content |
HEADER HYDROLASE 16-MAY-10 3AIM
TITLE R267E MUTANT OF A HSL-LIKE CARBOXYLESTERASE FROM SULFOLOBUS TOKODAII
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 303AA LONG HYPOTHETICAL ESTERASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: CARBOXYLESTERASE;
COMPND 5 EC: 3.1.1.1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS TOKODAII;
SOURCE 3 ORGANISM_TAXID: 111955;
SOURCE 4 STRAIN: 7;
SOURCE 5 GENE: ST0071;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)CODONPLUS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A+
KEYWDS CARBOXYLESTERASE, THERMOPHILIC, DIMER, ARCHAEA, R267E, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR C.ANGKAWIDJAJA,S.KANAYA
REVDAT 1 08-JUN-11 3AIM 0
JRNL AUTH C.ANGKAWIDJAJA,Y.KOGA,K.TAKANO,S.KANAYA
JRNL TITL STRUCTURAL CHARACTERIZATION OF A HSL-LIKE CARBOXYLESTERASE
JRNL TITL 2 FROM A THERMOACIDOPHILIC ARCHAEON SULFOLOBUS TOKODAII
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 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 WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 3 NUMBER OF REFLECTIONS : 67472
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) : 0.212
REMARK 3 R VALUE (WORKING SET) : 0.210
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3588
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3500
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 68.70
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE SET COUNT : 198
REMARK 3 BIN FREE R VALUE : 0.3330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8940
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 105
REMARK 3 SOLVENT ATOMS : 158
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.98000
REMARK 3 B22 (A**2) : -0.93000
REMARK 3 B33 (A**2) : 1.09000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.68000
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): 0.217
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.155
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.502
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9253 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12568 ; 0.897 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1128 ; 8.370 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 432 ;35.182 ;24.167
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1476 ;19.024 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 44 ;19.167 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1366 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7072 ; 0.017 ; 0.021
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): 5616 ; 1.701 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9056 ; 2.771 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3637 ; 4.682 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3512 ; 6.800 ; 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 : 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 : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3AIM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB029298.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : MIRRORS
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71172
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.15700
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.39200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.800
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: 3AIK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.92
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 8.5, 0.2M AMMONIUM
REMARK 280 PHOSPHATE MONOBASIC, 50% MPD , VAPOR DIFFUSION, SITTING DROP,
REMARK 280 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 57.41750
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, 3, 4
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22120 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ILE A 2
REMARK 465 ASP A 3
REMARK 465 PRO A 4
REMARK 465 LYS A 5
REMARK 465 ILE A 6
REMARK 465 LYS A 7
REMARK 465 LYS A 8
REMARK 465 LEU A 9
REMARK 465 LEU A 10
REMARK 465 GLU A 11
REMARK 465 SER A 12
REMARK 465 THR A 13
REMARK 465 ILE A 14
REMARK 465 GLN A 15
REMARK 465 LEU A 16
REMARK 465 PRO A 17
REMARK 465 ILE A 18
REMARK 465 GLY A 19
REMARK 465 LYS A 20
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ILE B 2
REMARK 465 ASP B 3
REMARK 465 PRO B 4
REMARK 465 LYS B 5
REMARK 465 ILE B 6
REMARK 465 LYS B 7
REMARK 465 LYS B 8
REMARK 465 LEU B 9
REMARK 465 LEU B 10
REMARK 465 GLU B 11
REMARK 465 SER B 12
REMARK 465 THR B 13
REMARK 465 ILE B 14
REMARK 465 GLN B 15
REMARK 465 LEU B 16
REMARK 465 PRO B 17
REMARK 465 ILE B 18
REMARK 465 GLY B 19
REMARK 465 LYS B 20
REMARK 465 MET C -19
REMARK 465 GLY C -18
REMARK 465 SER C -17
REMARK 465 SER C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 HIS C -10
REMARK 465 SER C -9
REMARK 465 SER C -8
REMARK 465 GLY C -7
REMARK 465 LEU C -6
REMARK 465 VAL C -5
REMARK 465 PRO C -4
REMARK 465 ARG C -3
REMARK 465 GLY C -2
REMARK 465 SER C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 ILE C 2
REMARK 465 ASP C 3
REMARK 465 PRO C 4
REMARK 465 LYS C 5
REMARK 465 ILE C 6
REMARK 465 LYS C 7
REMARK 465 LYS C 8
REMARK 465 LEU C 9
REMARK 465 LEU C 10
REMARK 465 GLU C 11
REMARK 465 SER C 12
REMARK 465 THR C 13
REMARK 465 ILE C 14
REMARK 465 GLN C 15
REMARK 465 LEU C 16
REMARK 465 PRO C 17
REMARK 465 ILE C 18
REMARK 465 GLY C 19
REMARK 465 LYS C 20
REMARK 465 MET D -19
REMARK 465 GLY D -18
REMARK 465 SER D -17
REMARK 465 SER D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 HIS D -10
REMARK 465 SER D -9
REMARK 465 SER D -8
REMARK 465 GLY D -7
REMARK 465 LEU D -6
REMARK 465 VAL D -5
REMARK 465 PRO D -4
REMARK 465 ARG D -3
REMARK 465 GLY D -2
REMARK 465 SER D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ILE D 2
REMARK 465 ASP D 3
REMARK 465 PRO D 4
REMARK 465 LYS D 5
REMARK 465 ILE D 6
REMARK 465 LYS D 7
REMARK 465 LYS D 8
REMARK 465 LEU D 9
REMARK 465 LEU D 10
REMARK 465 GLU D 11
REMARK 465 SER D 12
REMARK 465 THR D 13
REMARK 465 ILE D 14
REMARK 465 GLN D 15
REMARK 465 LEU D 16
REMARK 465 PRO D 17
REMARK 465 ILE D 18
REMARK 465 GLY D 19
REMARK 465 LYS D 20
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 D 177 CD1 TYR D 177 CE1 -0.097
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 183 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP C 183 CB - CG - OD1 ANGL. DEV. = 5.5 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 LYS A 44 131.47 -176.37
REMARK 500 ASP A 85 -172.17 -175.44
REMARK 500 PHE A 117 128.76 -35.07
REMARK 500 SER A 150 -125.58 64.32
REMARK 500 TYR A 177 59.15 31.71
REMARK 500 PHE A 197 -58.05 74.19
REMARK 500 HIS A 242 44.41 -99.01
REMARK 500 ASN A 270 0.77 83.61
REMARK 500 LYS B 44 138.81 -175.97
REMARK 500 PHE B 117 135.00 -35.06
REMARK 500 SER B 150 -124.73 63.12
REMARK 500 TYR B 177 59.57 34.11
REMARK 500 SER B 181 146.12 -173.29
REMARK 500 PHE B 197 -60.22 76.45
REMARK 500 HIS B 242 51.96 -94.04
REMARK 500 LYS C 44 160.00 175.36
REMARK 500 ASP C 85 -171.22 -174.88
REMARK 500 SER C 150 -116.72 54.07
REMARK 500 TYR C 177 63.41 32.09
REMARK 500 PHE C 197 -60.97 74.03
REMARK 500 PHE C 214 -38.69 -36.51
REMARK 500 PRO C 234 150.74 -40.17
REMARK 500 HIS C 242 48.18 -93.31
REMARK 500 PRO D 51 92.71 -67.26
REMARK 500 VAL D 82 -39.23 -131.79
REMARK 500 ASP D 85 -167.66 -176.09
REMARK 500 ASP D 108 63.69 -101.84
REMARK 500 PHE D 117 139.45 -36.77
REMARK 500 SER D 150 -124.91 61.27
REMARK 500 TYR D 177 61.38 38.73
REMARK 500 SER D 181 146.39 -174.74
REMARK 500 PHE D 196 50.00 -114.41
REMARK 500 PHE D 197 -64.55 68.88
REMARK 500 HIS D 242 44.57 -91.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 TYR A 70 GLY A 71 149.72
REMARK 500 TYR B 70 GLY B 71 146.06
REMARK 500 TYR C 70 GLY C 71 149.69
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ILE A 185 23.8 L L OUTSIDE RANGE
REMARK 500 ASN A 230 24.1 L L OUTSIDE RANGE
REMARK 500 GLN A 262 23.5 L L OUTSIDE RANGE
REMARK 500 ILE B 185 24.6 L L OUTSIDE RANGE
REMARK 500 VAL B 263 22.1 L L OUTSIDE RANGE
REMARK 500 TYR D 177 24.6 L L OUTSIDE RANGE
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 A 385 DISTANCE = 5.33 ANGSTROMS
REMARK 525 HOH A 525 DISTANCE = 5.15 ANGSTROMS
REMARK 525 HOH A 541 DISTANCE = 8.93 ANGSTROMS
REMARK 525 HOH A 542 DISTANCE = 7.90 ANGSTROMS
REMARK 525 HOH A 544 DISTANCE = 10.64 ANGSTROMS
REMARK 525 HOH A 573 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 576 DISTANCE = 11.17 ANGSTROMS
REMARK 525 HOH B 533 DISTANCE = 6.85 ANGSTROMS
REMARK 525 HOH B 534 DISTANCE = 7.61 ANGSTROMS
REMARK 525 HOH B 535 DISTANCE = 8.04 ANGSTROMS
REMARK 525 HOH B 536 DISTANCE = 9.55 ANGSTROMS
REMARK 525 HOH B 537 DISTANCE = 9.75 ANGSTROMS
REMARK 525 HOH B 616 DISTANCE = 7.67 ANGSTROMS
REMARK 525 HOH B 621 DISTANCE = 5.11 ANGSTROMS
REMARK 525 HOH C 540 DISTANCE = 8.86 ANGSTROMS
REMARK 525 HOH C 575 DISTANCE = 5.77 ANGSTROMS
REMARK 525 HOH C 577 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH D 538 DISTANCE = 5.61 ANGSTROMS
REMARK 525 HOH D 539 DISTANCE = 5.50 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD C 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD C 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD C 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD D 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD D 306
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AIK RELATED DB: PDB
REMARK 900 PARENT PROTEIN, PARENT PROTEIN COMPLEXED WITH INHIBITOR
REMARK 900 RELATED ID: 3AIL RELATED DB: PDB
REMARK 900 PARENT PROTEIN, PARENT PROTEIN COMPLEXED WITH INHIBITOR
REMARK 900 RELATED ID: 3AIN RELATED DB: PDB
REMARK 900 RELATED ID: 3AIO RELATED DB: PDB
DBREF 3AIM A 1 303 UNP Q976W8 Q976W8_SULTO 1 303
DBREF 3AIM B 1 303 UNP Q976W8 Q976W8_SULTO 1 303
DBREF 3AIM C 1 303 UNP Q976W8 Q976W8_SULTO 1 303
DBREF 3AIM D 1 303 UNP Q976W8 Q976W8_SULTO 1 303
SEQADV 3AIM MET A -19 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLY A -18 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER A -17 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER A -16 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS A -15 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS A -14 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS A -13 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS A -12 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS A -11 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS A -10 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER A -9 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER A -8 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLY A -7 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM LEU A -6 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM VAL A -5 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM PRO A -4 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM ARG A -3 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLY A -2 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER A -1 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS A 0 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLU A 267 UNP Q976W8 ARG 267 ENGINEERED MUTATION
SEQADV 3AIM MET B -19 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLY B -18 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER B -17 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER B -16 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS B -15 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS B -14 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS B -13 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS B -12 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS B -11 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS B -10 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER B -9 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER B -8 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLY B -7 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM LEU B -6 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM VAL B -5 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM PRO B -4 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM ARG B -3 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLY B -2 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER B -1 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS B 0 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLU B 267 UNP Q976W8 ARG 267 ENGINEERED MUTATION
SEQADV 3AIM MET C -19 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLY C -18 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER C -17 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER C -16 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS C -15 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS C -14 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS C -13 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS C -12 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS C -11 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS C -10 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER C -9 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER C -8 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLY C -7 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM LEU C -6 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM VAL C -5 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM PRO C -4 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM ARG C -3 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLY C -2 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER C -1 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS C 0 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLU C 267 UNP Q976W8 ARG 267 ENGINEERED MUTATION
SEQADV 3AIM MET D -19 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLY D -18 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER D -17 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER D -16 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS D -15 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS D -14 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS D -13 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS D -12 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS D -11 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS D -10 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER D -9 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER D -8 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLY D -7 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM LEU D -6 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM VAL D -5 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM PRO D -4 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM ARG D -3 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLY D -2 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM SER D -1 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM HIS D 0 UNP Q976W8 EXPRESSION TAG
SEQADV 3AIM GLU D 267 UNP Q976W8 ARG 267 ENGINEERED MUTATION
SEQRES 1 A 323 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 323 LEU VAL PRO ARG GLY SER HIS MET ILE ASP PRO LYS ILE
SEQRES 3 A 323 LYS LYS LEU LEU GLU SER THR ILE GLN LEU PRO ILE GLY
SEQRES 4 A 323 LYS ALA SER VAL GLU GLU ILE ARG SER LEU PHE LYS GLN
SEQRES 5 A 323 PHE SER SER LEU THR PRO ARG GLU GLU VAL GLY LYS ILE
SEQRES 6 A 323 GLU ASP ILE THR ILE PRO GLY SER GLU THR ASN ILE LYS
SEQRES 7 A 323 ALA ARG VAL TYR TYR PRO LYS THR GLN GLY PRO TYR GLY
SEQRES 8 A 323 VAL LEU VAL TYR TYR HIS GLY GLY GLY PHE VAL LEU GLY
SEQRES 9 A 323 ASP ILE GLU SER TYR ASP PRO LEU CYS ARG ALA ILE THR
SEQRES 10 A 323 ASN SER CYS GLN CYS VAL THR ILE SER VAL ASP TYR ARG
SEQRES 11 A 323 LEU ALA PRO GLU ASN LYS PHE PRO ALA ALA VAL VAL ASP
SEQRES 12 A 323 SER PHE ASP ALA LEU LYS TRP VAL TYR ASN ASN SER GLU
SEQRES 13 A 323 LYS PHE ASN GLY LYS TYR GLY ILE ALA VAL GLY GLY ASP
SEQRES 14 A 323 SER ALA GLY GLY ASN LEU ALA ALA VAL THR ALA ILE LEU
SEQRES 15 A 323 SER LYS LYS GLU ASN ILE LYS LEU LYS TYR GLN VAL LEU
SEQRES 16 A 323 ILE TYR PRO ALA VAL SER PHE ASP LEU ILE THR LYS SER
SEQRES 17 A 323 LEU TYR ASP ASN GLY GLU GLY PHE PHE LEU THR ARG GLU
SEQRES 18 A 323 HIS ILE ASP TRP PHE GLY GLN GLN TYR LEU ARG SER PHE
SEQRES 19 A 323 ALA ASP LEU LEU ASP PHE ARG PHE SER PRO ILE LEU ALA
SEQRES 20 A 323 ASP LEU ASN ASP LEU PRO PRO ALA LEU ILE ILE THR ALA
SEQRES 21 A 323 GLU HIS ASP PRO LEU ARG ASP GLN GLY GLU ALA TYR ALA
SEQRES 22 A 323 ASN LYS LEU LEU GLN SER GLY VAL GLN VAL THR SER VAL
SEQRES 23 A 323 GLU PHE ASN ASN VAL ILE HIS GLY PHE VAL SER PHE PHE
SEQRES 24 A 323 PRO PHE ILE GLU GLN GLY ARG ASP ALA ILE GLY LEU ILE
SEQRES 25 A 323 GLY TYR VAL LEU ARG LYS VAL PHE TYR GLY LYS
SEQRES 1 B 323 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 323 LEU VAL PRO ARG GLY SER HIS MET ILE ASP PRO LYS ILE
SEQRES 3 B 323 LYS LYS LEU LEU GLU SER THR ILE GLN LEU PRO ILE GLY
SEQRES 4 B 323 LYS ALA SER VAL GLU GLU ILE ARG SER LEU PHE LYS GLN
SEQRES 5 B 323 PHE SER SER LEU THR PRO ARG GLU GLU VAL GLY LYS ILE
SEQRES 6 B 323 GLU ASP ILE THR ILE PRO GLY SER GLU THR ASN ILE LYS
SEQRES 7 B 323 ALA ARG VAL TYR TYR PRO LYS THR GLN GLY PRO TYR GLY
SEQRES 8 B 323 VAL LEU VAL TYR TYR HIS GLY GLY GLY PHE VAL LEU GLY
SEQRES 9 B 323 ASP ILE GLU SER TYR ASP PRO LEU CYS ARG ALA ILE THR
SEQRES 10 B 323 ASN SER CYS GLN CYS VAL THR ILE SER VAL ASP TYR ARG
SEQRES 11 B 323 LEU ALA PRO GLU ASN LYS PHE PRO ALA ALA VAL VAL ASP
SEQRES 12 B 323 SER PHE ASP ALA LEU LYS TRP VAL TYR ASN ASN SER GLU
SEQRES 13 B 323 LYS PHE ASN GLY LYS TYR GLY ILE ALA VAL GLY GLY ASP
SEQRES 14 B 323 SER ALA GLY GLY ASN LEU ALA ALA VAL THR ALA ILE LEU
SEQRES 15 B 323 SER LYS LYS GLU ASN ILE LYS LEU LYS TYR GLN VAL LEU
SEQRES 16 B 323 ILE TYR PRO ALA VAL SER PHE ASP LEU ILE THR LYS SER
SEQRES 17 B 323 LEU TYR ASP ASN GLY GLU GLY PHE PHE LEU THR ARG GLU
SEQRES 18 B 323 HIS ILE ASP TRP PHE GLY GLN GLN TYR LEU ARG SER PHE
SEQRES 19 B 323 ALA ASP LEU LEU ASP PHE ARG PHE SER PRO ILE LEU ALA
SEQRES 20 B 323 ASP LEU ASN ASP LEU PRO PRO ALA LEU ILE ILE THR ALA
SEQRES 21 B 323 GLU HIS ASP PRO LEU ARG ASP GLN GLY GLU ALA TYR ALA
SEQRES 22 B 323 ASN LYS LEU LEU GLN SER GLY VAL GLN VAL THR SER VAL
SEQRES 23 B 323 GLU PHE ASN ASN VAL ILE HIS GLY PHE VAL SER PHE PHE
SEQRES 24 B 323 PRO PHE ILE GLU GLN GLY ARG ASP ALA ILE GLY LEU ILE
SEQRES 25 B 323 GLY TYR VAL LEU ARG LYS VAL PHE TYR GLY LYS
SEQRES 1 C 323 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 323 LEU VAL PRO ARG GLY SER HIS MET ILE ASP PRO LYS ILE
SEQRES 3 C 323 LYS LYS LEU LEU GLU SER THR ILE GLN LEU PRO ILE GLY
SEQRES 4 C 323 LYS ALA SER VAL GLU GLU ILE ARG SER LEU PHE LYS GLN
SEQRES 5 C 323 PHE SER SER LEU THR PRO ARG GLU GLU VAL GLY LYS ILE
SEQRES 6 C 323 GLU ASP ILE THR ILE PRO GLY SER GLU THR ASN ILE LYS
SEQRES 7 C 323 ALA ARG VAL TYR TYR PRO LYS THR GLN GLY PRO TYR GLY
SEQRES 8 C 323 VAL LEU VAL TYR TYR HIS GLY GLY GLY PHE VAL LEU GLY
SEQRES 9 C 323 ASP ILE GLU SER TYR ASP PRO LEU CYS ARG ALA ILE THR
SEQRES 10 C 323 ASN SER CYS GLN CYS VAL THR ILE SER VAL ASP TYR ARG
SEQRES 11 C 323 LEU ALA PRO GLU ASN LYS PHE PRO ALA ALA VAL VAL ASP
SEQRES 12 C 323 SER PHE ASP ALA LEU LYS TRP VAL TYR ASN ASN SER GLU
SEQRES 13 C 323 LYS PHE ASN GLY LYS TYR GLY ILE ALA VAL GLY GLY ASP
SEQRES 14 C 323 SER ALA GLY GLY ASN LEU ALA ALA VAL THR ALA ILE LEU
SEQRES 15 C 323 SER LYS LYS GLU ASN ILE LYS LEU LYS TYR GLN VAL LEU
SEQRES 16 C 323 ILE TYR PRO ALA VAL SER PHE ASP LEU ILE THR LYS SER
SEQRES 17 C 323 LEU TYR ASP ASN GLY GLU GLY PHE PHE LEU THR ARG GLU
SEQRES 18 C 323 HIS ILE ASP TRP PHE GLY GLN GLN TYR LEU ARG SER PHE
SEQRES 19 C 323 ALA ASP LEU LEU ASP PHE ARG PHE SER PRO ILE LEU ALA
SEQRES 20 C 323 ASP LEU ASN ASP LEU PRO PRO ALA LEU ILE ILE THR ALA
SEQRES 21 C 323 GLU HIS ASP PRO LEU ARG ASP GLN GLY GLU ALA TYR ALA
SEQRES 22 C 323 ASN LYS LEU LEU GLN SER GLY VAL GLN VAL THR SER VAL
SEQRES 23 C 323 GLU PHE ASN ASN VAL ILE HIS GLY PHE VAL SER PHE PHE
SEQRES 24 C 323 PRO PHE ILE GLU GLN GLY ARG ASP ALA ILE GLY LEU ILE
SEQRES 25 C 323 GLY TYR VAL LEU ARG LYS VAL PHE TYR GLY LYS
SEQRES 1 D 323 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 323 LEU VAL PRO ARG GLY SER HIS MET ILE ASP PRO LYS ILE
SEQRES 3 D 323 LYS LYS LEU LEU GLU SER THR ILE GLN LEU PRO ILE GLY
SEQRES 4 D 323 LYS ALA SER VAL GLU GLU ILE ARG SER LEU PHE LYS GLN
SEQRES 5 D 323 PHE SER SER LEU THR PRO ARG GLU GLU VAL GLY LYS ILE
SEQRES 6 D 323 GLU ASP ILE THR ILE PRO GLY SER GLU THR ASN ILE LYS
SEQRES 7 D 323 ALA ARG VAL TYR TYR PRO LYS THR GLN GLY PRO TYR GLY
SEQRES 8 D 323 VAL LEU VAL TYR TYR HIS GLY GLY GLY PHE VAL LEU GLY
SEQRES 9 D 323 ASP ILE GLU SER TYR ASP PRO LEU CYS ARG ALA ILE THR
SEQRES 10 D 323 ASN SER CYS GLN CYS VAL THR ILE SER VAL ASP TYR ARG
SEQRES 11 D 323 LEU ALA PRO GLU ASN LYS PHE PRO ALA ALA VAL VAL ASP
SEQRES 12 D 323 SER PHE ASP ALA LEU LYS TRP VAL TYR ASN ASN SER GLU
SEQRES 13 D 323 LYS PHE ASN GLY LYS TYR GLY ILE ALA VAL GLY GLY ASP
SEQRES 14 D 323 SER ALA GLY GLY ASN LEU ALA ALA VAL THR ALA ILE LEU
SEQRES 15 D 323 SER LYS LYS GLU ASN ILE LYS LEU LYS TYR GLN VAL LEU
SEQRES 16 D 323 ILE TYR PRO ALA VAL SER PHE ASP LEU ILE THR LYS SER
SEQRES 17 D 323 LEU TYR ASP ASN GLY GLU GLY PHE PHE LEU THR ARG GLU
SEQRES 18 D 323 HIS ILE ASP TRP PHE GLY GLN GLN TYR LEU ARG SER PHE
SEQRES 19 D 323 ALA ASP LEU LEU ASP PHE ARG PHE SER PRO ILE LEU ALA
SEQRES 20 D 323 ASP LEU ASN ASP LEU PRO PRO ALA LEU ILE ILE THR ALA
SEQRES 21 D 323 GLU HIS ASP PRO LEU ARG ASP GLN GLY GLU ALA TYR ALA
SEQRES 22 D 323 ASN LYS LEU LEU GLN SER GLY VAL GLN VAL THR SER VAL
SEQRES 23 D 323 GLU PHE ASN ASN VAL ILE HIS GLY PHE VAL SER PHE PHE
SEQRES 24 D 323 PRO PHE ILE GLU GLN GLY ARG ASP ALA ILE GLY LEU ILE
SEQRES 25 D 323 GLY TYR VAL LEU ARG LYS VAL PHE TYR GLY LYS
HET MPD A 304 8
HET PO4 A 305 5
HET PO4 A 306 5
HET MPD B 304 8
HET MPD B 305 8
HET MRD B 306 8
HET MRD B 307 8
HET PO4 B 308 5
HET MRD C 304 8
HET MRD C 305 8
HET PO4 C 306 5
HET MRD C 307 8
HET MRD D 304 8
HET PO4 D 305 5
HET MRD D 306 8
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM PO4 PHOSPHATE ION
HETNAM MRD (4R)-2-METHYLPENTANE-2,4-DIOL
FORMUL 5 MPD 3(C6 H14 O2)
FORMUL 6 PO4 5(O4 P 3-)
FORMUL 10 MRD 7(C6 H14 O2)
FORMUL 20 HOH *158(H2 O)
HELIX 1 1 SER A 22 SER A 35 1 14
HELIX 2 2 TYR A 89 GLN A 101 1 13
HELIX 3 3 PRO A 118 ASN A 134 1 17
HELIX 4 4 SER A 135 ASN A 139 5 5
HELIX 5 5 SER A 150 GLU A 166 1 17
HELIX 6 6 THR A 186 GLY A 193 1 8
HELIX 7 7 THR A 199 LEU A 211 1 13
HELIX 8 8 SER A 213 ASP A 219 5 7
HELIX 9 9 SER A 223 ALA A 227 5 5
HELIX 10 10 LEU A 245 SER A 259 1 15
HELIX 11 11 GLY A 274 PHE A 279 5 6
HELIX 12 12 ILE A 282 GLY A 302 1 21
HELIX 13 13 SER B 22 LEU B 36 1 15
HELIX 14 14 TYR B 89 GLN B 101 1 13
HELIX 15 15 PRO B 118 ASN B 134 1 17
HELIX 16 16 SER B 135 ASN B 139 5 5
HELIX 17 17 SER B 150 LYS B 165 1 16
HELIX 18 18 THR B 186 ASN B 192 1 7
HELIX 19 19 THR B 199 LEU B 211 1 13
HELIX 20 20 SER B 213 ASP B 219 5 7
HELIX 21 21 SER B 223 ALA B 227 5 5
HELIX 22 22 LEU B 245 SER B 259 1 15
HELIX 23 23 GLY B 274 PHE B 279 5 6
HELIX 24 24 ILE B 282 GLY B 302 1 21
HELIX 25 25 SER C 22 LEU C 36 1 15
HELIX 26 26 TYR C 89 GLN C 101 1 13
HELIX 27 27 PRO C 118 SER C 135 1 18
HELIX 28 28 GLU C 136 ASN C 139 5 4
HELIX 29 29 SER C 150 ASN C 167 1 18
HELIX 30 30 THR C 186 ASN C 192 1 7
HELIX 31 31 THR C 199 LEU C 211 1 13
HELIX 32 32 SER C 213 ASP C 219 5 7
HELIX 33 33 SER C 223 ALA C 227 5 5
HELIX 34 34 LEU C 245 SER C 259 1 15
HELIX 35 35 GLY C 274 PHE C 279 5 6
HELIX 36 36 ILE C 282 GLY C 302 1 21
HELIX 37 37 SER D 22 PHE D 33 1 12
HELIX 38 38 TYR D 89 GLN D 101 1 13
HELIX 39 39 PRO D 118 ASN D 134 1 17
HELIX 40 40 SER D 135 PHE D 138 5 4
HELIX 41 41 SER D 150 GLU D 166 1 17
HELIX 42 42 THR D 186 GLY D 193 1 8
HELIX 43 43 THR D 199 LEU D 211 1 13
HELIX 44 44 SER D 213 ASP D 219 5 7
HELIX 45 45 SER D 223 ALA D 227 5 5
HELIX 46 46 LEU D 245 SER D 259 1 15
HELIX 47 47 GLY D 274 PHE D 279 5 6
HELIX 48 48 ILE D 282 GLY D 302 1 21
SHEET 1 A16 LYS A 44 PRO A 51 0
SHEET 2 A16 ASN A 56 TYR A 63 -1 O VAL A 61 N GLU A 46
SHEET 3 A16 VAL A 103 VAL A 107 -1 O THR A 104 N TYR A 62
SHEET 4 A16 VAL A 72 TYR A 76 1 N LEU A 73 O VAL A 103
SHEET 5 A16 ILE A 144 ASP A 149 1 O ALA A 145 N VAL A 72
SHEET 6 A16 TYR A 172 ILE A 176 1 O ILE A 176 N GLY A 148
SHEET 7 A16 ALA A 235 ALA A 240 1 O LEU A 236 N LEU A 175
SHEET 8 A16 VAL A 263 PHE A 268 1 O VAL A 266 N ILE A 237
SHEET 9 A16 VAL D 263 PHE D 268 -1 O GLU D 267 N GLU A 267
SHEET 10 A16 ALA D 235 ALA D 240 1 N ILE D 237 O VAL D 266
SHEET 11 A16 TYR D 172 ILE D 176 1 N LEU D 175 O LEU D 236
SHEET 12 A16 ILE D 144 ASP D 149 1 N VAL D 146 O VAL D 174
SHEET 13 A16 VAL D 72 TYR D 76 1 N VAL D 74 O ALA D 145
SHEET 14 A16 VAL D 103 VAL D 107 1 O VAL D 103 N LEU D 73
SHEET 15 A16 ASN D 56 TYR D 63 -1 N TYR D 62 O THR D 104
SHEET 16 A16 LYS D 44 PRO D 51 -1 N ILE D 50 O ILE D 57
SHEET 1 B16 LYS B 44 PRO B 51 0
SHEET 2 B16 ASN B 56 TYR B 63 -1 O ALA B 59 N ILE B 48
SHEET 3 B16 VAL B 103 VAL B 107 -1 O THR B 104 N TYR B 62
SHEET 4 B16 VAL B 72 TYR B 76 1 N LEU B 73 O VAL B 103
SHEET 5 B16 ILE B 144 ASP B 149 1 O ALA B 145 N VAL B 74
SHEET 6 B16 TYR B 172 ILE B 176 1 O ILE B 176 N GLY B 148
SHEET 7 B16 ALA B 235 ALA B 240 1 O LEU B 236 N LEU B 175
SHEET 8 B16 VAL B 263 PHE B 268 1 O PHE B 268 N THR B 239
SHEET 9 B16 VAL C 263 PHE C 268 -1 O GLU C 267 N GLU B 267
SHEET 10 B16 ALA C 235 ALA C 240 1 N THR C 239 O PHE C 268
SHEET 11 B16 TYR C 172 ILE C 176 1 N LEU C 175 O LEU C 236
SHEET 12 B16 GLY C 143 ASP C 149 1 N VAL C 146 O VAL C 174
SHEET 13 B16 GLY C 71 TYR C 76 1 N VAL C 74 O ALA C 145
SHEET 14 B16 VAL C 103 VAL C 107 1 O VAL C 103 N LEU C 73
SHEET 15 B16 ASN C 56 TYR C 63 -1 N TYR C 62 O THR C 104
SHEET 16 B16 LYS C 44 PRO C 51 -1 N LYS C 44 O TYR C 63
SSBOND 1 CYS A 100 CYS A 102 1555 1555 2.06
SSBOND 2 CYS B 100 CYS B 102 1555 1555 2.07
SSBOND 3 CYS D 100 CYS D 102 1555 1555 2.06
CISPEP 1 GLY A 68 PRO A 69 0 -2.34
CISPEP 2 ALA A 112 PRO A 113 0 0.02
CISPEP 3 PHE A 117 PRO A 118 0 20.80
CISPEP 4 GLY B 68 PRO B 69 0 -1.57
CISPEP 5 ALA B 112 PRO B 113 0 9.79
CISPEP 6 PHE B 117 PRO B 118 0 7.86
CISPEP 7 GLY C 68 PRO C 69 0 0.08
CISPEP 8 ALA C 112 PRO C 113 0 6.22
CISPEP 9 PHE C 117 PRO C 118 0 18.33
CISPEP 10 GLY D 68 PRO D 69 0 -2.07
CISPEP 11 ALA D 112 PRO D 113 0 7.00
CISPEP 12 PHE D 117 PRO D 118 0 1.06
SITE 1 AC1 8 PHE A 81 SER A 150 ALA A 151 ALA A 179
SITE 2 AC1 8 PHE A 206 LEU A 245 HOH A 562 HOH A 578
SITE 1 AC2 3 PHE A 30 GLY A 79 HOH A 562
SITE 1 AC3 3 PRO A 118 ARG A 212 ARG A 221
SITE 1 AC4 4 SER B 150 ALA B 151 ALA B 179 PHE B 206
SITE 1 AC5 6 SER B 34 THR B 37 SER B 88 PRO B 91
SITE 2 AC5 6 LEU B 92 SER B 277
SITE 1 AC6 4 PHE B 30 GLY B 79 TYR B 89 SER B 277
SITE 1 AC7 2 LEU B 217 SER B 223
SITE 1 AC8 3 PRO B 118 ARG B 212 ARG B 221
SITE 1 AC9 5 ALA C 151 ALA C 179 PHE C 206 PHE C 222
SITE 2 AC9 5 HOH C 567
SITE 1 BC1 2 GLY C 207 GLN C 208
SITE 1 BC2 2 ARG C 212 ARG C 221
SITE 1 BC3 1 LEU C 217
SITE 1 BC4 4 ALA D 151 ALA D 179 PHE D 206 HOH D 563
SITE 1 BC5 3 PRO D 118 ARG D 212 ARG D 221
SITE 1 BC6 2 GLN D 208 PHE D 214
CRYST1 76.213 114.835 102.219 90.00 109.74 90.00 P 1 21 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 0.013121 0.000000 0.004708 0.00000
SCALE2 0.000000 0.008708 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010394 0.00000
TER 2236 LYS A 303
TER 4472 LYS B 303
TER 6708 LYS C 303
TER 8944 LYS D 303
MASTER 643 0 15 48 32 0 18 6 9203 4 111 100
END |