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HEADER HYDROLASE 08-JUN-21 7OSB
TITLE CRYSTAL STRUCTURE OF A DOUBLE MUTANT PETASE (S238F/W159H) FROM
TITLE 2 IDEONELLA SAKAIENSIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: PET HYDROLASE,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;
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 GENE: ISF6_4831;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.J.SHAKESPEARE,M.ZAHN,M.D.ALLEN,J.E.MCGEEHAN
REVDAT 1 13-OCT-21 7OSB 0
JRNL AUTH E.ERICKSON,T.J.SHAKESPEARE,F.BRATTI,B.L.BUSS,R.GRAHAM,
JRNL AUTH 2 M.A.HAWKINS,G.KONIG,W.E.MICHENER,J.MISCALL,K.J.RAMIREZ,
JRNL AUTH 3 N.A.RORRER,M.ZAHN,A.R.PICKFORD,J.E.MCGEEHAN,G.BECKHAM
JRNL TITL COMPARATIVE PERFORMANCE OF PETASE AS A FUNCTION OF REACTION
JRNL TITL 2 CONDITIONS, SUBSTRATE PROPERTIES, AND PRODUCT ACCUMULATION.
JRNL REF CHEMSUSCHEM 2021
JRNL REFN ISSN 1864-564X
JRNL PMID 34587366
JRNL DOI 10.1002/CSSC.202101932
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.4
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.02
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 178676
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.207
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 8759
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.46
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.71
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL
REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3874
REMARK 3 BIN FREE R VALUE : 0.3728
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 170
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5848
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 1082
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 18.11
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -15.89460
REMARK 3 B22 (A**2) : 10.99590
REMARK 3 B33 (A**2) : 4.89880
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.290
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.065
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.064
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.060
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.059
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6102 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 8327 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1996 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES : 1055 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6102 ; 10.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 828 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6709 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 0.94
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.16
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 12.96
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 4.1964 -59.0433 -13.1823
REMARK 3 T TENSOR
REMARK 3 T11: -0.0614 T22: 0.0319
REMARK 3 T33: 0.0198 T12: 0.0292
REMARK 3 T13: 0.0003 T23: -0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 0.0975 L22: 0.7948
REMARK 3 L33: 0.565 L12: -0.1397
REMARK 3 L13: -0.3265 L23: 0.2636
REMARK 3 S TENSOR
REMARK 3 S11: 0.1065 S12: -0.0281 S13: -0.0735
REMARK 3 S21: -0.0281 S22: 0.0099 S23: 0.027
REMARK 3 S31: -0.0735 S32: 0.027 S33: -0.1164
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 5.4361 -99.7667 -21.8643
REMARK 3 T TENSOR
REMARK 3 T11: 0.1163 T22: -0.0537
REMARK 3 T33: -0.0591 T12: 0.0412
REMARK 3 T13: -0.0116 T23: -0.0118
REMARK 3 L TENSOR
REMARK 3 L11: 0.1119 L22: 0.7829
REMARK 3 L33: 0.3054 L12: -0.2475
REMARK 3 L13: -0.1272 L23: 0.0546
REMARK 3 S TENSOR
REMARK 3 S11: -0.0627 S12: -0.0187 S13: 0.1361
REMARK 3 S21: -0.0187 S22: 0.0088 S23: -0.0054
REMARK 3 S31: 0.1361 S32: -0.0054 S33: 0.0539
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 25.3645 -136.342 -23.5881
REMARK 3 T TENSOR
REMARK 3 T11: 0.0855 T22: -0.0366
REMARK 3 T33: -0.037 T12: 0.0548
REMARK 3 T13: 0.0445 T23: 0.0307
REMARK 3 L TENSOR
REMARK 3 L11: 0.0449 L22: 0.4827
REMARK 3 L33: 0.5802 L12: -0.0441
REMARK 3 L13: 0.1349 L23: -0.2735
REMARK 3 S TENSOR
REMARK 3 S11: -0.0027 S12: 0.0724 S13: -0.1285
REMARK 3 S21: 0.0724 S22: -0.0498 S23: 0.0011
REMARK 3 S31: -0.1285 S32: 0.0011 S33: 0.0526
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 7OSB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUN-21.
REMARK 100 THE DEPOSITION ID IS D_1292116280.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-19
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DIALS, XIA2, DIALS
REMARK 200 DATA SCALING SOFTWARE : XIA2, DIALS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 178688
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 20.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 1.990
REMARK 200 R MERGE (I) : 0.02805
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.9900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.69940
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.110
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: 6EQE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.95M AMMONIUM SULFATE, 0.1M SODIUM
REMARK 280 CITRATE, PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 82.40400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 82.40400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 26.18950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 116.97850
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.18950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 116.97850
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 82.40400
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.18950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 116.97850
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 82.40400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.18950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 116.97850
REMARK 290 SMTRY3 8 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH B 613 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 PHE A 3
REMARK 465 PRO A 4
REMARK 465 ARG A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 ARG A 8
REMARK 465 LEU A 9
REMARK 465 MET A 10
REMARK 465 GLN A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 VAL A 14
REMARK 465 LEU A 15
REMARK 465 GLY A 16
REMARK 465 GLY A 17
REMARK 465 LEU A 18
REMARK 465 MET A 19
REMARK 465 ALA A 20
REMARK 465 VAL A 21
REMARK 465 SER A 22
REMARK 465 ALA A 23
REMARK 465 ALA A 24
REMARK 465 ALA A 25
REMARK 465 THR A 26
REMARK 465 ALA A 27
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 HIS A 298
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 PHE B 3
REMARK 465 PRO B 4
REMARK 465 ARG B 5
REMARK 465 ALA B 6
REMARK 465 SER B 7
REMARK 465 ARG B 8
REMARK 465 LEU B 9
REMARK 465 MET B 10
REMARK 465 GLN B 11
REMARK 465 ALA B 12
REMARK 465 ALA B 13
REMARK 465 VAL B 14
REMARK 465 LEU B 15
REMARK 465 GLY B 16
REMARK 465 GLY B 17
REMARK 465 LEU B 18
REMARK 465 MET B 19
REMARK 465 ALA B 20
REMARK 465 VAL B 21
REMARK 465 SER B 22
REMARK 465 ALA B 23
REMARK 465 ALA B 24
REMARK 465 ALA B 25
REMARK 465 THR B 26
REMARK 465 ALA B 27
REMARK 465 GLU B 292
REMARK 465 HIS B 293
REMARK 465 HIS B 294
REMARK 465 HIS B 295
REMARK 465 HIS B 296
REMARK 465 HIS B 297
REMARK 465 HIS B 298
REMARK 465 MET C 1
REMARK 465 ASN C 2
REMARK 465 PHE C 3
REMARK 465 PRO C 4
REMARK 465 ARG C 5
REMARK 465 ALA C 6
REMARK 465 SER C 7
REMARK 465 ARG C 8
REMARK 465 LEU C 9
REMARK 465 MET C 10
REMARK 465 GLN C 11
REMARK 465 ALA C 12
REMARK 465 ALA C 13
REMARK 465 VAL C 14
REMARK 465 LEU C 15
REMARK 465 GLY C 16
REMARK 465 GLY C 17
REMARK 465 LEU C 18
REMARK 465 MET C 19
REMARK 465 ALA C 20
REMARK 465 VAL C 21
REMARK 465 SER C 22
REMARK 465 ALA C 23
REMARK 465 ALA C 24
REMARK 465 ALA C 25
REMARK 465 THR C 26
REMARK 465 ALA C 27
REMARK 465 GLU C 292
REMARK 465 HIS C 293
REMARK 465 HIS C 294
REMARK 465 HIS C 295
REMARK 465 HIS C 296
REMARK 465 HIS C 297
REMARK 465 HIS C 298
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 C 421 O HOH C 482 1.59
REMARK 500 O HOH C 401 O HOH C 418 1.59
REMARK 500 O HOH C 523 O HOH C 677 2.07
REMARK 500 O HOH C 401 O HOH C 462 2.13
REMARK 500 O HOH C 482 O HOH C 542 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 401 O HOH A 586 8445 1.92
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 THR A 88 -8.52 73.48
REMARK 500 SER A 160 -119.19 59.66
REMARK 500 SER A 214 -85.90 -135.17
REMARK 500 THR B 88 -8.25 72.15
REMARK 500 SER B 160 -120.49 60.56
REMARK 500 SER B 214 -83.34 -135.02
REMARK 500 SER B 214 -86.09 -133.34
REMARK 500 THR C 88 -8.17 74.04
REMARK 500 SER C 160 -118.26 59.46
REMARK 500 SER C 214 -87.77 -133.80
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 752 DISTANCE = 5.93 ANGSTROMS
REMARK 525 HOH C 758 DISTANCE = 6.05 ANGSTROMS
DBREF1 7OSB A 1 290 UNP PETH_IDESA
DBREF2 7OSB A A0A0K8P6T7 1 290
DBREF1 7OSB B 1 290 UNP PETH_IDESA
DBREF2 7OSB B A0A0K8P6T7 1 290
DBREF1 7OSB C 1 290 UNP PETH_IDESA
DBREF2 7OSB C A0A0K8P6T7 1 290
SEQADV 7OSB HIS A 159 UNP A0A0K8P6T TRP 159 ENGINEERED MUTATION
SEQADV 7OSB PHE A 238 UNP A0A0K8P6T SER 238 ENGINEERED MUTATION
SEQADV 7OSB LEU A 291 UNP A0A0K8P6T LINKER
SEQADV 7OSB GLU A 292 UNP A0A0K8P6T LINKER
SEQADV 7OSB HIS A 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS A 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS A 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS A 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS A 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS A 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS B 159 UNP A0A0K8P6T TRP 159 ENGINEERED MUTATION
SEQADV 7OSB PHE B 238 UNP A0A0K8P6T SER 238 ENGINEERED MUTATION
SEQADV 7OSB LEU B 291 UNP A0A0K8P6T LINKER
SEQADV 7OSB GLU B 292 UNP A0A0K8P6T LINKER
SEQADV 7OSB HIS B 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS B 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS B 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS B 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS B 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS B 298 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS C 159 UNP A0A0K8P6T TRP 159 ENGINEERED MUTATION
SEQADV 7OSB PHE C 238 UNP A0A0K8P6T SER 238 ENGINEERED MUTATION
SEQADV 7OSB LEU C 291 UNP A0A0K8P6T LINKER
SEQADV 7OSB GLU C 292 UNP A0A0K8P6T LINKER
SEQADV 7OSB HIS C 293 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS C 294 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS C 295 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS C 296 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS C 297 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 7OSB HIS C 298 UNP A0A0K8P6T EXPRESSION TAG
SEQRES 1 A 298 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 A 298 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 A 298 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 A 298 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 A 298 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 A 298 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 A 298 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 A 298 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 A 298 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 A 298 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 A 298 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 A 298 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 A 298 MET GLY HIS SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 A 298 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 A 298 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 A 298 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 A 298 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 A 298 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 A 298 GLY SER HIS PHE CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 A 298 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 A 298 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 A 298 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 A 298 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 298 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 B 298 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 B 298 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 B 298 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 B 298 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 B 298 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 B 298 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 B 298 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 B 298 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 B 298 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 B 298 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 B 298 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 B 298 MET GLY HIS SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 B 298 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 B 298 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 B 298 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 B 298 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 B 298 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 B 298 GLY SER HIS PHE CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 B 298 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 B 298 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 B 298 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 B 298 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 C 298 MET ASN PHE PRO ARG ALA SER ARG LEU MET GLN ALA ALA
SEQRES 2 C 298 VAL LEU GLY GLY LEU MET ALA VAL SER ALA ALA ALA THR
SEQRES 3 C 298 ALA GLN THR ASN PRO TYR ALA ARG GLY PRO ASN PRO THR
SEQRES 4 C 298 ALA ALA SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL
SEQRES 5 C 298 ARG SER PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA
SEQRES 6 C 298 GLY THR VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL
SEQRES 7 C 298 GLY ALA ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN
SEQRES 8 C 298 SER SER ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS
SEQRES 9 C 298 GLY PHE VAL VAL ILE THR ILE ASP THR ASN SER THR LEU
SEQRES 10 C 298 ASP GLN PRO SER SER ARG SER SER GLN GLN MET ALA ALA
SEQRES 11 C 298 LEU ARG GLN VAL ALA SER LEU ASN GLY THR SER SER SER
SEQRES 12 C 298 PRO ILE TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL
SEQRES 13 C 298 MET GLY HIS SER MET GLY GLY GLY GLY SER LEU ILE SER
SEQRES 14 C 298 ALA ALA ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN
SEQRES 15 C 298 ALA PRO TRP ASP SER SER THR ASN PHE SER SER VAL THR
SEQRES 16 C 298 VAL PRO THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE
SEQRES 17 C 298 ALA PRO VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER
SEQRES 18 C 298 MET SER ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY
SEQRES 19 C 298 GLY SER HIS PHE CYS ALA ASN SER GLY ASN SER ASN GLN
SEQRES 20 C 298 ALA LEU ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG
SEQRES 21 C 298 PHE MET ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS
SEQRES 22 C 298 GLU ASN PRO ASN SER THR ARG VAL SER ASP PHE ARG THR
SEQRES 23 C 298 ALA ASN CYS SER LEU GLU HIS HIS HIS HIS HIS HIS
HET SO4 A 301 5
HET CL A 302 1
HET SO4 A 303 5
HET SO4 A 304 5
HET SO4 B 301 5
HET SO4 B 302 5
HET GOL B 303 6
HET CL B 304 1
HET SO4 B 305 5
HET SO4 B 306 5
HET SO4 B 307 5
HET SO4 C 301 5
HET GOL C 302 6
HET CL C 303 1
HET SO4 C 304 5
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 4 SO4 10(O4 S 2-)
FORMUL 5 CL 3(CL 1-)
FORMUL 10 GOL 2(C3 H8 O3)
FORMUL 19 HOH *1082(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 PRO A 210 SER A 213 5 4
HELIX 7 AA7 SER A 214 MET A 222 1 9
HELIX 8 AA8 ASN A 246 ASP A 263 1 18
HELIX 9 AA9 ASP A 265 ARG A 267 5 3
HELIX 10 AB1 TYR A 268 GLU A 274 1 7
HELIX 11 AB2 THR B 39 ALA B 45 1 7
HELIX 12 AB3 ARG B 90 LYS B 95 5 6
HELIX 13 AB4 TRP B 96 SER B 103 1 8
HELIX 14 AB5 GLN B 119 GLY B 139 1 21
HELIX 15 AB6 SER B 160 ASN B 173 1 14
HELIX 16 AB7 PRO B 210 SER B 213 5 4
HELIX 17 AB8 SER B 214 MET B 222 1 9
HELIX 18 AB9 ASN B 246 ASP B 263 1 18
HELIX 19 AC1 ASP B 265 ARG B 267 5 3
HELIX 20 AC2 TYR B 268 GLU B 274 1 7
HELIX 21 AC3 THR C 39 ALA C 45 1 7
HELIX 22 AC4 ARG C 90 LYS C 95 5 6
HELIX 23 AC5 TRP C 96 SER C 103 1 8
HELIX 24 AC6 GLN C 119 GLY C 139 1 21
HELIX 25 AC7 SER C 160 ASN C 173 1 14
HELIX 26 AC8 PRO C 210 SER C 213 5 4
HELIX 27 AC9 SER C 214 MET C 222 1 9
HELIX 28 AD1 ASN C 246 ASP C 263 1 18
HELIX 29 AD2 ASP C 265 ARG C 267 5 3
HELIX 30 AD3 TYR C 268 GLU C 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 81 O ILE A 109
SHEET 5 AA1 6 VAL A 149 GLY A 158 1 O ASP A 150 N VAL A 78
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 GLN A 228 N ILE A 200
SHEET 3 AA2 3 VAL A 281 ALA A 287 -1 O ASP A 283 N GLU A 231
SHEET 1 AA3 6 VAL B 52 THR B 56 0
SHEET 2 AA3 6 ALA B 65 PRO B 71 -1 O VAL B 68 N PHE B 55
SHEET 3 AA3 6 VAL B 107 ASP B 112 -1 O VAL B 108 N TYR B 69
SHEET 4 AA3 6 VAL B 78 VAL B 84 1 N ILE B 81 O ILE B 109
SHEET 5 AA3 6 VAL B 149 GLY B 158 1 O ASP B 150 N VAL B 78
SHEET 6 AA3 6 ALA B 178 ALA B 179 1 O ALA B 178 N VAL B 156
SHEET 1 AA4 3 THR B 198 CYS B 203 0
SHEET 2 AA4 3 LYS B 227 ILE B 232 1 O GLN B 228 N ILE B 200
SHEET 3 AA4 3 VAL B 281 ALA B 287 -1 O ARG B 285 N PHE B 229
SHEET 1 AA5 6 VAL C 52 THR C 56 0
SHEET 2 AA5 6 ALA C 65 PRO C 71 -1 O VAL C 68 N PHE C 55
SHEET 3 AA5 6 VAL C 107 ASP C 112 -1 O VAL C 108 N TYR C 69
SHEET 4 AA5 6 VAL C 78 VAL C 84 1 N ILE C 81 O ILE C 109
SHEET 5 AA5 6 VAL C 149 GLY C 158 1 O ASP C 150 N VAL C 78
SHEET 6 AA5 6 ALA C 178 ALA C 179 1 O ALA C 178 N VAL C 156
SHEET 1 AA6 3 THR C 198 CYS C 203 0
SHEET 2 AA6 3 LYS C 227 ILE C 232 1 O GLN C 228 N ILE C 200
SHEET 3 AA6 3 VAL C 281 ALA C 287 -1 O ASP C 283 N GLU C 231
SSBOND 1 CYS A 203 CYS A 239 1555 1555 2.07
SSBOND 2 CYS A 273 CYS A 289 1555 1555 2.03
SSBOND 3 CYS B 203 CYS B 239 1555 1555 2.06
SSBOND 4 CYS B 273 CYS B 289 1555 1555 2.04
SSBOND 5 CYS C 203 CYS C 239 1555 1555 2.07
SSBOND 6 CYS C 273 CYS C 289 1555 1555 2.05
CRYST1 52.379 233.957 164.808 90.00 90.00 90.00 C 2 2 21 24
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 0.019092 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004274 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006068 0.00000
TER 1974 HIS A 293
TER 3948 LEU B 291
TER 5903 LEU C 291
MASTER 478 0 15 30 27 0 0 6 6995 3 74 69
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