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HEADER HYDROLASE 08-OCT-24 9JUX
TITLE CRYSTAL STRUCTURE OF HYPERTHERMOSTABLE CARBOXYLESTERASE FROM
TITLE 2 ANOXYBACILLUS GEOTHERMALIS D9
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CARBOXYLESTERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 3.1.1.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANOXYBACTEROIDES RUPIENSE;
SOURCE 3 ORGANISM_TAXID: 311460;
SOURCE 4 GENE: EST, GFC29_2339;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET51B(+)
KEYWDS CARBOXYLESTERASE, ANOXYBACILLUS, THERMOSTABLE ENZYME, HYPER-
KEYWDS 2 THERMOPHILIC, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.F.Y.A.RAHMAN,U.U.M.JOHAN,R.N.Z.R.A.RAHMAN,N.D.M.NOOR,F.M.SHARIFF,
AUTHOR 2 M.S.M.ALI
REVDAT 1 15-OCT-25 9JUX 0
JRNL AUTH N.F.Y.A.RAHMAN,U.U.M.JOHAN,R.N.Z.R.A.RAHMAN,N.D.M.NOOR,
JRNL AUTH 2 F.M.SHARIFF,M.S.M.ALI
JRNL TITL CRYSTAL STRUCTURE OF CARBOXYLESTERASE FROM BACILLUS D9
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.67 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0430 (REFMACAT 0.4.100)
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.67
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 88429
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.036
REMARK 3 FREE R VALUE TEST SET COUNT : 4453
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) : 1.67
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.71
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5995
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.3080
REMARK 3 BIN FREE R VALUE SET COUNT : 334
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5841
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 207
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.79
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.09600
REMARK 3 B22 (A**2) : -2.16200
REMARK 3 B33 (A**2) : 2.25800
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): 0.129
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.103
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.084
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.842
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.953
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5991 ; 0.014 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 8109 ; 2.252 ; 1.842
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 723 ; 5.999 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 27 ;10.557 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1053 ;13.025 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 864 ; 0.144 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4593 ; 0.012 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2678 ; 0.211 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4162 ; 0.317 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 258 ; 0.106 ; 0.200
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): 2901 ; 5.585 ; 1.743
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3621 ; 7.436 ; 3.136
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3090 ; 8.431 ; 2.064
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4488 ;11.261 ; 3.665
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): 5991 ; 7.482 ; 3.000
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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 5 A 246
REMARK 3 ORIGIN FOR THE GROUP (A): 2.6909 11.6534 27.8688
REMARK 3 T TENSOR
REMARK 3 T11: 0.0552 T22: 0.1137
REMARK 3 T33: 0.0211 T12: -0.0238
REMARK 3 T13: -0.0078 T23: -0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 1.6690 L22: 1.4439
REMARK 3 L33: 1.2801 L12: -0.2997
REMARK 3 L13: -0.0073 L23: 0.2370
REMARK 3 S TENSOR
REMARK 3 S11: -0.0596 S12: -0.0324 S13: 0.0987
REMARK 3 S21: 0.0252 S22: 0.0052 S23: 0.1213
REMARK 3 S31: 0.0010 S32: -0.1339 S33: 0.0544
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 5 B 246
REMARK 3 ORIGIN FOR THE GROUP (A): 7.1676 -15.1011 53.1542
REMARK 3 T TENSOR
REMARK 3 T11: 0.0464 T22: 0.0992
REMARK 3 T33: 0.0115 T12: 0.0003
REMARK 3 T13: -0.0024 T23: -0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 1.6668 L22: 1.4251
REMARK 3 L33: 1.4438 L12: 0.1836
REMARK 3 L13: 0.0065 L23: -0.2030
REMARK 3 S TENSOR
REMARK 3 S11: 0.0158 S12: 0.0414 S13: -0.0839
REMARK 3 S21: -0.0426 S22: -0.0182 S23: -0.1066
REMARK 3 S31: 0.0438 S32: 0.0715 S33: 0.0024
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 5 C 246
REMARK 3 ORIGIN FOR THE GROUP (A): -10.9567 13.9204 68.5912
REMARK 3 T TENSOR
REMARK 3 T11: 0.0665 T22: 0.1231
REMARK 3 T33: 0.0601 T12: 0.0019
REMARK 3 T13: 0.0326 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 1.8243 L22: 1.5979
REMARK 3 L33: 1.1982 L12: 0.0735
REMARK 3 L13: 0.2837 L23: 0.0838
REMARK 3 S TENSOR
REMARK 3 S11: 0.0076 S12: -0.0233 S13: 0.1548
REMARK 3 S21: -0.0512 S22: -0.0301 S23: -0.1309
REMARK 3 S31: -0.0301 S32: 0.0622 S33: 0.0225
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
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 NOT BEEN USED
REMARK 4
REMARK 4 9JUX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-OCT-24.
REMARK 100 THE DEPOSITION ID IS D_1300052108.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-23
REMARK 200 TEMPERATURE (KELVIN) : 293.15
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 88855
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.667
REMARK 200 RESOLUTION RANGE LOW (A) : 47.480
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 2.000
REMARK 200 R MERGE (I) : 0.01900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.67
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 47.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
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 : 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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM ACETATE TRIHYDRATE, 0.1M
REMARK 280 SODIUM CACODYLATE TRIHYDRATE PH6.5, 30% W/V POLYETHYLENE GLYCOL
REMARK 280 8,000, COUNTER-DIFFUSION, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 29.48500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 57.44250
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.81400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 57.44250
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.48500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.81400
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, 3
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 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 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 231 CD GLU A 231 OE1 0.071
REMARK 500 GLU B 172 CD GLU B 172 OE2 0.140
REMARK 500 GLU C 231 CD GLU C 231 OE1 0.066
REMARK 500 GLU C 235 CD GLU C 235 OE2 0.100
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 MET A 73 CG - SD - CE ANGL. DEV. = 14.7 DEGREES
REMARK 500 ARG A 80 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 MET A 126 CG - SD - CE ANGL. DEV. = -12.2 DEGREES
REMARK 500 ARG A 174 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 156 CB - CG - CD ANGL. DEV. = 17.6 DEGREES
REMARK 500 ARG B 156 CG - CD - NE ANGL. DEV. = -15.6 DEGREES
REMARK 500 ARG B 156 CD - NE - CZ ANGL. DEV. = 9.2 DEGREES
REMARK 500 MET B 160 CG - SD - CE ANGL. DEV. = -10.4 DEGREES
REMARK 500 GLU B 172 CG - CD - OE1 ANGL. DEV. = -12.5 DEGREES
REMARK 500 GLU B 172 CG - CD - OE2 ANGL. DEV. = 12.6 DEGREES
REMARK 500 ARG B 174 NE - CZ - NH1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG B 174 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 ARG C 16 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 36 NE - CZ - NH1 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LYS C 121 CB - CG - CD ANGL. DEV. = 15.6 DEGREES
REMARK 500 ARG C 156 NE - CZ - NH2 ANGL. DEV. = 3.5 DEGREES
REMARK 500 MET C 160 CG - SD - CE ANGL. DEV. = -12.9 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 ALA A 13 -110.98 -128.47
REMARK 500 THR A 25 -4.83 78.31
REMARK 500 SER A 93 -120.72 62.44
REMARK 500 ALA B 13 -120.05 -134.21
REMARK 500 THR B 25 -8.52 75.34
REMARK 500 SER B 93 -117.55 66.77
REMARK 500 LYS B 157 -31.85 69.74
REMARK 500 HIS B 191 69.94 -106.33
REMARK 500 ALA C 13 -107.07 -130.35
REMARK 500 SER C 93 -114.02 58.42
REMARK 500 SER C 122 146.84 -173.45
REMARK 500 LYS C 157 -28.45 79.87
REMARK 500 HIS C 191 56.44 -105.98
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG B 80 0.07 SIDE CHAIN
REMARK 500 ARG B 156 0.12 SIDE CHAIN
REMARK 500 ARG C 156 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 9JUX A 5 246 UNP A0A160FBT3_9BACI
DBREF2 9JUX A A0A160FBT3 5 246
DBREF1 9JUX B 5 246 UNP A0A160FBT3_9BACI
DBREF2 9JUX B A0A160FBT3 5 246
DBREF1 9JUX C 5 246 UNP A0A160FBT3_9BACI
DBREF2 9JUX C A0A160FBT3 5 246
SEQRES 1 A 242 SER PRO LYS PRO PHE THR PHE GLU ALA GLY GLU ARG ALA
SEQRES 2 A 242 VAL LEU LEU LEU HIS GLY PHE THR GLY ASN SER SER ASP
SEQRES 3 A 242 VAL ARG MET LEU GLY ARG PHE LEU GLU SER LYS GLY TYR
SEQRES 4 A 242 THR CYS HIS ALA PRO ILE TYR LYS GLY HIS GLY VAL PRO
SEQRES 5 A 242 PRO GLU GLU LEU VAL HIS THR GLY PRO ASP ASP TRP TRP
SEQRES 6 A 242 GLN ASP VAL MET ASN ALA TYR GLU PHE LEU ARG GLU LYS
SEQRES 7 A 242 GLY TYR GLN LYS ILE ALA VAL VAL GLY LEU SER LEU GLY
SEQRES 8 A 242 GLY VAL PHE SER LEU LYS LEU GLY TYR THR VAL PRO VAL
SEQRES 9 A 242 VAL GLY ILE VAL PRO MET CYS ALA PRO MET TYR ILE LYS
SEQRES 10 A 242 SER GLU GLU THR MET TYR GLN GLY VAL LEU ASP TYR ALA
SEQRES 11 A 242 ARG GLU TYR LYS LYS ARG GLU GLY LYS ALA PRO GLU GLN
SEQRES 12 A 242 ILE GLU LYS GLU MET GLU GLU PHE ARG LYS THR PRO MET
SEQRES 13 A 242 LYS THR LEU LYS ALA LEU GLN ALA LEU ILE ALA GLU VAL
SEQRES 14 A 242 ARG ASN HIS ILE ASP LEU ILE TYR ALA PRO THR PHE VAL
SEQRES 15 A 242 VAL GLN ALA ARG HIS ASP ASP MET ILE ASN THR ASP SER
SEQRES 16 A 242 ALA ASN ILE ILE TYR ASN GLY VAL GLU SER PRO ILE LYS
SEQRES 17 A 242 GLN ILE LYS TRP TYR GLU GLU SER GLY HIS VAL ILE THR
SEQRES 18 A 242 LEU ASP LYS GLU LYS GLU GLN LEU HIS GLU ASP ILE TYR
SEQRES 19 A 242 ALA PHE LEU GLU SER LEU ASP TRP
SEQRES 1 B 242 SER PRO LYS PRO PHE THR PHE GLU ALA GLY GLU ARG ALA
SEQRES 2 B 242 VAL LEU LEU LEU HIS GLY PHE THR GLY ASN SER SER ASP
SEQRES 3 B 242 VAL ARG MET LEU GLY ARG PHE LEU GLU SER LYS GLY TYR
SEQRES 4 B 242 THR CYS HIS ALA PRO ILE TYR LYS GLY HIS GLY VAL PRO
SEQRES 5 B 242 PRO GLU GLU LEU VAL HIS THR GLY PRO ASP ASP TRP TRP
SEQRES 6 B 242 GLN ASP VAL MET ASN ALA TYR GLU PHE LEU ARG GLU LYS
SEQRES 7 B 242 GLY TYR GLN LYS ILE ALA VAL VAL GLY LEU SER LEU GLY
SEQRES 8 B 242 GLY VAL PHE SER LEU LYS LEU GLY TYR THR VAL PRO VAL
SEQRES 9 B 242 VAL GLY ILE VAL PRO MET CYS ALA PRO MET TYR ILE LYS
SEQRES 10 B 242 SER GLU GLU THR MET TYR GLN GLY VAL LEU ASP TYR ALA
SEQRES 11 B 242 ARG GLU TYR LYS LYS ARG GLU GLY LYS ALA PRO GLU GLN
SEQRES 12 B 242 ILE GLU LYS GLU MET GLU GLU PHE ARG LYS THR PRO MET
SEQRES 13 B 242 LYS THR LEU LYS ALA LEU GLN ALA LEU ILE ALA GLU VAL
SEQRES 14 B 242 ARG ASN HIS ILE ASP LEU ILE TYR ALA PRO THR PHE VAL
SEQRES 15 B 242 VAL GLN ALA ARG HIS ASP ASP MET ILE ASN THR ASP SER
SEQRES 16 B 242 ALA ASN ILE ILE TYR ASN GLY VAL GLU SER PRO ILE LYS
SEQRES 17 B 242 GLN ILE LYS TRP TYR GLU GLU SER GLY HIS VAL ILE THR
SEQRES 18 B 242 LEU ASP LYS GLU LYS GLU GLN LEU HIS GLU ASP ILE TYR
SEQRES 19 B 242 ALA PHE LEU GLU SER LEU ASP TRP
SEQRES 1 C 242 SER PRO LYS PRO PHE THR PHE GLU ALA GLY GLU ARG ALA
SEQRES 2 C 242 VAL LEU LEU LEU HIS GLY PHE THR GLY ASN SER SER ASP
SEQRES 3 C 242 VAL ARG MET LEU GLY ARG PHE LEU GLU SER LYS GLY TYR
SEQRES 4 C 242 THR CYS HIS ALA PRO ILE TYR LYS GLY HIS GLY VAL PRO
SEQRES 5 C 242 PRO GLU GLU LEU VAL HIS THR GLY PRO ASP ASP TRP TRP
SEQRES 6 C 242 GLN ASP VAL MET ASN ALA TYR GLU PHE LEU ARG GLU LYS
SEQRES 7 C 242 GLY TYR GLN LYS ILE ALA VAL VAL GLY LEU SER LEU GLY
SEQRES 8 C 242 GLY VAL PHE SER LEU LYS LEU GLY TYR THR VAL PRO VAL
SEQRES 9 C 242 VAL GLY ILE VAL PRO MET CYS ALA PRO MET TYR ILE LYS
SEQRES 10 C 242 SER GLU GLU THR MET TYR GLN GLY VAL LEU ASP TYR ALA
SEQRES 11 C 242 ARG GLU TYR LYS LYS ARG GLU GLY LYS ALA PRO GLU GLN
SEQRES 12 C 242 ILE GLU LYS GLU MET GLU GLU PHE ARG LYS THR PRO MET
SEQRES 13 C 242 LYS THR LEU LYS ALA LEU GLN ALA LEU ILE ALA GLU VAL
SEQRES 14 C 242 ARG ASN HIS ILE ASP LEU ILE TYR ALA PRO THR PHE VAL
SEQRES 15 C 242 VAL GLN ALA ARG HIS ASP ASP MET ILE ASN THR ASP SER
SEQRES 16 C 242 ALA ASN ILE ILE TYR ASN GLY VAL GLU SER PRO ILE LYS
SEQRES 17 C 242 GLN ILE LYS TRP TYR GLU GLU SER GLY HIS VAL ILE THR
SEQRES 18 C 242 LEU ASP LYS GLU LYS GLU GLN LEU HIS GLU ASP ILE TYR
SEQRES 19 C 242 ALA PHE LEU GLU SER LEU ASP TRP
FORMUL 4 HOH *207(H2 O)
HELIX 1 AA1 SER A 28 LYS A 41 1 14
HELIX 2 AA2 PRO A 56 VAL A 61 1 6
HELIX 3 AA3 GLY A 64 LYS A 82 1 19
HELIX 4 AA4 SER A 93 VAL A 106 1 14
HELIX 5 AA5 SER A 122 GLU A 141 1 20
HELIX 6 AA6 ALA A 144 ARG A 156 1 13
HELIX 7 AA7 THR A 162 ASN A 175 1 14
HELIX 8 AA8 HIS A 176 ILE A 180 5 5
HELIX 9 AA9 THR A 197 VAL A 207 1 11
HELIX 10 AB1 VAL A 223 ASP A 227 5 5
HELIX 11 AB2 GLU A 229 SER A 243 1 15
HELIX 12 AB3 ASN B 27 ASP B 30 5 4
HELIX 13 AB4 VAL B 31 LYS B 41 1 11
HELIX 14 AB5 PRO B 56 VAL B 61 1 6
HELIX 15 AB6 GLY B 64 LYS B 82 1 19
HELIX 16 AB7 SER B 93 VAL B 106 1 14
HELIX 17 AB8 SER B 122 GLU B 141 1 20
HELIX 18 AB9 ALA B 144 ARG B 156 1 13
HELIX 19 AC1 PRO B 159 ASN B 175 1 17
HELIX 20 AC2 HIS B 176 ILE B 180 5 5
HELIX 21 AC3 ASP B 198 VAL B 207 1 10
HELIX 22 AC4 VAL B 223 ASP B 227 5 5
HELIX 23 AC5 GLU B 229 SER B 243 1 15
HELIX 24 AC6 SER C 28 LYS C 41 1 14
HELIX 25 AC7 PRO C 56 VAL C 61 1 6
HELIX 26 AC8 GLY C 64 LYS C 82 1 19
HELIX 27 AC9 SER C 93 VAL C 106 1 14
HELIX 28 AD1 SER C 122 GLU C 141 1 20
HELIX 29 AD2 ALA C 144 ARG C 156 1 13
HELIX 30 AD3 PRO C 159 ASN C 175 1 17
HELIX 31 AD4 HIS C 176 ILE C 180 5 5
HELIX 32 AD5 ASP C 198 VAL C 207 1 10
HELIX 33 AD6 VAL C 223 ASP C 227 5 5
HELIX 34 AD7 GLU C 229 LEU C 244 1 16
SHEET 1 AA1 5 PHE A 9 PHE A 11 0
SHEET 2 AA1 5 THR A 44 ALA A 47 -1 O ALA A 47 N PHE A 9
SHEET 3 AA1 5 ALA A 17 LEU A 21 1 N LEU A 20 O HIS A 46
SHEET 4 AA1 5 ILE A 87 LEU A 92 1 O ALA A 88 N LEU A 19
SHEET 5 AA1 5 GLY A 110 MET A 114 1 O MET A 114 N GLY A 91
SHEET 1 AA2 2 THR A 184 ALA A 189 0
SHEET 2 AA2 2 LYS A 212 TYR A 217 1 O GLN A 213 N VAL A 186
SHEET 1 AA3 5 PHE B 9 PHE B 11 0
SHEET 2 AA3 5 THR B 44 ALA B 47 -1 O CYS B 45 N PHE B 11
SHEET 3 AA3 5 ALA B 17 LEU B 21 1 N LEU B 20 O HIS B 46
SHEET 4 AA3 5 ILE B 87 LEU B 92 1 O LEU B 92 N LEU B 21
SHEET 5 AA3 5 GLY B 110 MET B 114 1 O MET B 114 N GLY B 91
SHEET 1 AA4 2 THR B 184 ALA B 189 0
SHEET 2 AA4 2 LYS B 212 TYR B 217 1 O GLN B 213 N VAL B 186
SHEET 1 AA5 5 PHE C 9 PHE C 11 0
SHEET 2 AA5 5 THR C 44 ALA C 47 -1 O ALA C 47 N PHE C 9
SHEET 3 AA5 5 ALA C 17 LEU C 21 1 N LEU C 20 O HIS C 46
SHEET 4 AA5 5 ILE C 87 LEU C 92 1 O ALA C 88 N LEU C 19
SHEET 5 AA5 5 ILE C 111 MET C 114 1 O MET C 114 N GLY C 91
SHEET 1 AA6 2 THR C 184 ALA C 189 0
SHEET 2 AA6 2 LYS C 212 TYR C 217 1 O GLN C 213 N VAL C 186
CRYST1 58.970 111.628 114.885 90.00 90.00 90.00 P 21 21 21 12
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 0.016958 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008958 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008704 0.00000
TER 1948 TRP A 246
TER 3896 TRP B 246
TER 5844 TRP C 246
MASTER 406 0 0 34 21 0 0 6 6048 3 0 57
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