESIDUES (MSPISRHHHHHHLVPRGS) ARE EXPRESSION TAGS.
DBREF 7BUK A -17 388 PDB 7BUK 7BUK -17 388
DBREF 7BUK B -17 388 PDB 7BUK 7BUK -17 388
SEQRES 1 A 406 MET SER PRO ILE SER ARG HIS HIS HIS HIS HIS HIS LEU
SEQRES 2 A 406 VAL PRO ARG GLY SER ALA SER LEU ARG ALA ASN ASP ALA
SEQRES 3 A 406 PRO ILE VAL LEU LEU HIS GLY PHE THR GLY TRP GLY ARG
SEQRES 4 A 406 GLU GLU MET PHE GLY PHE LYS TYR TRP GLY GLY VAL ARG
SEQRES 5 A 406 GLY ASP ILE GLU GLN TRP LEU ASN GLU ASN GLY TYR ARG
SEQRES 6 A 406 THR TYR THR LEU ALA VAL GLY PRO LEU SER SER ASN TRP
SEQRES 7 A 406 ASP ARG ALA CYS GLU ALA TYR ALA GLN LEU VAL GLY GLY
SEQRES 8 A 406 THR VAL ASP TYR GLY ALA ALA HIS ALA ALA LYS HIS GLY
SEQRES 9 A 406 HIS ALA ARG PHE GLY ARG THR TYR PRO GLY LEU LEU PRO
SEQRES 10 A 406 GLU LEU LYS ARG GLY GLY ARG ILE HIS ILE ILE ALA HIS
SEQRES 11 A 406 SER GLN GLY GLY GLN ASN ALA ARG MET LEU VAL SER LEU
SEQRES 12 A 406 LEU GLU ASN GLY SER GLN GLU GLU ARG GLU TYR ALA LYS
SEQRES 13 A 406 ALA HIS ASN VAL SER LEU SER PRO LEU PHE GLU GLY GLY
SEQRES 14 A 406 HIS HIS PHE VAL LEU SER VAL THR THR ILE ALA THR PRO
SEQRES 15 A 406 HIS ASP GLY THR THR LEU VAL ASN MET VAL ASP PHE THR
SEQRES 16 A 406 ASP ARG PHE PHE ASP LEU GLN LYS ALA VAL LEU GLU ALA
SEQRES 17 A 406 ALA ALA VAL ALA SER ASN VAL PRO TYR THR SER GLN VAL
SEQRES 18 A 406 TYR ASP PHE LYS LEU ASP GLN TRP GLY LEU ARG ARG GLN
SEQRES 19 A 406 PRO GLY GLU SER PHE ASP HIS TYR PHE ASP ARG LEU LYS
SEQRES 20 A 406 ARG SER PRO VAL TRP THR SER THR ASP THR ALA ARG TYR
SEQRES 21 A 406 ASP LEU SER VAL SER GLY ALA LEU LYS LEU ASN GLN TRP
SEQRES 22 A 406 VAL GLN ALA SER PRO ASN THR TYR TYR LEU SER PHE SER
SEQRES 23 A 406 THR GLU ARG THR TYR ARG GLY ALA LEU THR GLY ASN HIS
SEQRES 24 A 406 TYR PRO GLU LEU GLY MET ASN ALA PHE SER ALA VAL VAL
SEQRES 25 A 406 CYS ALA PRO PHE LEU GLY SER TYR ARG GLU PRO THR LEU
SEQRES 26 A 406 GLY ILE ASP ASP ARG TRP LEU GLU ASN ASP GLY ILE VAL
SEQRES 27 A 406 ASN THR VAL SER MET ASN GLY PRO LYS ARG GLY SER SER
SEQRES 28 A 406 ASP ARG ILE VAL PRO TYR ASP GLY THR LEU LYS LYS GLY
SEQRES 29 A 406 VAL TRP ASN ASP MET GLY THR TYR ASN VAL ASP HIS LEU
SEQRES 30 A 406 GLU ILE ILE GLY VAL ASP PRO ASN PRO SER PHE ASP ILE
SEQRES 31 A 406 ARG ALA PHE TYR LEU ARG LEU ALA GLU GLN LEU ALA SER
SEQRES 32 A 406 LEU ARG PRO
SEQRES 1 B 406 MET SER PRO ILE SER ARG HIS HIS HIS HIS HIS HIS LEU
SEQRES 2 B 406 VAL PRO ARG GLY SER ALA SER LEU ARG ALA ASN ASP ALA
SEQRES 3 B 406 PRO ILE VAL LEU LEU HIS GLY PHE THR GLY TRP GLY ARG
SEQRES 4 B 406 GLU GLU MET PHE GLY PHE LYS TYR TRP GLY GLY VAL ARG
SEQRES 5 B 406 GLY ASP ILE GLU GLN TRP LEU ASN GLU ASN GLY TYR ARG
SEQRES 6 B 406 THR TYR THR LEU ALA VAL GLY PRO LEU SER SER ASN TRP
SEQRES 7 B 406 ASP ARG ALA CYS GLU ALA TYR ALA GLN LEU VAL GLY GLY
SEQRES 8 B 406 THR VAL ASP TYR GLY ALA ALA HIS ALA ALA LYS HIS GLY
SEQRES 9 B 406 HIS ALA ARG PHE GLY ARG THR TYR PRO GLY LEU LEU PRO
SEQRES 10 B 406 GLU LEU LYS ARG GLY GLY ARG ILE HIS ILE ILE ALA HIS
SEQRES 11 B 406 SER GLN GLY GLY GLN ASN ALA ARG MET LEU VAL SER LEU
SEQRES 12 B 406 LEU GLU ASN GLY SER GLN GLU GLU ARG GLU TYR ALA LYS
SEQRES 13 B 406 ALA HIS ASN VAL SER LEU SER PRO LEU PHE GLU GLY GLY
SEQRES 14 B 406 HIS HIS PHE VAL LEU SER VAL THR THR ILE ALA THR PRO
SEQRES 15 B 406 HIS ASP GLY THR THR LEU VAL ASN MET VAL ASP PHE THR
SEQRES 16 B 406 ASP ARG PHE PHE ASP LEU GLN LYS ALA VAL LEU GLU ALA
SEQRES 17 B 406 ALA ALA VAL ALA SER ASN VAL PRO TYR THR SER GLN VAL
SEQRES 18 B 406 TYR ASP PHE LYS LEU ASP GLN TRP GLY LEU ARG ARG GLN
SEQRES 19 B 406 PRO GLY GLU SER PHE ASP HIS TYR PHE ASP ARG LEU LYS
SEQRES 20 B 406 ARG SER PRO VAL TRP THR SER THR ASP THR ALA ARG TYR
SEQRES 21 B 406 ASP LEU SER VAL SER GLY ALA LEU LYS LEU ASN GLN TRP
SEQRES 22 B 406 VAL GLN ALA SER PRO ASN THR TYR TYR LEU SER PHE SER
SEQRES 23 B 406 THR GLU ARG THR TYR ARG GLY ALA LEU THR GLY ASN HIS
SEQRES 24 B 406 TYR PRO GLU LEU GLY MET ASN ALA PHE SER ALA VAL VAL
SEQRES 25 B 406 CYS ALA PRO PHE LEU GLY SER TYR ARG GLU PRO THR LEU
SEQRES 26 B 406 GLY ILE ASP ASP ARG TRP LEU GLU ASN ASP GLY ILE VAL
SEQRES 27 B 406 ASN THR VAL SER MET ASN GLY PRO LYS ARG GLY SER SER
SEQRES 28 B 406 ASP ARG ILE VAL PRO TYR ASP GLY THR LEU LYS LYS GLY
SEQRES 29 B 406 VAL TRP ASN ASP MET GLY THR TYR ASN VAL ASP HIS LEU
SEQRES 30 B 406 GLU ILE ILE GLY VAL ASP PRO ASN PRO SER PHE ASP ILE
SEQRES 31 B 406 ARG ALA PHE TYR LEU ARG LEU ALA GLU GLN LEU ALA SER
SEQRES 32 B 406 LEU ARG PRO
HET ZN A 401 1
HET CA A 402 1
HET ZN B 401 1
HET CA B 402 1
HETNAM ZN ZINC ION
HETNAM CA CALCIUM ION
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 CA 2(CA 2+)
FORMUL 7 HOH *183(H2 O)
HELIX 1 AA1 GLU A 23 PHE A 27 5 5
HELIX 2 AA2 GLY A 31 GLY A 35 5 5
HELIX 3 AA3 ASP A 36 ASN A 44 1 9
HELIX 4 AA4 SER A 58 GLY A 72 1 15
HELIX 5 AA5 GLY A 78 GLY A 86 1 9
HELIX 6 AA6 LEU A 98 GLY A 104 5 7
HELIX 7 AA7 GLN A 114 GLY A 129 1 16
HELIX 8 AA8 SER A 130 HIS A 140 1 11
HELIX 9 AA9 SER A 145 GLU A 149 5 5
HELIX 10 AB1 THR A 168 MET A 173 5 6
HELIX 11 AB2 ASP A 175 ALA A 191 1 17
HELIX 12 AB3 LEU A 208 GLY A 212 5 5
HELIX 13 AB4 SER A 220 ARG A 230 1 11
HELIX 14 AB5 SER A 231 SER A 236 1 6
HELIX 15 AB6 THR A 239 SER A 245 1 7
HELIX 16 AB7 SER A 245 GLN A 254 1 10
HELIX 17 AB8 ASN A 288 CYS A 295 1 8
HELIX 18 AB9 CYS A 295 GLY A 300 1 6
HELIX 19 AC1 GLU A 304 GLY A 308 5 5
HELIX 20 AC2 ASP A 310 LEU A 314 5 5
HELIX 21 AC3 ASN A 321 ASN A 326 5 6
HELIX 22 AC4 ASP A 371 SER A 385 1 15
HELIX 23 AC5 GLU B 23 PHE B 27 5 5
HELIX 24 AC6 GLY B 31 GLY B 35 5 5
HELIX 25 AC7 ASP B 36 ASN B 44 1 9
HELIX 26 AC8 SER B 58 GLY B 72 1 15
HELIX 27 AC9 GLY B 78 GLY B 86 1 9
HELIX 28 AD1 LEU B 98 LYS B 102 5 5
HELIX 29 AD2 GLN B 114 GLY B 129 1 16
HELIX 30 AD3 SER B 130 ASN B 141 1 12
HELIX 31 AD4 SER B 145 GLU B 149 5 5
HELIX 32 AD5 THR B 168 MET B 173 5 6
HELIX 33 AD6 ASP B 175 ALA B 190 1 16
HELIX 34 AD7 LEU B 208 GLY B 212 5 5
HELIX 35 AD8 SER B 220 LYS B 229 1 10
HELIX 36 AD9 SER B 231 SER B 236 1 6
HELIX 37 AE1 THR B 239 SER B 245 1 7
HELIX 38 AE2 SER B 245 GLN B 254 1 10
HELIX 39 AE3 ASN B 288 CYS B 295 1 8
HELIX 40 AE4 CYS B 295 GLY B 300 1 6
HELIX 41 AE5 GLU B 304 GLY B 308 5 5
HELIX 42 AE6 ASP B 310 LEU B 314 5 5
HELIX 43 AE7 ASN B 321 ASN B 326 5 6
HELIX 44 AE8 ASP B 371 SER B 385 1 15
SHEET 1 AA1 7 THR A 48 LEU A 51 0
SHEET 2 AA1 7 ILE A 10 LEU A 13 1 N LEU A 12 O LEU A 51
SHEET 3 AA1 7 ILE A 107 HIS A 112 1 O HIS A 108 N VAL A 11
SHEET 4 AA1 7 VAL A 155 ILE A 161 1 O THR A 159 N ALA A 111
SHEET 5 AA1 7 TYR A 263 GLU A 270 1 O TYR A 263 N VAL A 158
SHEET 6 AA1 7 TRP A 348 ASN A 355 1 O MET A 351 N SER A 266
SHEET 7 AA1 7 ILE A 336 PRO A 338 1 N VAL A 337 O TRP A 348
SHEET 1 AA2 2 GLY A 73 ASP A 76 0
SHEET 2 AA2 2 PHE A 90 TYR A 94 -1 O ARG A 92 N VAL A 75
SHEET 1 AA3 2 THR A 272 ARG A 274 0
SHEET 2 AA3 2 HIS A 281 PRO A 283 -1 O TYR A 282 N TYR A 273
SHEET 1 AA4 7 THR B 48 LEU B 51 0
SHEET 2 AA4 7 ILE B 10 LEU B 13 1 N LEU B 12 O LEU B 51
SHEET 3 AA4 7 ILE B 107 HIS B 112 1 O HIS B 108 N VAL B 11
SHEET 4 AA4 7 VAL B 155 ILE B 161 1 O SER B 157 N ILE B 109
SHEET 5 AA4 7 TYR B 263 THR B 269 1 O PHE B 267 N THR B 160
SHEET 6 AA4 7 TRP B 348 TYR B 354 1 O TYR B 354 N SER B 268
SHEET 7 AA4 7 ILE B 336 PRO B 338 1 N VAL B 337 O TRP B 348
SHEET 1 AA5 2 GLY B 73 ASP B 76 0
SHEET 2 AA5 2 PHE B 90 TYR B 94 -1 O ARG B 92 N VAL B 75
SHEET 1 AA6 2 THR B 272 ARG B 274 0
SHEET 2 AA6 2 HIS B 281 PRO B 283 -1 O TYR B 282 N TYR B 273
LINK OD1 ASP A 61 ZN ZN A 401 1555 1555 2.08
LINK OD2 ASP A 61 ZN ZN A 401 1555 1555 2.65
LINK NE2 HIS A 81 ZN ZN A 401 1555 1555 2.43
LINK NE2 HIS A 87 ZN ZN A 401 1555 1555 2.15
LINK OD2 ASP A 238 ZN ZN A 401 1555 1555 1.98
LINK O GLY A 286 CA CA A 402 1555 1555 2.18
LINK OE2 GLU A 360 CA CA A 402 1555 1555 2.37
LINK OD2 ASP A 365 CA CA A 402 1555 1555 2.58
LINK O PRO A 366 CA CA A 402 1555 1555 2.46
LINK OD1 ASP B 61 ZN ZN B 401 1555 1555 2.06
LINK NE2 HIS B 81 ZN ZN B 401 1555 1555 2.07
LINK NE2 HIS B 87 ZN ZN B 401 1555 1555 2.17
LINK OD2 ASP B 238 ZN ZN B 401 1555 1555 1.94
LINK O GLY B 286 CA CA B 402 1555 1555 2.35
LINK OE2 GLU B 360 CA CA B 402 1555 1555 2.30
LINK OD2 ASP B 365 CA CA B 402 1555 1555 2.42
LINK O PRO B 366 CA CA B 402 1555 1555 2.36
SITE 1 AC1 4 ASP A 61 HIS A 81 HIS A 87 ASP A 238
SITE 1 AC2 4 GLY A 286 GLU A 360 ASP A 365 PRO A 366
SITE 1 AC3 5 SER B 58 ASP B 61 HIS B 81 HIS B 87
SITE 2 AC3 5 ASP B 238
SITE 1 AC4 4 GLY B 286 GLU B 360 ASP B 365 PRO B 366
CRYST1 117.592 81.269 99.522 90.00 97.32 90.00 C 1 2 1 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 0.008504 0.000000 0.001092 0.00000
SCALE2 0.000000 0.012305 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010131 0.00000
TER 3057 PRO A 388
TER 6114 PRO B 388
MASTER 418 0 4 44 22 0 5 6 6299 2 22 64
END
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