| content |
HEADER HYDROLASE 19-APR-17 5XH2
TITLE CRYSTAL STRUCTURE OF A NOVEL PET HYDROLASE R103G/S131A MUTANT IN
TITLE 2 COMPLEX WITH PNP FROM IDEONELLA SAKAIENSIS 201-F6
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY(ETHYLENE TEREPHTHALATE) HYDROLASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PETASE;
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 201-F6);
SOURCE 3 ORGANISM_TAXID: 1547922;
SOURCE 4 STRAIN: 201-F6;
SOURCE 5 GENE: ISF6_4831;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS POLY(ETHYLENE TEREPHTHALATE) HYDROLASE, SUBSTRATE BINDING, INHIBITOR,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.HAN,W.D.LIU,Y.Y.ZHENG,C.C.CHEN,R.T.GUO
REVDAT 1 20-DEC-17 5XH2 0
JRNL AUTH X.HAN,W.D.LIU,J.W.HUANG,J.MA,Y.Y.ZHENG,T.P.KO,L.XU,
JRNL AUTH 2 Y.S.CHENG,C.C.CHEN,R.T.GUO
JRNL TITL STRUCTURAL INSIGHT INTO CATALYTIC MECHANISM OF PET HYDROLASE
JRNL REF NAT COMMUN 2017
JRNL REFN ESSN 2041-1723
JRNL DOI 10.1038/S41467-017-02255-Z
REMARK 2
REMARK 2 RESOLUTION. 1.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 66256
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) : 0.100
REMARK 3 R VALUE (WORKING SET) : 0.098
REMARK 3 FREE R VALUE : 0.125
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 3391
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) : 1.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.23
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4705
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.99
REMARK 3 BIN R VALUE (WORKING SET) : 0.1030
REMARK 3 BIN FREE R VALUE SET COUNT : 223
REMARK 3 BIN FREE R VALUE : 0.1400
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1912
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 30
REMARK 3 SOLVENT ATOMS : 365
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 10.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.30000
REMARK 3 B22 (A**2) : 0.29000
REMARK 3 B33 (A**2) : 0.01000
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): 0.027
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.029
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.016
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.773
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.984
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.979
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2028 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1766 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2782 ; 1.489 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4127 ; 0.821 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 280 ; 6.596 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 76 ;32.729 ;23.684
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 295 ;10.441 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;17.151 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 309 ; 0.106 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2328 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 416 ; 0.003 ; 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): 3794 ; 7.103 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 224 ;26.525 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3882 ; 9.793 ; 5.000
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 5XH2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1300003520.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-APR-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSRRC
REMARK 200 BEAMLINE : TPS 05A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9998
REMARK 200 MONOCHROMATOR : LN2 COOLED SI(111) DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300-HS
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000, HKL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69716
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.200
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.000
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 10.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.24
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.9
REMARK 200 DATA REDUNDANCY IN SHELL : 7.60
REMARK 200 R MERGE FOR SHELL (I) : 0.21200
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: PHASER
REMARK 200 STARTING MODEL: 4WFI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, NACL, HEPES, PH 7.5,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K
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 25.39200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.18650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 25.76600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.18650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.39200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 25.76600
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: 170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 SER A 261
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 637 O HOH A 659 1.61
REMARK 500 O HOH A 438 O HOH A 506 1.61
REMARK 500 O HOH A 569 O HOH A 704 1.63
REMARK 500 O HOH A 484 O HOH A 608 1.77
REMARK 500 O HOH A 617 O HOH A 656 2.04
REMARK 500 O HOH A 412 O HOH A 595 2.09
REMARK 500 O HOH A 581 O HOH A 585 2.11
REMARK 500 O HOH A 658 O HOH A 709 2.13
REMARK 500 O HOH A 439 O HOH A 629 2.14
REMARK 500 O HOH A 414 O HOH A 645 2.16
REMARK 500 O HOH A 628 O HOH A 675 2.16
REMARK 500 O HOH A 413 O HOH A 644 2.16
REMARK 500 O HOH A 579 O HOH A 649 2.17
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 695 O HOH A 702 3545 1.11
REMARK 500 O HOH A 612 O HOH A 656 4555 1.88
REMARK 500 O HOH A 660 O HOH A 703 4555 1.99
REMARK 500 O HOH A 469 O HOH A 703 4555 2.06
REMARK 500 O HOH A 476 O HOH A 695 3555 2.10
REMARK 500 O HOH A 627 O HOH A 726 4555 2.11
REMARK 500 O HOH A 461 O HOH A 653 3545 2.17
REMARK 500 O HOH A 738 O HOH A 755 4555 2.19
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 ASN A 44 37.79 -145.85
REMARK 500 THR A 59 -12.31 76.38
REMARK 500 ALA A 131 -120.08 67.01
REMARK 500 SER A 185 -85.30 -129.14
REMARK 500 SER A 185 -82.62 -131.00
REMARK 500 SER A 185 -86.56 -129.00
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 765 DISTANCE = 6.94 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO A 305
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5XH3 RELATED DB: PDB
DBREF1 5XH2 A 1 261 UNP PETH_IDESA
DBREF2 5XH2 A A0A0K8P6T7 30 290
SEQADV 5XH2 MET A 0 UNP A0A0K8P6T EXPRESSION TAG
SEQADV 5XH2 GLY A 103 UNP A0A0K8P6T ARG 132 ENGINEERED MUTATION
SEQADV 5XH2 ALA A 131 UNP A0A0K8P6T SER 160 ENGINEERED MUTATION
SEQRES 1 A 262 MET ASN PRO TYR ALA ARG GLY PRO ASN PRO THR ALA ALA
SEQRES 2 A 262 SER LEU GLU ALA SER ALA GLY PRO PHE THR VAL ARG SER
SEQRES 3 A 262 PHE THR VAL SER ARG PRO SER GLY TYR GLY ALA GLY THR
SEQRES 4 A 262 VAL TYR TYR PRO THR ASN ALA GLY GLY THR VAL GLY ALA
SEQRES 5 A 262 ILE ALA ILE VAL PRO GLY TYR THR ALA ARG GLN SER SER
SEQRES 6 A 262 ILE LYS TRP TRP GLY PRO ARG LEU ALA SER HIS GLY PHE
SEQRES 7 A 262 VAL VAL ILE THR ILE ASP THR ASN SER THR LEU ASP GLN
SEQRES 8 A 262 PRO SER SER ARG SER SER GLN GLN MET ALA ALA LEU GLY
SEQRES 9 A 262 GLN VAL ALA SER LEU ASN GLY THR SER SER SER PRO ILE
SEQRES 10 A 262 TYR GLY LYS VAL ASP THR ALA ARG MET GLY VAL MET GLY
SEQRES 11 A 262 TRP ALA MET GLY GLY GLY GLY SER LEU ILE SER ALA ALA
SEQRES 12 A 262 ASN ASN PRO SER LEU LYS ALA ALA ALA PRO GLN ALA PRO
SEQRES 13 A 262 TRP ASP SER SER THR ASN PHE SER SER VAL THR VAL PRO
SEQRES 14 A 262 THR LEU ILE PHE ALA CYS GLU ASN ASP SER ILE ALA PRO
SEQRES 15 A 262 VAL ASN SER SER ALA LEU PRO ILE TYR ASP SER MET SER
SEQRES 16 A 262 ARG ASN ALA LYS GLN PHE LEU GLU ILE ASN GLY GLY SER
SEQRES 17 A 262 HIS SER CYS ALA ASN SER GLY ASN SER ASN GLN ALA LEU
SEQRES 18 A 262 ILE GLY LYS LYS GLY VAL ALA TRP MET LYS ARG PHE MET
SEQRES 19 A 262 ASP ASN ASP THR ARG TYR SER THR PHE ALA CYS GLU ASN
SEQRES 20 A 262 PRO ASN SER THR ARG VAL SER ASP PHE ARG THR ALA ASN
SEQRES 21 A 262 CYS SER
HET SO4 A 301 5
HET SO4 A 302 5
HET SO4 A 303 5
HET SO4 A 304 5
HET NPO A 305 10
HETNAM SO4 SULFATE ION
HETNAM NPO P-NITROPHENOL
FORMUL 2 SO4 4(O4 S 2-)
FORMUL 6 NPO C6 H5 N O3
FORMUL 7 HOH *365(H2 O)
HELIX 1 AA1 THR A 10 ALA A 16 1 7
HELIX 2 AA2 ARG A 61 LYS A 66 5 6
HELIX 3 AA3 TRP A 67 SER A 74 1 8
HELIX 4 AA4 GLN A 90 GLY A 110 1 21
HELIX 5 AA5 ALA A 131 ASN A 144 1 14
HELIX 6 AA6 SER A 185 MET A 193 1 9
HELIX 7 AA7 ASN A 217 ASP A 234 1 18
HELIX 8 AA8 ASP A 236 ARG A 238 5 3
HELIX 9 AA9 TYR A 239 GLU A 245 1 7
SHEET 1 AA1 6 VAL A 23 THR A 27 0
SHEET 2 AA1 6 ALA A 36 PRO A 42 -1 O VAL A 39 N PHE A 26
SHEET 3 AA1 6 VAL A 78 ASP A 83 -1 O VAL A 79 N TYR A 40
SHEET 4 AA1 6 VAL A 49 VAL A 55 1 N ILE A 52 O ILE A 80
SHEET 5 AA1 6 VAL A 120 GLY A 129 1 O ASP A 121 N VAL A 49
SHEET 6 AA1 6 ALA A 149 ALA A 150 1 O ALA A 149 N VAL A 127
SHEET 1 AA2 3 THR A 169 CYS A 174 0
SHEET 2 AA2 3 LYS A 198 ILE A 203 1 O GLN A 199 N ILE A 171
SHEET 3 AA2 3 VAL A 252 ALA A 258 -1 O ASP A 254 N GLU A 202
SSBOND 1 CYS A 174 CYS A 210 1555 1555 2.03
SSBOND 2 CYS A 244 CYS A 260 1555 1555 2.11
SITE 1 AC1 8 TYR A 190 ARG A 256 THR A 257 HOH A 480
SITE 2 AC1 8 HOH A 492 HOH A 501 HOH A 523 HOH A 542
SITE 1 AC2 6 GLN A 90 PRO A 91 SER A 92 HOH A 408
SITE 2 AC2 6 HOH A 435 HOH A 472
SITE 1 AC3 7 GLY A 206 SER A 207 SER A 209 CYS A 210
SITE 2 AC3 7 HOH A 404 HOH A 414 HOH A 578
SITE 1 AC4 9 ALA A 60 ARG A 61 SER A 63 SER A 64
SITE 2 AC4 9 HOH A 402 HOH A 543 HOH A 564 HOH A 607
SITE 3 AC4 9 HOH A 611
SITE 1 AC5 9 SER A 32 GLY A 103 GLN A 104 SER A 107
SITE 2 AC5 9 MET A 132 TRP A 156 ILE A 179 HOH A 497
SITE 3 AC5 9 HOH A 511
CRYST1 50.784 51.532 84.373 90.00 90.00 90.00 P 21 21 21 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 0.019691 0.000000 0.000000 0.00000
SCALE2 0.000000 0.019405 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011852 0.00000
TER 1946 CYS A 260
MASTER 355 0 5 9 9 0 12 6 2307 1 34 21
END |