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HEADER TRANSFERASE 02-FEB-16 5HZ2
TITLE CRYSTAL STRUCTURE OF PHAC1 FROM RALSTONIA EUTROPHA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLY-BETA-HYDROXYBUTYRATE POLYMERASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (UNP RESIDUES 202-589);
COMPND 5 SYNONYM: PHB POLYMERASE,PHB SYNTHASE,POLY(3-HYDROXYALKANOATE)
COMPND 6 POLYMERASE,PHA POLYMERASE,POLY(3-HYDROXYBUTYRATE) POLYMERASE,
COMPND 7 POLYHYDROXYALKANOATE SYNTHASE,PHA SYNTHASE;
COMPND 8 EC: 2.3.1.-;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CUPRIAVIDUS NECATOR;
SOURCE 3 ORGANISM_TAXID: 381666;
SOURCE 4 STRAIN: ATCC 17699 / H16 / DSM 428 / STANIER 337;
SOURCE 5 GENE: PHBC, H16_A1437;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
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: PET30A
KEYWDS TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.KIM,K.-J.KIM
REVDAT 1 07-DEC-16 5HZ2 0
JRNL AUTH J.KIM,Y.J.KIM,S.Y.CHOI,S.Y.LEE,K.J.KIM
JRNL TITL CRYSTAL STRUCTURE OF RALSTONIA EUTROPHA POLYHYDROXYALKANOATE
JRNL TITL 2 SYNTHASE C-TERMINAL DOMAIN AND REACTION MECHANISMS.
JRNL REF BIOTECHNOL J 2016
JRNL REFN ESSN 1860-7314
JRNL PMID 27808482
JRNL DOI 10.1002/BIOT.201600648
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 38300
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) : 0.153
REMARK 3 R VALUE (WORKING SET) : 0.152
REMARK 3 FREE R VALUE : 0.190
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2001
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2688
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.2480
REMARK 3 BIN FREE R VALUE SET COUNT : 130
REMARK 3 BIN FREE R VALUE : 0.2810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3013
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 47
REMARK 3 SOLVENT ATOMS : 280
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.21000
REMARK 3 B22 (A**2) : -0.83000
REMARK 3 B33 (A**2) : -0.37000
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): 0.102
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.103
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.477
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.961
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3142 ; 0.020 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2919 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4306 ; 1.952 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6686 ; 1.196 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 387 ; 7.207 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 137 ;34.994 ;23.504
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 448 ;14.378 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;15.652 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 478 ; 0.192 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3556 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 742 ; 0.002 ; 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): 1551 ; 2.611 ; 2.766
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1550 ; 2.600 ; 2.765
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1937 ; 3.559 ; 4.135
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
REMARK 4
REMARK 4 5HZ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000217987.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-13; 16-OCT-13
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : PAL/PLS; PAL/PLS
REMARK 200 BEAMLINE : 7A (6B, 6C1); 7A (6B, 6C1)
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9798; 1.0072
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR;
REMARK 200 DOUBLE CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : RH COATED TORROIDAL MIRROR; RH
REMARK 200 COATED TORROIDAL MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270; ADSC QUANTUM
REMARK 200 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40301
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 (%) : 98.1
REMARK 200 DATA REDUNDANCY : 9.800
REMARK 200 R MERGE (I) : 0.05400
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.7000
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 (%) : 93.5
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.26100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 51.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, HEPES, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
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 36.62300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 43.92800
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 68.23950
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.62300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 43.92800
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 68.23950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.62300
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 43.92800
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 68.23950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.62300
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 43.92800
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 68.23950
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 26870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -522.0 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 73.24600
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -1.000000 0.000000 0.000000 73.24600
REMARK 350 BIOMT2 3 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 -1.000000 136.47900
REMARK 350 BIOMT1 4 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 4 0.000000 0.000000 -1.000000 136.47900
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 LEU A 590
REMARK 465 GLN A 591
REMARK 465 HIS A 592
REMARK 465 HIS A 593
REMARK 465 HIS A 594
REMARK 465 HIS A 595
REMARK 465 HIS A 596
REMARK 465 HIS A 597
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 248 177.47 77.44
REMARK 500 ASP A 254 52.44 -142.34
REMARK 500 ALA A 296 -63.27 -121.60
REMARK 500 CYS A 319 -130.93 56.93
REMARK 500 THR A 444 -80.37 -112.41
REMARK 500 ASN A 497 -172.21 78.59
REMARK 500 SER A 506 -164.90 79.61
REMARK 500 ARG A 521 -155.35 66.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 609
DBREF 5HZ2 A 202 589 UNP P23608 PHBC_CUPNH 202 589
SEQADV 5HZ2 LEU A 590 UNP P23608 EXPRESSION TAG
SEQADV 5HZ2 GLN A 591 UNP P23608 EXPRESSION TAG
SEQADV 5HZ2 HIS A 592 UNP P23608 EXPRESSION TAG
SEQADV 5HZ2 HIS A 593 UNP P23608 EXPRESSION TAG
SEQADV 5HZ2 HIS A 594 UNP P23608 EXPRESSION TAG
SEQADV 5HZ2 HIS A 595 UNP P23608 EXPRESSION TAG
SEQADV 5HZ2 HIS A 596 UNP P23608 EXPRESSION TAG
SEQADV 5HZ2 HIS A 597 UNP P23608 EXPRESSION TAG
SEQRES 1 A 396 ALA PHE GLU VAL GLY ARG ASN VAL ALA VAL THR GLU GLY
SEQRES 2 A 396 ALA VAL VAL PHE GLU ASN GLU TYR PHE GLN LEU LEU GLN
SEQRES 3 A 396 TYR LYS PRO LEU THR ASP LYS VAL HIS ALA ARG PRO LEU
SEQRES 4 A 396 LEU MET VAL PRO PRO CYS ILE ASN LYS TYR TYR ILE LEU
SEQRES 5 A 396 ASP LEU GLN PRO GLU SER SER LEU VAL ARG HIS VAL VAL
SEQRES 6 A 396 GLU GLN GLY HIS THR VAL PHE LEU VAL SER TRP ARG ASN
SEQRES 7 A 396 PRO ASP ALA SER MET ALA GLY SER THR TRP ASP ASP TYR
SEQRES 8 A 396 ILE GLU HIS ALA ALA ILE ARG ALA ILE GLU VAL ALA ARG
SEQRES 9 A 396 ASP ILE SER GLY GLN ASP LYS ILE ASN VAL LEU GLY PHE
SEQRES 10 A 396 CYS VAL GLY GLY THR ILE VAL SER THR ALA LEU ALA VAL
SEQRES 11 A 396 LEU ALA ALA ARG GLY GLU HIS PRO ALA ALA SER VAL THR
SEQRES 12 A 396 LEU LEU THR THR LEU LEU ASP PHE ALA ASP THR GLY ILE
SEQRES 13 A 396 LEU ASP VAL PHE VAL ASP GLU GLY HIS VAL GLN LEU ARG
SEQRES 14 A 396 GLU ALA THR LEU GLY GLY GLY ALA GLY ALA PRO CYS ALA
SEQRES 15 A 396 LEU LEU ARG GLY LEU GLU LEU ALA ASN THR PHE SER PHE
SEQRES 16 A 396 LEU ARG PRO ASN ASP LEU VAL TRP ASN TYR VAL VAL ASP
SEQRES 17 A 396 ASN TYR LEU LYS GLY ASN THR PRO VAL PRO PHE ASP LEU
SEQRES 18 A 396 LEU PHE TRP ASN GLY ASP ALA THR ASN LEU PRO GLY PRO
SEQRES 19 A 396 TRP TYR CYS TRP TYR LEU ARG HIS THR TYR LEU GLN ASN
SEQRES 20 A 396 GLU LEU LYS VAL PRO GLY LYS LEU THR VAL CYS GLY VAL
SEQRES 21 A 396 PRO VAL ASP LEU ALA SER ILE ASP VAL PRO THR TYR ILE
SEQRES 22 A 396 TYR GLY SER ARG GLU ASP HIS ILE VAL PRO TRP THR ALA
SEQRES 23 A 396 ALA TYR ALA SER THR ALA LEU LEU ALA ASN LYS LEU ARG
SEQRES 24 A 396 PHE VAL LEU GLY ALA SER GLY HIS ILE ALA GLY VAL ILE
SEQRES 25 A 396 ASN PRO PRO ALA LYS ASN LYS ARG SER HIS TRP THR ASN
SEQRES 26 A 396 ASP ALA LEU PRO GLU SER PRO GLN GLN TRP LEU ALA GLY
SEQRES 27 A 396 ALA ILE GLU HIS HIS GLY SER TRP TRP PRO ASP TRP THR
SEQRES 28 A 396 ALA TRP LEU ALA GLY GLN ALA GLY ALA LYS ARG ALA ALA
SEQRES 29 A 396 PRO ALA ASN TYR GLY ASN ALA ARG TYR ARG ALA ILE GLU
SEQRES 30 A 396 PRO ALA PRO GLY ARG TYR VAL LYS ALA LYS ALA LEU GLN
SEQRES 31 A 396 HIS HIS HIS HIS HIS HIS
HET GOL A 601 6
HET GOL A 602 6
HET SO4 A 603 5
HET SO4 A 604 5
HET SO4 A 605 5
HET SO4 A 606 5
HET SO4 A 607 5
HET SO4 A 608 5
HET SO4 A 609 5
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 4 SO4 7(O4 S 2-)
FORMUL 11 HOH *280(H2 O)
HELIX 1 AA1 LYS A 249 LEU A 255 5 7
HELIX 2 AA2 GLN A 256 SER A 259 5 4
HELIX 3 AA3 SER A 260 GLN A 268 1 9
HELIX 4 AA4 ASP A 281 ALA A 285 5 5
HELIX 5 AA5 THR A 288 ALA A 296 1 9
HELIX 6 AA6 ALA A 296 GLY A 309 1 14
HELIX 7 AA7 CYS A 319 ARG A 335 1 17
HELIX 8 AA8 LEU A 358 VAL A 362 5 5
HELIX 9 AA9 PRO A 381 LEU A 385 5 5
HELIX 10 AB1 ASP A 401 THR A 416 1 16
HELIX 11 AB2 PRO A 419 ASP A 428 1 10
HELIX 12 AB3 GLY A 434 THR A 444 1 11
HELIX 13 AB4 ASP A 464 ILE A 468 5 5
HELIX 14 AB5 PRO A 484 ALA A 490 1 7
HELIX 15 AB6 SER A 491 LEU A 494 5 4
HELIX 16 AB7 PRO A 515 ASN A 519 5 5
HELIX 17 AB8 SER A 532 GLY A 539 1 8
HELIX 18 AB9 TRP A 547 ALA A 559 1 13
HELIX 19 AC1 ARG A 583 ALA A 587 5 5
SHEET 1 AA111 ILE A 541 HIS A 544 0
SHEET 2 AA111 SER A 522 THR A 525 -1 N HIS A 523 O HIS A 543
SHEET 3 AA111 LEU A 499 GLY A 504 -1 N LEU A 503 O TRP A 524
SHEET 4 AA111 THR A 472 SER A 477 1 N ILE A 474 O ARG A 500
SHEET 5 AA111 ALA A 340 LEU A 346 1 N LEU A 345 O TYR A 473
SHEET 6 AA111 ILE A 313 PHE A 318 1 N GLY A 317 O LEU A 346
SHEET 7 AA111 LEU A 240 VAL A 243 1 N VAL A 243 O LEU A 316
SHEET 8 AA111 VAL A 272 TRP A 277 1 O PHE A 273 N MET A 242
SHEET 9 AA111 PHE A 223 TYR A 228 -1 N LEU A 226 O LEU A 274
SHEET 10 AA111 GLY A 214 GLU A 219 -1 N VAL A 217 O LEU A 225
SHEET 11 AA111 GLU A 578 PRO A 579 -1 O GLU A 578 N VAL A 216
SHEET 1 AA2 2 LYS A 234 HIS A 236 0
SHEET 2 AA2 2 LYS A 562 ALA A 564 -1 O ARG A 563 N VAL A 235
SHEET 1 AA3 2 LEU A 388 ALA A 391 0
SHEET 2 AA3 2 THR A 430 PRO A 433 -1 O LEU A 432 N GLU A 389
SHEET 1 AA4 2 THR A 457 VAL A 458 0
SHEET 2 AA4 2 VAL A 461 PRO A 462 -1 O VAL A 461 N VAL A 458
SSBOND 1 CYS A 382 CYS A 438 1555 1555 2.19
CISPEP 1 ALA A 580 PRO A 581 0 6.31
SITE 1 AC1 8 HIS A 366 VAL A 367 ALA A 510 ILE A 513
SITE 2 AC1 8 ASN A 514 ARG A 521 GOL A 602 HOH A 922
SITE 1 AC2 8 LEU A 255 HIS A 366 PRO A 419 ASP A 421
SITE 2 AC2 8 ALA A 510 GOL A 601 HOH A 707 HOH A 789
SITE 1 AC3 7 PRO A 381 CYS A 382 TRP A 439 ARG A 442
SITE 2 AC3 7 HIS A 443 SO4 A 609 HOH A 748
SITE 1 AC4 7 ALA A 202 PHE A 218 ASN A 220 ARG A 299
SITE 2 AC4 7 HOH A 773 HOH A 832 HOH A 918
SITE 1 AC5 4 THR A 232 ASP A 233 LYS A 234 HOH A 856
SITE 1 AC6 5 ARG A 478 TRP A 485 GLN A 534 HOH A 746
SITE 2 AC6 5 HOH A 906
SITE 1 AC7 6 ILE A 247 CYS A 319 TYR A 440 TYR A 445
SITE 2 AC7 6 ILE A 482 HOH A 705
SITE 1 AC8 4 PRO A 566 ALA A 567 ASN A 568 HOH A 901
SITE 1 AC9 7 ALA A 378 GLY A 379 ARG A 442 HIS A 443
SITE 2 AC9 7 GLN A 447 SO4 A 603 HOH A 777
CRYST1 73.246 87.856 136.479 90.00 90.00 90.00 I 2 2 2 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 0.013653 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011382 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007327 0.00000
TER 3014 ALA A 589
MASTER 343 0 9 19 17 0 16 6 3340 1 49 31
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