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HEADER HYDROLASE 29-OCT-20 7ATD
TITLE STRUCTURE OF INACTIVE ESTD11 S144A IN COMPLEX WITH METHYL-NAPROXEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTD11 S144A;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;
SOURCE 3 ORGANISM_TAXID: 77133;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PET22
KEYWDS ESTERASE HORMONE-SENSITIVE LIPASE METAGENOME LIBRARY CRYSTAL
KEYWDS 2 STRUCTURE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.MIGUEL-RUANO,I.RIVERA,J.A.HERMOSO
REVDAT 1 03-MAR-21 7ATD 0
JRNL AUTH V.MIGUEL-RUANO,I.RIVERA,J.RAJKOVIC,K.KNAPIK,A.TORRADO,
JRNL AUTH 2 J.M.OTERO,E.BENEVENTI,M.BECERRA,M.SANCHEZ-COSTA,A.HIDALGO,
JRNL AUTH 3 J.BERENGUER,M.I.GONZALEZ-SISO,J.CRUCES,M.L.RUA,J.A.HERMOSO
JRNL TITL BIOCHEMICAL AND STRUCTURAL CHARACTERIZATION OF A NOVEL
JRNL TITL 2 THERMOPHILIC ESTERASE ESTD11 PROVIDE CATALYTIC INSIGHTS FOR
JRNL TITL 3 THE HSL FAMILY
JRNL REF COMPUT STRUCT BIOTECHNOL J 2021
JRNL REFN ESSN 2001-0370
JRNL DOI 10.1016/J.CSBJ.2021.01.047
REMARK 2
REMARK 2 RESOLUTION. 1.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0267
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.48
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 94720
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 : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 5071
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) : 1.45
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6929
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.3250
REMARK 3 BIN FREE R VALUE SET COUNT : 340
REMARK 3 BIN FREE R VALUE : 0.3160
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4494
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 673
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 18.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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): 0.067
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.068
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.500
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.974
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4878 ; 0.008 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 4700 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6670 ; 1.526 ; 1.651
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10795 ; 1.452 ; 1.577
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 638 ; 5.951 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 254 ;28.024 ;20.236
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 781 ;13.549 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 52 ;20.228 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 628 ; 0.082 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5677 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1101 ; 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): 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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 2 296 B 2 296 9638 0.100 0.050
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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 7ATD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-OCT-20.
REMARK 100 THE DEPOSITION ID IS D_1292112052.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-MAR-17
REMARK 200 TEMPERATURE (KELVIN) : 291
REMARK 200 PH : 5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALBA
REMARK 200 BEAMLINE : XALOC
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.072
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 99895
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.450
REMARK 200 RESOLUTION RANGE LOW (A) : 48.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 10.20
REMARK 200 R MERGE (I) : 0.14200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 8.8000
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) : 1.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 10.30
REMARK 200 R MERGE FOR SHELL (I) : 1.75200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.200
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: 7AT0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.19
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.2M SODIUM FORMATE + 0.1M CITRATE PH
REMARK 280 5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K
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 23.92300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.57300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.12150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.57300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 23.92300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.12150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 MET B 1
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 1415 O HOH A 1640 1.70
REMARK 500 O HOH B 1501 O HOH B 1533 1.77
REMARK 500 O HOH B 1568 O HOH B 1667 1.78
REMARK 500 O HOH B 1555 O HOH B 1682 1.78
REMARK 500 O HOH B 1613 O HOH B 1667 1.88
REMARK 500 O HOH B 1501 O HOH B 1527 2.02
REMARK 500 O HOH B 1557 O HOH B 1628 2.07
REMARK 500 O HOH B 1401 O HOH B 1577 2.07
REMARK 500 O HOH A 1407 O HOH A 1646 2.12
REMARK 500 O HOH A 1434 O HOH A 1648 2.12
REMARK 500 O HOH A 1404 O HOH A 1573 2.13
REMARK 500 O HOH B 1601 O HOH B 1646 2.17
REMARK 500 O ARG A 17 O HOH A 1401 2.17
REMARK 500 O HOH A 1417 O HOH A 1710 2.18
REMARK 500 O HOH B 1423 O HOH B 1508 2.18
REMARK 500 O HOH A 1473 O HOH A 1726 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 B 1404 O HOH B 1546 3644 2.06
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 ALA A 144 -123.25 60.83
REMARK 500 PRO A 219 0.05 -69.87
REMARK 500 ALA A 237 51.42 -95.80
REMARK 500 ASP A 265 -0.24 74.58
REMARK 500 ALA B 144 -122.88 61.24
REMARK 500 ALA B 237 47.49 -98.30
REMARK 500 ASP B 265 -2.51 75.92
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 A1752 DISTANCE = 6.30 ANGSTROMS
REMARK 525 HOH A1753 DISTANCE = 6.37 ANGSTROMS
REMARK 525 HOH A1754 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH A1755 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH A1756 DISTANCE = 8.05 ANGSTROMS
REMARK 525 HOH A1757 DISTANCE = 9.65 ANGSTROMS
REMARK 525 HOH B1716 DISTANCE = 6.71 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 1307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1310
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1311
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1312
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1313
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1314
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue RXH B 1301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 1302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 1303
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 7AT0 RELATED DB: PDB
REMARK 900 RELATED ID: 7AT2 RELATED DB: PDB
REMARK 900 RELATED ID: 7AT3 RELATED DB: PDB
REMARK 900 RELATED ID: 7AT4 RELATED DB: PDB
DBREF 7ATD A 1 296 PDB 7ATD 7ATD 1 296
DBREF 7ATD B 1 296 PDB 7ATD 7ATD 1 296
SEQRES 1 A 296 MET ALA SER GLU ALA LEU THR MET ILE VAL ASN LEU LEU
SEQRES 2 A 296 ARG SER GLN ARG PRO LEU GLN GLU PRO THR VAL GLU GLN
SEQRES 3 A 296 MET ARG ALA GLY LEU GLU ALA MET ALA GLN MET SER PRO
SEQRES 4 A 296 LEU PRO ALA ASP VAL GLU LEU THR THR VAL ASP ALA GLY
SEQRES 5 A 296 GLY VAL PRO GLY ALA TRP VAL ARG VAL PRO GLU SER ASP
SEQRES 6 A 296 PRO ASP ARG VAL VAL LEU TYR LEU HIS GLY GLY GLY TYR
SEQRES 7 A 296 VAL ILE GLY SER ILE ARG THR HIS ARG ASP LEU ALA GLN
SEQRES 8 A 296 ARG ILE ALA ARG ALA ALA ARG CYS ARG VAL LEU LEU ILE
SEQRES 9 A 296 ASP TYR ARG LEU ALA PRO GLU HIS PRO HIS PRO ALA ALA
SEQRES 10 A 296 VAL GLU ASP SER THR ARG ALA TYR ARG TRP LEU LEU GLU
SEQRES 11 A 296 THR GLY SER ASP PRO LYS ARG MET ALA ILE ALA GLY ASP
SEQRES 12 A 296 ALA ALA GLY GLY GLY LEU THR VAL ALA THR LEU VAL ALA
SEQRES 13 A 296 LEU ARG ASP ALA GLY VAL PRO LEU PRO ALA ALA ALA VAL
SEQRES 14 A 296 CYS LEU SER PRO TRP VAL ASP LEU GLU GLY ILE GLY GLU
SEQRES 15 A 296 SER MET THR THR LYS ALA ALA VAL ASP PRO MET VAL GLN
SEQRES 16 A 296 ARG GLU PRO LEU LEU ARG MET ALA SER MET TYR LEU ALA
SEQRES 17 A 296 GLY GLN ASP PRO ARG THR PRO LEU ALA ALA PRO LEU TYR
SEQRES 18 A 296 ALA ASP LEU ARG GLY LEU PRO PRO LEU LEU ILE GLN VAL
SEQRES 19 A 296 GLY THR ALA GLU THR LEU LEU ASP ASP SER VAL ARG LEU
SEQRES 20 A 296 ALA GLU ARG ALA ARG ALA ALA GLY VAL GLN VAL THR LEU
SEQRES 21 A 296 GLU PRO TRP GLU ASP MET ILE HIS VAL TRP GLN ALA PHE
SEQRES 22 A 296 ALA ALA MET LEU PRO GLU GLY GLN GLN ALA ILE GLU ARG
SEQRES 23 A 296 ILE GLY GLU PHE LEU ARG GLN HIS TRP GLN
SEQRES 1 B 296 MET ALA SER GLU ALA LEU THR MET ILE VAL ASN LEU LEU
SEQRES 2 B 296 ARG SER GLN ARG PRO LEU GLN GLU PRO THR VAL GLU GLN
SEQRES 3 B 296 MET ARG ALA GLY LEU GLU ALA MET ALA GLN MET SER PRO
SEQRES 4 B 296 LEU PRO ALA ASP VAL GLU LEU THR THR VAL ASP ALA GLY
SEQRES 5 B 296 GLY VAL PRO GLY ALA TRP VAL ARG VAL PRO GLU SER ASP
SEQRES 6 B 296 PRO ASP ARG VAL VAL LEU TYR LEU HIS GLY GLY GLY TYR
SEQRES 7 B 296 VAL ILE GLY SER ILE ARG THR HIS ARG ASP LEU ALA GLN
SEQRES 8 B 296 ARG ILE ALA ARG ALA ALA ARG CYS ARG VAL LEU LEU ILE
SEQRES 9 B 296 ASP TYR ARG LEU ALA PRO GLU HIS PRO HIS PRO ALA ALA
SEQRES 10 B 296 VAL GLU ASP SER THR ARG ALA TYR ARG TRP LEU LEU GLU
SEQRES 11 B 296 THR GLY SER ASP PRO LYS ARG MET ALA ILE ALA GLY ASP
SEQRES 12 B 296 ALA ALA GLY GLY GLY LEU THR VAL ALA THR LEU VAL ALA
SEQRES 13 B 296 LEU ARG ASP ALA GLY VAL PRO LEU PRO ALA ALA ALA VAL
SEQRES 14 B 296 CYS LEU SER PRO TRP VAL ASP LEU GLU GLY ILE GLY GLU
SEQRES 15 B 296 SER MET THR THR LYS ALA ALA VAL ASP PRO MET VAL GLN
SEQRES 16 B 296 ARG GLU PRO LEU LEU ARG MET ALA SER MET TYR LEU ALA
SEQRES 17 B 296 GLY GLN ASP PRO ARG THR PRO LEU ALA ALA PRO LEU TYR
SEQRES 18 B 296 ALA ASP LEU ARG GLY LEU PRO PRO LEU LEU ILE GLN VAL
SEQRES 19 B 296 GLY THR ALA GLU THR LEU LEU ASP ASP SER VAL ARG LEU
SEQRES 20 B 296 ALA GLU ARG ALA ARG ALA ALA GLY VAL GLN VAL THR LEU
SEQRES 21 B 296 GLU PRO TRP GLU ASP MET ILE HIS VAL TRP GLN ALA PHE
SEQRES 22 B 296 ALA ALA MET LEU PRO GLU GLY GLN GLN ALA ILE GLU ARG
SEQRES 23 B 296 ILE GLY GLU PHE LEU ARG GLN HIS TRP GLN
HET FMT A1301 3
HET FMT A1302 3
HET FMT A1303 3
HET FMT A1304 3
HET FMT A1305 3
HET FMT A1306 3
HET ACT A1307 4
HET FMT A1308 3
HET FMT A1309 3
HET FMT A1310 3
HET FMT A1311 3
HET FMT A1312 3
HET FMT A1313 3
HET FMT A1314 3
HET RXH B1301 18
HET FMT B1302 3
HET ACT B1303 4
HETNAM FMT FORMIC ACID
HETNAM ACT ACETATE ION
HETNAM RXH NAPROXEN METHYL ESTER
HETSYN RXH METHYL (2S)-2-(6-METHOXYNAPHTHALEN-2-YL)PROPANOATE;
HETSYN 2 RXH (S)-METHYL 2-(6-METHOXYNAPHTHALEN-2-YL)PROPANOATE;
HETSYN 3 RXH (S)-NAPROXEN METHYL ESTER; METHYL-NAPROXEN;
FORMUL 3 FMT 14(C H2 O2)
FORMUL 9 ACT 2(C2 H3 O2 1-)
FORMUL 17 RXH
FORMUL 20 HOH *673(H2 O)
HELIX 1 AA1 GLU A 4 ARG A 17 1 14
HELIX 2 AA2 PRO A 18 GLU A 21 5 4
HELIX 3 AA3 THR A 23 GLN A 36 1 14
HELIX 4 AA4 SER A 82 ARG A 98 1 17
HELIX 5 AA5 PRO A 115 THR A 131 1 17
HELIX 6 AA6 ASP A 134 LYS A 136 5 3
HELIX 7 AA7 ALA A 144 ALA A 160 1 17
HELIX 8 AA8 GLY A 181 LYS A 187 1 7
HELIX 9 AA9 GLN A 195 ALA A 208 1 14
HELIX 10 AB1 ALA A 218 ALA A 222 5 5
HELIX 11 AB2 LEU A 240 ALA A 254 1 15
HELIX 12 AB3 VAL A 269 ALA A 274 5 6
HELIX 13 AB4 LEU A 277 GLN A 296 1 20
HELIX 14 AB5 SER B 3 ARG B 17 1 15
HELIX 15 AB6 PRO B 18 GLU B 21 5 4
HELIX 16 AB7 THR B 23 GLN B 36 1 14
HELIX 17 AB8 SER B 82 ARG B 98 1 17
HELIX 18 AB9 PRO B 115 THR B 131 1 17
HELIX 19 AC1 ASP B 134 LYS B 136 5 3
HELIX 20 AC2 ALA B 144 ALA B 160 1 17
HELIX 21 AC3 GLU B 182 LYS B 187 1 6
HELIX 22 AC4 GLN B 195 ALA B 208 1 14
HELIX 23 AC5 ALA B 218 ALA B 222 5 5
HELIX 24 AC6 LEU B 240 ALA B 254 1 15
HELIX 25 AC7 VAL B 269 ALA B 274 5 6
HELIX 26 AC8 LEU B 277 TRP B 295 1 19
SHEET 1 AA1 8 GLU A 45 ASP A 50 0
SHEET 2 AA1 8 PRO A 55 ARG A 60 -1 O TRP A 58 N THR A 47
SHEET 3 AA1 8 CYS A 99 ILE A 104 -1 O LEU A 103 N ALA A 57
SHEET 4 AA1 8 ASP A 65 LEU A 73 1 N VAL A 70 O LEU A 102
SHEET 5 AA1 8 MET A 138 ASP A 143 1 O ALA A 141 N LEU A 73
SHEET 6 AA1 8 ALA A 167 LEU A 171 1 O LEU A 171 N GLY A 142
SHEET 7 AA1 8 LEU A 230 GLY A 235 1 O LEU A 231 N CYS A 170
SHEET 8 AA1 8 VAL A 258 TRP A 263 1 O GLU A 261 N ILE A 232
SHEET 1 AA2 8 GLU B 45 ALA B 51 0
SHEET 2 AA2 8 VAL B 54 ARG B 60 -1 O VAL B 54 N ALA B 51
SHEET 3 AA2 8 CYS B 99 ILE B 104 -1 O LEU B 103 N ALA B 57
SHEET 4 AA2 8 ASP B 65 LEU B 73 1 N TYR B 72 O LEU B 102
SHEET 5 AA2 8 MET B 138 ASP B 143 1 O ALA B 141 N LEU B 73
SHEET 6 AA2 8 ALA B 167 LEU B 171 1 O LEU B 171 N GLY B 142
SHEET 7 AA2 8 LEU B 230 GLY B 235 1 O LEU B 231 N CYS B 170
SHEET 8 AA2 8 VAL B 258 TRP B 263 1 O GLU B 261 N ILE B 232
CISPEP 1 ALA A 109 PRO A 110 0 -2.54
CISPEP 2 HIS A 114 PRO A 115 0 6.65
CISPEP 3 ALA B 109 PRO B 110 0 1.82
CISPEP 4 HIS B 114 PRO B 115 0 8.99
SITE 1 AC1 5 VAL A 49 TRP A 58 TRP A 127 HOH A1563
SITE 2 AC1 5 HOH A1642
SITE 1 AC2 5 GLU A 45 LEU A 46 THR A 47 FMT A1303
SITE 2 AC2 5 HOH A1493
SITE 1 AC3 4 LEU A 46 THR A 47 THR A 48 FMT A1302
SITE 1 AC4 7 GLU A 4 ARG A 107 GLU A 111 HIS A 112
SITE 2 AC4 7 HOH A1404 HOH A1503 HOH A1573
SITE 1 AC5 4 ARG A 68 ARG A 292 GLN A 296 THR B 131
SITE 1 AC6 8 PRO A 22 ARG A 201 MET A 205 HOH A1402
SITE 2 AC6 8 HOH A1433 HOH A1581 VAL B 258 THR B 259
SITE 1 AC7 5 GLY A 76 GLY A 77 ALA A 144 ALA A 145
SITE 2 AC7 5 HIS A 268
SITE 1 AC8 4 THR A 47 TRP A 58 ARG A 60 ARG A 100
SITE 1 AC9 7 ARG A 68 TRP A 295 GLN A 296 HOH A1495
SITE 2 AC9 7 HOH A1514 THR B 131 GLY B 132
SITE 1 AD1 7 TYR A 221 ASP A 223 ARG A 250 ARG A 286
SITE 2 AD1 7 HOH A1415 HOH A1421 HOH A1640
SITE 1 AD2 2 HOH A1504 HOH A1525
SITE 1 AD3 3 ARG A 87 HOH A1432 HOH A1455
SITE 1 AD4 7 GLY A 226 PRO A 262 TRP A 263 GLU A 264
SITE 2 AD4 7 HOH A1469 HOH A1520 HOH A1644
SITE 1 AD5 5 GLY B 181 GLU B 182 ASP B 242 ARG B 246
SITE 2 AD5 5 HOH B1602
SITE 1 AD6 11 LEU B 19 MET B 34 ALA B 35 GLY B 75
SITE 2 AD6 11 GLY B 76 THR B 85 ASP B 143 MET B 193
SITE 3 AD6 11 HIS B 268 ALA B 272 ACT B1303
SITE 1 AD7 3 GLN B 16 MET B 34 PHE B 273
SITE 1 AD8 6 GLY B 76 GLY B 77 ALA B 144 ALA B 145
SITE 2 AD8 6 HIS B 268 RXH B1301
CRYST1 47.846 80.243 145.146 90.00 90.00 90.00 P 21 21 21 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 0.020900 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012462 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006890 0.00000
TER 2324 GLN A 296
TER 4707 GLN B 296
MASTER 415 0 17 26 16 0 29 6 5235 2 68 46
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