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HEADER HYDROLASE 11-AUG-24 9J5C
TITLE ESTS1 PHTHALATE ESTER DEGRADING ESTERASE FROM SULFOBACILLUS
TITLE 2 ACIDOPHILUS IN COMPLEX WITH DIETHYLHEXYL PHTHALATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA/BETA HYDROLASE FOLD-3 DOMAIN-CONTAINING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ESTS1 PHTHALATE ESTER DEGRADARING ESTERASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOBACILLUS ACIDOPHILUS DSM 10332;
SOURCE 3 ORGANISM_TAXID: 679936;
SOURCE 4 GENE: SULAC_0033;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008
KEYWDS ESTS1, PHTHALATE ESTER DEGRADING ESTERASE, DIETHYLHEXYL PHTHALATE,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.VERMA,P.KUMAR
REVDAT 1 25-DEC-24 9J5C 0
JRNL AUTH S.VERMA,S.CHOUDHARY,K.AMITH KUMAR,J.K.MAHTO,A.K.VAMSI K,
JRNL AUTH 2 I.MISHRA,V.B.PRAKASH,D.SIRCAR,S.TOMAR,A.KUMAR SHARMA,
JRNL AUTH 3 J.SINGLA,P.KUMAR
JRNL TITL MECHANISTIC AND STRUCTURAL INSIGHTS INTO ESTS1 ESTERASE: A
JRNL TITL 2 POTENT BROAD-SPECTRUM PHTHALATE DIESTER DEGRADING ENZYME.
JRNL REF STRUCTURE 2024
JRNL REFN ISSN 0969-2126
JRNL PMID 39642872
JRNL DOI 10.1016/J.STR.2024.11.006
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0352
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.45
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 8433
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.295
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.028
REMARK 3 FREE R VALUE TEST SET COUNT : 424
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 575
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 35
REMARK 3 BIN FREE R VALUE : 0.4500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2287
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 56
REMARK 3 SOLVENT ATOMS : 84
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 5.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.40500
REMARK 3 B22 (A**2) : 0.40500
REMARK 3 B33 (A**2) : -1.31300
REMARK 3 B12 (A**2) : 0.20200
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.448
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.384
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 41.144
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.887
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.750
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2441 ; 0.005 ; 0.012
REMARK 3 BOND LENGTHS OTHERS (A): 2237 ; 0.002 ; 0.016
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3331 ; 1.148 ; 1.665
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5218 ; 0.369 ; 1.563
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 304 ; 7.306 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 23 ; 9.299 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 361 ;15.429 ;10.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 361 ; 0.052 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2803 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 481 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 521 ; 0.216 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 50 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1171 ; 0.179 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 93 ; 0.179 ; 0.200
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): 1192 ; 0.000 ; 0.050
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1192 ; 0.000 ; 0.050
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1489 ; 0.000 ; 0.075
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1490 ; 0.000 ; 0.075
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1249 ; 0.000 ; 0.050
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1250 ; 0.000 ; 0.050
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1837 ; 0.000 ; 0.075
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1838 ; 0.000 ; 0.075
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): 4678 ; 0.012 ; 3.000
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 304
REMARK 3 RESIDUE RANGE : A 401 A 402
REMARK 3 ORIGIN FOR THE GROUP (A): -26.3822 -30.2149 -0.3103
REMARK 3 T TENSOR
REMARK 3 T11: 0.0283 T22: 0.0283
REMARK 3 T33: 0.0057 T12: 0.0132
REMARK 3 T13: -0.0042 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.3907 L22: 1.6396
REMARK 3 L33: 1.9836 L12: -0.3432
REMARK 3 L13: 0.1812 L23: 0.1342
REMARK 3 S TENSOR
REMARK 3 S11: 0.0240 S12: 0.0847 S13: 0.0590
REMARK 3 S21: -0.0456 S22: -0.0436 S23: 0.0287
REMARK 3 S31: -0.0830 S32: 0.1420 S33: 0.0197
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK BULK SOLVENT
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 THEIR
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 9J5C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-AUG-24.
REMARK 100 THE DEPOSITION ID IS D_1300050364.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JAN-23
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : RIGAKU HYPIX-6000HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO
REMARK 200 DATA SCALING SOFTWARE : CRYSALISPRO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8440
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 25.640
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.060
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 15.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.83
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 : 3.700
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM MALONATE, 0.1 M HEPES (PH 7.0),
REMARK 280 JEFFAMINE ED-2001, VAPOR DIFFUSION, TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-Y,X,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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 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 22.43600
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 22.43600
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 22.43600
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 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 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 PRO A 15
REMARK 465 PRO A 16
REMARK 465 LEU A 17
REMARK 465 ASN A 18
REMARK 465 ARG A 19
REMARK 465 GLU A 20
REMARK 465 GLY A 21
REMARK 465 LEU A 22
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 HG SER A 154 O4 TKU A 401 1.57
REMARK 500 OG SER A 154 H ALA A 155 1.57
REMARK 500 OG SER A 154 O4 TKU A 401 2.18
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 PHE A 85 -5.60 84.69
REMARK 500 PRO A 122 47.06 -105.83
REMARK 500 SER A 154 -108.72 67.43
REMARK 500 TYR A 181 62.68 32.54
REMARK 500 LYS A 193 -102.32 -53.12
REMARK 500 ARG A 194 -82.86 10.22
REMARK 500 ARG A 194 -81.15 8.15
REMARK 500 LEU A 201 -58.12 80.59
REMARK 500 SER A 227 79.14 -111.40
REMARK 500 TYR A 247 74.11 -100.10
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 LYS A 193 ARG A 194 147.87
REMARK 500 LYS A 193 ARG A 194 149.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 166 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 LYS A 193 13.17
REMARK 500
REMARK 500 REMARK: NULL
DBREF 9J5C A 1 304 UNP G8TV28 G8TV28_SULAD 1 304
SEQADV 9J5C HIS A -5 UNP G8TV28 EXPRESSION TAG
SEQADV 9J5C HIS A -4 UNP G8TV28 EXPRESSION TAG
SEQADV 9J5C HIS A -3 UNP G8TV28 EXPRESSION TAG
SEQADV 9J5C HIS A -2 UNP G8TV28 EXPRESSION TAG
SEQADV 9J5C HIS A -1 UNP G8TV28 EXPRESSION TAG
SEQADV 9J5C HIS A 0 UNP G8TV28 EXPRESSION TAG
SEQRES 1 A 310 HIS HIS HIS HIS HIS HIS MET PRO LEU ASP PRO ARG VAL
SEQRES 2 A 310 GLU GLN PHE LEU ALA GLN MET PRO PRO LEU ASN ARG GLU
SEQRES 3 A 310 GLY LEU SER LEU ALA GLU ALA ARG GLN GLN PHE LYS GLN
SEQRES 4 A 310 GLY ALA LEU LEU LEU ASP GLN MET VAL PRO PRO PRO PRO
SEQRES 5 A 310 VAL ASP THR GLU ASP GLY THR VAL VAL THR THR HIS GLY
SEQRES 6 A 310 PRO VAL ARG ILE ARG ARG TYR ILE PRO ASP ARG LEU ARG
SEQRES 7 A 310 PHE SER HIS PRO LEU VAL PHE TYR HIS GLY GLY GLY PHE
SEQRES 8 A 310 VAL PHE GLY ASP ILE ASP THR HIS HIS GLY LEU VAL ALA
SEQRES 9 A 310 ARG LEU CYS GLN THR VAL GLY ALA THR VAL ILE SER VAL
SEQRES 10 A 310 ASP TYR SER LEU ALA PRO GLU ALA LYS PHE PRO VAL PRO
SEQRES 11 A 310 VAL ALA GLU CYS ILE ASP VAL ALA ARG TRP ALA ALA HIS
SEQRES 12 A 310 GLU ALA PRO GLY TRP GLY LEU LYS PRO SER ILE VAL VAL
SEQRES 13 A 310 ALA GLY ASP SER ALA GLY GLY ASN LEU ALA ALA VAL VAL
SEQRES 14 A 310 SER GLN ARG ALA LYS ASP GLU SER LEU PRO ILE ALA ALA
SEQRES 15 A 310 GLN LEU LEU PHE TYR PRO ALA LEU ASP MET VAL HIS GLU
SEQRES 16 A 310 THR PRO SER LYS ARG ASP PHE ALA ARG GLY TYR LEU LEU
SEQRES 17 A 310 GLU ALA ASP ALA MET GLN TRP PHE GLY GLU GLN TYR LEU
SEQRES 18 A 310 ARG THR PRO ASP ASP VAL SER HIS PRO TRP ALA SER PRO
SEQRES 19 A 310 ALA LEU SER PRO ASP LEU THR GLY LEU PRO PRO ALA LEU
SEQRES 20 A 310 VAL ILE THR ALA GLU TYR ASP PRO LEU ARG ASP GLU GLY
SEQRES 21 A 310 GLU ALA TYR ALA GLU ALA LEU ARG ALA ALA GLY VAL PRO
SEQRES 22 A 310 THR GLU GLN ILE ARG PHE ASP GLY MET ILE HIS GLY PHE
SEQRES 23 A 310 MET THR MET PRO ILE PHE PRO GLN MET GLU ALA ALA ILE
SEQRES 24 A 310 GLU ALA VAL ALA ARG PHE LEU GLU ARG ILE ASP
HET TKU A 401 66
HET TKU A 402 66
HETNAM TKU ~{O}1-[(2~{R})-2-ETHYLHEXYL] ~{O}2-[(2~{S})-2-
HETNAM 2 TKU ETHYLHEXYL] BENZENE-1,2-DICARBOXYLATE
HETSYN TKU BIS(2-ETHYLHEXYL) PHTHALATE; DIETHYLHEXYL PHTHALATE; 1-
HETSYN 2 TKU O-[(2S)-2-ETHYLHEXYL] 2-O-[(2R)-2-ETHYLHEXYL] BENZENE-
HETSYN 3 TKU 1,2-DICARBOXYLATE
FORMUL 2 TKU 2(C24 H38 O4)
FORMUL 4 HOH *84(H2 O)
HELIX 1 AA1 ASP A 4 GLN A 13 1 10
HELIX 2 AA2 LEU A 24 VAL A 42 1 19
HELIX 3 AA3 HIS A 93 GLY A 105 1 13
HELIX 4 AA4 PRO A 122 ALA A 139 1 18
HELIX 5 AA5 PRO A 140 GLY A 143 5 4
HELIX 6 AA6 SER A 154 ALA A 167 1 14
HELIX 7 AA7 THR A 190 PHE A 196 1 7
HELIX 8 AA8 GLU A 203 LEU A 215 1 13
HELIX 9 AA9 THR A 217 HIS A 223 5 7
HELIX 10 AB1 SER A 227 SER A 231 5 5
HELIX 11 AB2 LEU A 250 ALA A 264 1 15
HELIX 12 AB3 GLY A 279 MET A 283 5 5
HELIX 13 AB4 PRO A 287 ARG A 302 1 16
SHEET 1 AA1 8 ASP A 48 THR A 56 0
SHEET 2 AA1 8 GLY A 59 ILE A 67 -1 O ILE A 63 N GLY A 52
SHEET 3 AA1 8 VAL A 108 ASP A 112 -1 O VAL A 108 N TYR A 66
SHEET 4 AA1 8 LEU A 77 TYR A 80 1 N PHE A 79 O VAL A 111
SHEET 5 AA1 8 ILE A 148 ASP A 153 1 O ALA A 151 N TYR A 80
SHEET 6 AA1 8 ILE A 174 PHE A 180 1 O ALA A 175 N ILE A 148
SHEET 7 AA1 8 ALA A 240 ALA A 245 1 O LEU A 241 N LEU A 179
SHEET 8 AA1 8 THR A 268 PHE A 273 1 O ILE A 271 N THR A 244
CISPEP 1 ALA A 116 PRO A 117 0 2.32
CISPEP 2 PHE A 121 PRO A 122 0 -2.89
CRYST1 108.258 108.258 44.872 90.00 90.00 120.00 P 63 6
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 0.009237 0.005333 0.000000 0.00000
SCALE2 0.000000 0.010666 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022286 0.00000
TER 4598 ASP A 304
MASTER 364 0 2 13 8 0 0 6 2427 1 132 24
END |