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HEADER HYDROLASE 07-MAR-11 3QZU
TITLE CRYSTAL STRUCTURE OF BACILLUS SUBTILIS LIPASE A 7-FOLD MUTANT; THE
TITLE 2 OUTCOME OF DIRECTED EVOLUTION TOWARDS THERMOSTABILITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPASE ESTA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: LIPASE A, TRIACYLGLYCEROL LIPASE;
COMPND 5 EC: 3.1.1.3;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS SUBSP. SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: BSU02700, ESTA, LIP, LIPA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) RP;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS ALPHA/BETA HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.PIJNING,W.AUGUSTYNIAK,M.T.REETZ,B.W.DIJKSTRA
REVDAT 1 08-FEB-12 3QZU 0
JRNL AUTH W.AUGUSTYNIAK,A.A.BRZEZINSKA,T.PIJNING,H.WIENK,R.BOELENS,
JRNL AUTH 2 B.W.DIJKSTRA,M.T.REETZ
JRNL TITL BIOPHYSICAL CHARACTERIZATION OF MUTANTS OF BACILLUS SUBTILIS
JRNL TITL 2 LIPASE EVOLVED FOR THERMOSTABILITY: FACTORS CONTRIBUTING TO
JRNL TITL 3 INCREASED ACTIVITY RETENTION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.16
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 32229
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) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1700
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) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2444
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 121
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2700
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 42
REMARK 3 SOLVENT ATOMS : 482
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.60000
REMARK 3 B22 (A**2) : 0.15000
REMARK 3 B33 (A**2) : 0.59000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.083
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.725
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.907
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2805 ; 0.011 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3804 ; 1.107 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 367 ; 5.851 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 124 ;33.835 ;25.645
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 442 ;10.420 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;10.000 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 421 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2132 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1779 ; 0.621 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2843 ; 1.145 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1026 ; 1.967 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 958 ; 3.238 ; 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 2 A 181 5
REMARK 3 1 B 2 B 181 5
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 712 ; 0.07 ; 0.50
REMARK 3 LOOSE POSITIONAL 1 A (A): 627 ; 0.21 ; 5.00
REMARK 3 MEDIUM THERMAL 1 A (A**2): 712 ; 2.05 ; 2.00
REMARK 3 LOOSE THERMAL 1 A (A**2): 627 ; 2.09 ; 10.00
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 : 1.40
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
REMARK 4
REMARK 4 3QZU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064311.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8726
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43134
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.710
REMARK 200 RESOLUTION RANGE LOW (A) : 45.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.15900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.71
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.81
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.30
REMARK 200 R MERGE FOR SHELL (I) : 0.82200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1I6W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.78
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% (W/V) PEG 3350, 0.2 M (NH4)2)SO4,
REMARK 280 0.1 M BISTRIS-HCL, 0.03 M BES-NAOH, 0.03% (W/V) NAN3, PH 6.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 22.75550
REMARK 290 SMTRY3 2 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 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 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 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 ALA A 1
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 O HOH A 267 O HOH A 388 2.07
REMARK 500 O HOH A 374 O HOH B 188 2.13
REMARK 500 O HOH A 302 O HOH A 380 2.14
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 77 -123.16 61.38
REMARK 500 LEU A 90 -141.08 -111.36
REMARK 500 ALA A 97 -63.08 -108.21
REMARK 500 ALA A 113 91.65 -69.33
REMARK 500 THR A 180 47.97 -95.99
REMARK 500 SER B 77 -120.19 56.18
REMARK 500 LEU B 90 -144.85 -114.60
REMARK 500 ALA B 97 -69.67 -102.69
REMARK 500 ASN B 179 85.78 -155.33
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH B 432 DISTANCE = 6.45 ANGSTROMS
REMARK 525 HOH B 447 DISTANCE = 7.08 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 184
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 185
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 186
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 182
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 183
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 184
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 185
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1I6W RELATED DB: PDB
REMARK 900 WILD TYPE PROTEIN.
DBREF 3QZU A 1 181 UNP P37957 ESTA_BACSU 32 212
DBREF 3QZU B 1 181 UNP P37957 ESTA_BACSU 32 212
SEQADV 3QZU GLN A 33 UNP P37957 ARG 64 ENGINEERED MUTATION
SEQADV 3QZU ASN A 34 UNP P37957 ASP 65 ENGINEERED MUTATION
SEQADV 3QZU ASP A 35 UNP P37957 LYS 66 ENGINEERED MUTATION
SEQADV 3QZU ASP A 112 UNP P37957 LYS 143 ENGINEERED MUTATION
SEQADV 3QZU ASP A 134 UNP P37957 MET 165 ENGINEERED MUTATION
SEQADV 3QZU CYS A 139 UNP P37957 TYR 170 ENGINEERED MUTATION
SEQADV 3QZU MET A 157 UNP P37957 ILE 188 ENGINEERED MUTATION
SEQADV 3QZU GLN B 33 UNP P37957 ARG 64 ENGINEERED MUTATION
SEQADV 3QZU ASN B 34 UNP P37957 ASP 65 ENGINEERED MUTATION
SEQADV 3QZU ASP B 35 UNP P37957 LYS 66 ENGINEERED MUTATION
SEQADV 3QZU ASP B 112 UNP P37957 LYS 143 ENGINEERED MUTATION
SEQADV 3QZU ASP B 134 UNP P37957 MET 165 ENGINEERED MUTATION
SEQADV 3QZU CYS B 139 UNP P37957 TYR 170 ENGINEERED MUTATION
SEQADV 3QZU MET B 157 UNP P37957 ILE 188 ENGINEERED MUTATION
SEQRES 1 A 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 A 181 GLY ALA SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU
SEQRES 3 A 181 VAL SER GLN GLY TRP SER GLN ASN ASP LEU TYR ALA VAL
SEQRES 4 A 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 A 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 A 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 A 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP
SEQRES 8 A 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 A 181 ALA ASN ARG LEU THR THR GLY ASP ALA LEU PRO GLY THR
SEQRES 10 A 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 A 181 SER ALA ASP ASP ILE VAL MET ASN CYS LEU SER ARG LEU
SEQRES 12 A 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 A 181 MET GLY LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE
SEQRES 14 A 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
SEQRES 1 B 181 ALA GLU HIS ASN PRO VAL VAL MET VAL HIS GLY ILE GLY
SEQRES 2 B 181 GLY ALA SER PHE ASN PHE ALA GLY ILE LYS SER TYR LEU
SEQRES 3 B 181 VAL SER GLN GLY TRP SER GLN ASN ASP LEU TYR ALA VAL
SEQRES 4 B 181 ASP PHE TRP ASP LYS THR GLY THR ASN TYR ASN ASN GLY
SEQRES 5 B 181 PRO VAL LEU SER ARG PHE VAL GLN LYS VAL LEU ASP GLU
SEQRES 6 B 181 THR GLY ALA LYS LYS VAL ASP ILE VAL ALA HIS SER MET
SEQRES 7 B 181 GLY GLY ALA ASN THR LEU TYR TYR ILE LYS ASN LEU ASP
SEQRES 8 B 181 GLY GLY ASN LYS VAL ALA ASN VAL VAL THR LEU GLY GLY
SEQRES 9 B 181 ALA ASN ARG LEU THR THR GLY ASP ALA LEU PRO GLY THR
SEQRES 10 B 181 ASP PRO ASN GLN LYS ILE LEU TYR THR SER ILE TYR SER
SEQRES 11 B 181 SER ALA ASP ASP ILE VAL MET ASN CYS LEU SER ARG LEU
SEQRES 12 B 181 ASP GLY ALA ARG ASN VAL GLN ILE HIS GLY VAL GLY HIS
SEQRES 13 B 181 MET GLY LEU LEU TYR SER SER GLN VAL ASN SER LEU ILE
SEQRES 14 B 181 LYS GLU GLY LEU ASN GLY GLY GLY GLN ASN THR ASN
HET CL A 182 1
HET SO4 A 183 5
HET GOL A 184 6
HET GOL A 185 6
HET GOL A 186 6
HET CL B 182 1
HET SO4 B 183 5
HET GOL B 184 6
HET GOL B 185 6
HETNAM CL CHLORIDE ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 CL 2(CL 1-)
FORMUL 4 SO4 2(O4 S 2-)
FORMUL 5 GOL 5(C3 H8 O3)
FORMUL 12 HOH *482(H2 O)
HELIX 1 1 ALA A 15 ASN A 18 5 4
HELIX 2 2 PHE A 19 GLN A 29 1 11
HELIX 3 3 SER A 32 ASN A 34 5 3
HELIX 4 4 THR A 47 GLY A 67 1 21
HELIX 5 5 MET A 78 LEU A 90 1 13
HELIX 6 6 ASP A 91 ASN A 94 5 4
HELIX 7 7 ALA A 105 THR A 109 5 5
HELIX 8 8 MET A 137 ARG A 142 1 6
HELIX 9 9 HIS A 156 TYR A 161 5 6
HELIX 10 10 SER A 162 ASN A 174 1 13
HELIX 11 11 ALA B 15 ASN B 18 5 4
HELIX 12 12 PHE B 19 GLN B 29 1 11
HELIX 13 13 SER B 32 ASN B 34 5 3
HELIX 14 14 THR B 47 GLY B 67 1 21
HELIX 15 15 MET B 78 LEU B 90 1 13
HELIX 16 16 ASP B 91 ASN B 94 5 4
HELIX 17 17 ALA B 105 THR B 109 5 5
HELIX 18 18 MET B 137 ARG B 142 1 6
HELIX 19 19 HIS B 156 TYR B 161 5 6
HELIX 20 20 SER B 162 ASN B 174 1 13
SHEET 1 A 6 LEU A 36 ALA A 38 0
SHEET 2 A 6 VAL A 6 VAL A 9 1 N VAL A 6 O TYR A 37
SHEET 3 A 6 VAL A 71 HIS A 76 1 O ASP A 72 N VAL A 7
SHEET 4 A 6 VAL A 96 LEU A 102 1 O VAL A 100 N ILE A 73
SHEET 5 A 6 LEU A 124 SER A 130 1 O LEU A 124 N VAL A 99
SHEET 6 A 6 ARG A 147 ILE A 151 1 O VAL A 149 N SER A 127
SHEET 1 B 6 LEU B 36 ALA B 38 0
SHEET 2 B 6 VAL B 6 VAL B 9 1 N VAL B 6 O TYR B 37
SHEET 3 B 6 VAL B 71 HIS B 76 1 O ASP B 72 N VAL B 7
SHEET 4 B 6 VAL B 96 LEU B 102 1 O LEU B 102 N ALA B 75
SHEET 5 B 6 LEU B 124 SER B 130 1 O LEU B 124 N VAL B 99
SHEET 6 B 6 ARG B 147 ILE B 151 1 O VAL B 149 N SER B 127
SSBOND 1 CYS A 139 CYS B 139 1555 1555 2.84
SITE 1 AC1 4 ILE A 12 SER A 77 MET A 78 HOH A 272
SITE 1 AC2 5 TRP A 42 VAL A 54 ARG A 57 HOH A 246
SITE 2 AC2 5 HOH A 360
SITE 1 AC3 6 MET A 137 ASN A 138 CYS A 139 ARG A 142
SITE 2 AC3 6 ARG B 107 HOH B 264
SITE 1 AC4 4 ARG A 107 ASP A 144 ARG B 142 HOH B 309
SITE 1 AC5 5 SER A 162 SER A 163 GLN A 164 HOH A 201
SITE 2 AC5 5 HOH A 477
SITE 1 AC6 4 ILE B 12 SER B 77 MET B 78 HOH B 314
SITE 1 AC7 3 TRP B 42 ARG B 57 HOH B 240
SITE 1 AC8 4 SER B 162 SER B 163 GLN B 164 HOH B 371
SITE 1 AC9 2 ILE B 135 HOH B 209
CRYST1 59.163 45.511 77.613 90.00 101.10 90.00 P 1 21 1 4
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 0.016902 0.000000 0.003316 0.00000
SCALE2 0.000000 0.021973 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013130 0.00000
TER 1368 ASN A 181
TER 2722 ASN B 181
MASTER 346 0 9 20 12 0 12 6 3224 2 42 28
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