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HEADER HYDROLASE 02-SEP-19 6KUS
TITLE CRYSTAL STRCUTURE OF PETASE S121E, D186H, S242T, N246D MUTANT FROM
TITLE 2 IDEONELLA SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PETASE,PET-DIGESTING ENZYME;
COMPND 5 EC: 3.1.1.101;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: IDEONELLA SAKAIENSIS (STRAIN NBRC 110686 /
SOURCE 3 TISTR 2288 / 201-F6);
SOURCE 4 ORGANISM_TAXID: 1547922;
SOURCE 5 GENE: ISF6_4831;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PETASE, PET HYDROLASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.JOO,K.-J.KIM
REVDAT 1 02-SEP-20 6KUS 0
JRNL AUTH S.JOO,K.-J.KIM
JRNL TITL CRYSTAL STRCUTURE OF PETASE A248D, R280K MUTANT FROM
JRNL TITL 2 IDEONELLA SAKAIENSIS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.21
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 3 NUMBER OF REFLECTIONS : 24668
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.500
REMARK 3 FREE R VALUE TEST SET COUNT : 1168
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1698
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.77
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 74
REMARK 3 BIN FREE R VALUE : 0.2380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1928
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 99
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.32000
REMARK 3 B22 (A**2) : -1.49000
REMARK 3 B33 (A**2) : -0.51000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.12000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.107
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.104
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.461
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.946
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1975 ; 0.011 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 1742 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2689 ; 1.660 ; 1.640
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4052 ; 1.517 ; 1.566
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 261 ; 7.067 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 90 ;29.857 ;21.444
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 292 ;12.035 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;18.512 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 269 ; 0.083 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2270 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 421 ; 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 6KUS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-SEP-19.
REMARK 100 THE DEPOSITION ID IS D_1300013703.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-DEC-18
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97834
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25836
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 20.7700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.83
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: 5XJH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG 10K, 0.1M BIS-TRIS, PH 5.0,
REMARK 280 0.15M AMMONIUM ACETATE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 57.49650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.60350
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 57.49650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 25.60350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9840 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 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 13
REMARK 465 GLY A 14
REMARK 465 SER A 15
REMARK 465 SER A 16
REMARK 465 HIS A 17
REMARK 465 HIS A 18
REMARK 465 HIS A 19
REMARK 465 HIS A 20
REMARK 465 HIS A 21
REMARK 465 HIS A 22
REMARK 465 SER A 23
REMARK 465 SER A 24
REMARK 465 GLY A 25
REMARK 465 LEU A 26
REMARK 465 VAL A 27
REMARK 465 PRO A 28
REMARK 465 ARG A 29
REMARK 465 GLU A 292
REMARK 465 ASP A 293
REMARK 465 PRO A 294
REMARK 465 ALA A 295
REMARK 465 ALA A 296
REMARK 465 ASN A 297
REMARK 465 LYS A 298
REMARK 465 ALA A 299
REMARK 465 ARG A 300
REMARK 465 LYS A 301
REMARK 465 GLU A 302
REMARK 465 ALA A 303
REMARK 465 GLU A 304
REMARK 465 LEU A 305
REMARK 465 ALA A 306
REMARK 465 ALA A 307
REMARK 465 ALA A 308
REMARK 465 THR A 309
REMARK 465 ALA A 310
REMARK 465 GLU A 311
REMARK 465 GLN A 312
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 ASN A 73 36.69 -145.46
REMARK 500 THR A 88 -8.53 77.51
REMARK 500 SER A 160 -118.79 62.18
REMARK 500 SER A 214 -92.02 -123.00
REMARK 500
REMARK 500 REMARK: NULL
DBREF1 6KUS A 34 290 UNP PETH_IDESA
DBREF2 6KUS A A0A0K8P6T7 34 290
SEQADV 6KUS MET A 13 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS GLY A 14 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS SER A 15 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS SER A 16 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS HIS A 17 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS HIS A 18 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS HIS A 19 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS HIS A 20 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS HIS A 21 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS HIS A 22 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS SER A 23 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS SER A 24 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS GLY A 25 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS LEU A 26 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS VAL A 27 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS PRO A 28 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS ARG A 29 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS GLY A 30 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS SER A 31 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS HIS A 32 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS MET A 33 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS GLU A 121 UNP A0A0K8P6T SER 121 ENGINEERED MUTATION
SEQADV 6KUS HIS A 186 UNP A0A0K8P6T ASP 186 ENGINEERED MUTATION
SEQADV 6KUS THR A 242 UNP A0A0K8P6T SER 242 ENGINEERED MUTATION
SEQADV 6KUS ASP A 246 UNP A0A0K8P6T ASN 246 ENGINEERED MUTATION
SEQADV 6KUS LEU A 291 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS GLU A 292 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS ASP A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS PRO A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS ALA A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS ALA A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS ASN A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS LYS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS ALA A 299 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS ARG A 300 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS LYS A 301 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS GLU A 302 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS ALA A 303 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS GLU A 304 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS LEU A 305 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS ALA A 306 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS ALA A 307 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS ALA A 308 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS THR A 309 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS ALA A 310 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS GLU A 311 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 6KUS GLN A 312 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 300 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 300 LEU VAL PRO ARG GLY SER HIS MET ARG GLY PRO ASN PRO
SEQRES 3 A 300 THR ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR
SEQRES 4 A 300 VAL ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY
SEQRES 5 A 300 ALA GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR
SEQRES 6 A 300 VAL GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG
SEQRES 7 A 300 GLN SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER
SEQRES 8 A 300 HIS GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR
SEQRES 9 A 300 LEU ASP GLN PRO GLU SER ARG SER SER GLN GLN MET ALA
SEQRES 10 A 300 ALA LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER
SEQRES 11 A 300 SER PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY
SEQRES 12 A 300 VAL MET GLY TRP SER MET GLY GLY GLY GLY SER LEU ILE
SEQRES 13 A 300 SER ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO
SEQRES 14 A 300 GLN ALA PRO TRP HIS SER SER THR ASN PHE SER SER VAL
SEQRES 15 A 300 THR VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER
SEQRES 16 A 300 ILE ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP
SEQRES 17 A 300 SER MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN
SEQRES 18 A 300 GLY GLY SER HIS SER CYS ALA ASN THR GLY ASN SER ASP
SEQRES 19 A 300 GLN ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS
SEQRES 20 A 300 ARG PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA
SEQRES 21 A 300 CYS GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG
SEQRES 22 A 300 THR ALA ASN CYS SER LEU GLU ASP PRO ALA ALA ASN LYS
SEQRES 23 A 300 ALA ARG LYS GLU ALA GLU LEU ALA ALA ALA THR ALA GLU
SEQRES 24 A 300 GLN
FORMUL 2 HOH *99(H2 O)
HELIX 1 AA1 THR A 39 ALA A 45 1 7
HELIX 2 AA2 ARG A 90 LYS A 95 5 6
HELIX 3 AA3 TRP A 96 SER A 103 1 8
HELIX 4 AA4 GLN A 119 GLY A 139 1 21
HELIX 5 AA5 SER A 160 ASN A 173 1 14
HELIX 6 AA6 SER A 214 SER A 221 1 8
HELIX 7 AA7 ASP A 246 ASP A 263 1 18
HELIX 8 AA8 ASP A 265 ARG A 267 5 3
HELIX 9 AA9 TYR A 268 GLU A 274 1 7
SHEET 1 AA1 6 VAL A 52 THR A 56 0
SHEET 2 AA1 6 ALA A 65 PRO A 71 -1 O VAL A 68 N PHE A 55
SHEET 3 AA1 6 VAL A 107 ASP A 112 -1 O VAL A 108 N TYR A 69
SHEET 4 AA1 6 VAL A 78 VAL A 84 1 N ILE A 83 O ILE A 109
SHEET 5 AA1 6 VAL A 149 GLY A 158 1 O MET A 157 N ALA A 82
SHEET 6 AA1 6 ALA A 178 ALA A 179 1 O ALA A 178 N VAL A 156
SHEET 1 AA2 3 THR A 198 CYS A 203 0
SHEET 2 AA2 3 LYS A 227 ILE A 232 1 O LEU A 230 N ALA A 202
SHEET 3 AA2 3 VAL A 281 ALA A 287 -1 O ASP A 283 N GLU A 231
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.05
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.08
CRYST1 114.993 51.207 51.060 90.00 109.64 90.00 C 1 2 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 0.008696 0.000000 0.003103 0.00000
SCALE2 0.000000 0.019529 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020794 0.00000
TER 1929 LEU A 291
MASTER 306 0 0 9 9 0 0 6 2027 1 4 24
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