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HEADER HYDROLASE 28-OCT-20 7AT4
TITLE STRUCTURE OF ESTD11 IN COMPLEX WITH NAPROXEN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTD11;
COMPND 3 CHAIN: A;
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_PLASMID: 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 7AT4 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. 1.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0258
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) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.05
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 30878
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) : 0.156
REMARK 3 FREE R VALUE : 0.191
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.013
REMARK 3 FREE R VALUE TEST SET COUNT : 1548
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) : 1.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.74
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2160
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2390
REMARK 3 BIN FREE R VALUE SET COUNT : 116
REMARK 3 BIN FREE R VALUE : 0.3040
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2243
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 86
REMARK 3 SOLVENT ATOMS : 302
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.28
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.01200
REMARK 3 B22 (A**2) : 0.01100
REMARK 3 B33 (A**2) : 0.00100
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): 0.103
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.100
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.069
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.105
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.955
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2435 ; 0.011 ; 0.013
REMARK 3 BOND LENGTHS OTHERS (A): 2301 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3322 ; 1.712 ; 1.645
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5301 ; 1.460 ; 1.569
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 306 ; 5.901 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 126 ;27.890 ;20.159
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 383 ;14.403 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;23.204 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 309 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2795 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 523 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 525 ; 0.223 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 55 ; 0.244 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1195 ; 0.168 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 258 ; 0.205 ; 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): 1203 ; 1.677 ; 1.685
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1204 ; 1.678 ; 1.689
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1510 ; 2.399 ; 2.525
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1511 ; 2.402 ; 2.528
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1230 ; 3.247 ; 2.188
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1229 ; 3.248 ; 2.188
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1808 ; 4.860 ; 3.106
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1809 ; 4.858 ; 3.106
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 : 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 7AT4 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_1292112045.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-MAY-20
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) : 0.979
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 : 30890
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
REMARK 200 RESOLUTION RANGE LOW (A) : 45.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 13.20
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.73
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.60
REMARK 200 R MERGE FOR SHELL (I) : 0.95000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.100
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 (%): 42.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.14
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: 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 24.08600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 45.30200
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 63.12550
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 24.08600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 45.30200
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 63.12550
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 24.08600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 45.30200
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 63.12550
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 24.08600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 45.30200
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 63.12550
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 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 A1703 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1710 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1830 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A1925 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 ALA A 189
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 1876 O HOH A 1938 1.71
REMARK 500 OE2 GLU A 63 O HOH A 1701 2.15
REMARK 500 O HOH A 1820 O HOH A 1929 2.16
REMARK 500 O HOH A 1719 O HOH A 1973 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 1912 O HOH A 1919 8544 2.12
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 SER A 144 -115.72 58.25
REMARK 500 ALA A 237 34.00 -95.69
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 FMT A 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1602
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1604
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 1606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPX A 1607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPX A 1608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPX A 1609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NPX A 1610
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: 7ATD RELATED DB: PDB
DBREF 7AT4 A 1 296 PDB 7AT4 7AT4 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 SER 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
HET FMT A1601 3
HET FMT A1602 3
HET FMT A1603 3
HET FMT A1604 3
HET FMT A1605 3
HET FMT A1606 3
HET NPX A1607 17
HET NPX A1608 17
HET NPX A1609 17
HET NPX A1610 17
HETNAM FMT FORMIC ACID
HETNAM NPX (2R)-2-(6-METHOXYNAPHTHALEN-2-YL)PROPANOIC ACID
HETSYN NPX (R)-NAPROXEN
FORMUL 2 FMT 6(C H2 O2)
FORMUL 8 NPX 4(C14 H14 O3)
FORMUL 12 HOH *302(H2 O)
HELIX 1 AA1 SER A 3 ARG A 17 1 15
HELIX 2 AA2 THR A 23 GLN A 36 1 14
HELIX 3 AA3 SER A 82 ARG A 98 1 17
HELIX 4 AA4 PRO A 115 THR A 131 1 17
HELIX 5 AA5 ASP A 134 LYS A 136 5 3
HELIX 6 AA6 SER A 144 ALA A 160 1 17
HELIX 7 AA7 GLU A 182 LYS A 187 1 6
HELIX 8 AA8 GLN A 195 ALA A 208 1 14
HELIX 9 AA9 ALA A 218 ALA A 222 5 5
HELIX 10 AB1 LEU A 240 ALA A 254 1 15
HELIX 11 AB2 VAL A 269 ALA A 274 5 6
HELIX 12 AB3 LEU A 277 GLN A 296 1 20
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 VAL A 101 N VAL A 59
SHEET 4 AA1 8 ASP A 65 LEU A 73 1 N TYR A 72 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
CISPEP 1 ALA A 109 PRO A 110 0 -1.35
CISPEP 2 HIS A 114 PRO A 115 0 5.51
SITE 1 AC1 5 GLU A 45 TRP A 58 ARG A 60 ARG A 100
SITE 2 AC1 5 HOH A1711
SITE 1 AC2 6 LEU A 46 THR A 47 THR A 48 ASP A 50
SITE 2 AC2 6 HOH A1706 HOH A1880
SITE 1 AC3 3 GLU A 32 SER A 82 ARG A 84
SITE 1 AC4 3 MET A 34 MET A 37 NPX A1608
SITE 1 AC5 5 GLY A 76 GLY A 77 SER A 144 ALA A 145
SITE 2 AC5 5 HIS A 268
SITE 1 AC6 4 PRO A 18 GLU A 21 NPX A1607 HOH A1907
SITE 1 AC7 10 LEU A 13 GLN A 16 PRO A 18 PRO A 22
SITE 2 AC7 10 MET A 34 PRO A 192 PRO A 198 FMT A1606
SITE 3 AC7 10 NPX A1608 NPX A1609
SITE 1 AC8 9 PRO A 18 GLN A 20 PRO A 22 GLN A 26
SITE 2 AC8 9 GLY A 30 LEU A 31 MET A 34 FMT A1604
SITE 3 AC8 9 NPX A1607
SITE 1 AC9 11 LEU A 12 LEU A 13 MET A 34 MET A 37
SITE 2 AC9 11 SER A 38 ALA A 272 PHE A 273 MET A 276
SITE 3 AC9 11 NPX A1607 NPX A1610 HOH A1708
SITE 1 AD1 10 LEU A 31 GLY A 75 GLY A 76 THR A 85
SITE 2 AD1 10 HIS A 86 ASP A 143 MET A 193 VAL A 269
SITE 3 AD1 10 ALA A 272 NPX A1609
CRYST1 48.172 90.604 126.251 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 0.020759 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011037 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007921 0.00000
TER 2298 GLN A 296
MASTER 368 0 10 12 8 0 21 6 2631 1 86 23
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