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HEADER HYDROLASE 15-MAR-17 5NFQ
TITLE NOVEL EPOXIDE HYDROLASES BELONGING TO THE ALPHA/BETA HYDROLASES
TITLE 2 SUPERFAMILY IN METAGENOMES FROM HOT ENVIRONMENTS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPOXIDE HYDROLASE BELONGING TO ALPHA/BETA HYDROLASE
COMPND 3 SUPERFAMILY METAGENOMIC FROM TOMSK SAMPLE;
COMPND 4 CHAIN: A;
COMPND 5 EC: 3.3.2.10;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METAGENOME;
SOURCE 3 ORGANISM_TAXID: 256318;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EPOXIDE HYDROLASES, METAGENOMICS, INDUSTRIAL BIOCATALYSIS,
KEYWDS 2 STEREOSELECTIVITY, PROTEIN STRUCTURE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR E.E.FERRANDI,S.A.DE ROSE,C.SAYER,E.GUAZZELLI,C.MARCHESI,V.SANEEI,
AUTHOR 2 M.N.ISUPOV,J.A.LITTLECHILD,D.MONTI
REVDAT 1 16-MAY-18 5NFQ 0
JRNL AUTH E.E.FERRANDI,S.A.DE ROSE,C.SAYER,E.GUAZZELLI,C.MARCHESI,
JRNL AUTH 2 V.SANEEI,M.N.ISUPOV,J.A.LITTLECHILD,D.MONTI
JRNL TITL NOVEL EPOXIDE HYDROLASES BELONGING TO THE ALPHA/BETA
JRNL TITL 2 HYDROLASES SUPERFAMILY IN METAGENOMES FROM HOT ENVIRONMENTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.36
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 33829
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) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1824
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1957
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.31
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE SET COUNT : 108
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2354
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 75
REMARK 3 SOLVENT ATOMS : 311
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.49000
REMARK 3 B22 (A**2) : 0.27000
REMARK 3 B33 (A**2) : -0.76000
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): 0.097
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.069
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.083
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2698 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3683 ; 1.419 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 349 ; 5.890 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 132 ;36.722 ;23.561
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 426 ;13.463 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;16.181 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 389 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2112 ; 0.007 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 1262 ; 2.610 ; 4.819
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1591 ; 3.693 ; 8.107
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1434 ; 3.857 ; 5.772
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): 11695 ; 6.412 ;35.882
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: NULL
REMARK 4
REMARK 4 5NFQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004042.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35698
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 39.360
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.4
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10600
REMARK 200 FOR THE DATA SET : 9.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 1.01500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MORDA
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: E8 12.5% W/V PEG 1000, 12.5% W/V PEG
REMARK 280 3350, 12.5% V/V MPD 0.03 M OF EACH ETHYLENE GLYCOL 0.1 M MOPS/
REMARK 280 HEPES-NA PH 7.5, MICROBATCH, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
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
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 78.72500
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 78.72500
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 20.60000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.09000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 20.60000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.09000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 78.72500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 20.60000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.09000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 78.72500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 20.60000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.09000
REMARK 290 SMTRY3 8 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: 2870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 34.0 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 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 A 768 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 HIS A 299
REMARK 465 HIS A 300
REMARK 465 HIS A 301
REMARK 465 HIS A 302
REMARK 465 HIS A 303
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 THR A 2 123.36 163.06
REMARK 500 PRO A 36 62.67 -109.65
REMARK 500 GLU A 37 -130.50 -108.11
REMARK 500 SER A 38 -178.04 -177.23
REMARK 500 ARG A 64 -122.88 49.61
REMARK 500 ASP A 102 -132.15 58.27
REMARK 500 HIS A 117 -20.39 73.06
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 PRO A 58 ASP A 59 149.26
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 PEG A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 414
DBREF 5NFQ A 1 303 PDB 5NFQ 5NFQ 1 303
SEQRES 1 A 303 MET THR PHE GLU LEU LYS ARG VAL ALA LEU PRO ASN GLY
SEQRES 2 A 303 ILE HIS LEU ASP VAL VAL ASP GLU GLY PRO THR ASP ALA
SEQRES 3 A 303 PRO VAL LEU ILE PHE LEU HIS GLY PHE PRO GLU SER HIS
SEQRES 4 A 303 ARG THR TRP ARG HIS GLN ILE ARG HIS PHE SER ASP ARG
SEQRES 5 A 303 PHE ARG CYS ILE ALA PRO ASP GLN ARG GLY TYR ARG GLY
SEQRES 6 A 303 SER SER LYS PRO GLN GLU VAL ALA ALA TYR THR PRO ASP
SEQRES 7 A 303 LYS LEU ILE GLY ASP ILE PHE LEU LEU ALA ASP THR LEU
SEQRES 8 A 303 GLY ILE GLY SER PHE THR ILE VAL GLY HIS ASP TRP GLY
SEQRES 9 A 303 GLY ALA ILE ALA TRP GLY VAL ALA LEU GLY GLY GLN HIS
SEQRES 10 A 303 LEU ARG VAL GLU ARG ALA ILE ILE ALA ASN ALA PRO HIS
SEQRES 11 A 303 PRO ALA ILE PHE GLN LYS LEU LEU TYR THR HIS PRO VAL
SEQRES 12 A 303 GLN ARG GLU ALA SER GLN TYR ILE ARG GLY PHE ARG ASP
SEQRES 13 A 303 PRO ALA ASN ASP ALA LEU VAL LYS GLU HIS GLY LEU THR
SEQRES 14 A 303 GLY LEU LEU MET LYS GLU VAL LYS TRP ASP ARG PRO SER
SEQRES 15 A 303 ALA MET GLU PRO GLU GLU ARG ASP GLN LEU LEU ARG ASP
SEQRES 16 A 303 TRP GLN ASN HIS ASP ALA ALA PHE GLY MET LEU ASN TYR
SEQRES 17 A 303 TYR ARG ALA SER PRO ILE ASP VAL PRO THR MET ASP ALA
SEQRES 18 A 303 PRO PHE LYS VAL PRO ALA GLY TYR THR PRO PRO GLN LEU
SEQRES 19 A 303 PRO ARG LEU THR ILE PRO THR LEU VAL ILE TRP ALA LEU
SEQRES 20 A 303 ASP ASP LEU ALA LEU PRO PRO GLU ASN LEU GLU GLY LEU
SEQRES 21 A 303 GLU GLU ILE ILE ASP PRO LEU THR ILE VAL ARG VAL PRO
SEQRES 22 A 303 ASP CYS GLY HIS PHE VAL PRO TRP GLU ALA PRO ASP ALA
SEQRES 23 A 303 VAL ASN ALA ALA MET GLU GLY PHE LEU ALA GLY HIS HIS
SEQRES 24 A 303 HIS HIS HIS HIS
HET PEG A 401 7
HET PEG A 402 7
HET EDO A 403 4
HET EDO A 404 4
HET EDO A 405 4
HET EDO A 406 4
HET EDO A 407 4
HET EDO A 408 4
HET EDO A 409 4
HET EDO A 410 4
HET EDO A 411 4
HET PGE A 412 10
HET PGE A 413 10
HET IMD A 414 5
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM EDO 1,2-ETHANEDIOL
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM IMD IMIDAZOLE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 PEG 2(C4 H10 O3)
FORMUL 4 EDO 9(C2 H6 O2)
FORMUL 13 PGE 2(C6 H14 O4)
FORMUL 15 IMD C3 H5 N2 1+
FORMUL 16 HOH *311(H2 O)
HELIX 1 AA1 SER A 38 THR A 41 5 4
HELIX 2 AA2 TRP A 42 SER A 50 1 9
HELIX 3 AA3 GLU A 71 TYR A 75 5 5
HELIX 4 AA4 THR A 76 LEU A 91 1 16
HELIX 5 AA5 ASP A 102 GLN A 116 1 15
HELIX 6 AA6 ILE A 133 HIS A 141 1 9
HELIX 7 AA7 HIS A 141 SER A 148 1 8
HELIX 8 AA8 SER A 148 ARG A 155 1 8
HELIX 9 AA9 ASP A 156 ALA A 158 5 3
HELIX 10 AB1 ASN A 159 GLU A 175 1 17
HELIX 11 AB2 GLU A 185 TRP A 196 1 12
HELIX 12 AB3 ASN A 198 SER A 212 1 15
HELIX 13 AB4 PRO A 253 GLU A 258 5 6
HELIX 14 AB5 GLY A 259 ILE A 264 1 6
HELIX 15 AB6 PHE A 278 ALA A 283 1 6
HELIX 16 AB7 ALA A 283 ALA A 296 1 14
SHEET 1 AA1 8 LEU A 5 ALA A 9 0
SHEET 2 AA1 8 HIS A 15 GLU A 21 -1 O LEU A 16 N VAL A 8
SHEET 3 AA1 8 ARG A 54 ASP A 59 -1 O CYS A 55 N GLU A 21
SHEET 4 AA1 8 VAL A 28 LEU A 32 1 N PHE A 31 O ILE A 56
SHEET 5 AA1 8 PHE A 96 HIS A 101 1 O VAL A 99 N LEU A 32
SHEET 6 AA1 8 VAL A 120 ALA A 126 1 O ALA A 126 N GLY A 100
SHEET 7 AA1 8 THR A 241 ALA A 246 1 O ILE A 244 N ILE A 125
SHEET 8 AA1 8 LEU A 267 VAL A 272 1 O VAL A 270 N VAL A 243
CISPEP 1 PHE A 35 PRO A 36 0 -0.73
CISPEP 2 ASP A 265 PRO A 266 0 5.76
SITE 1 AC1 4 ARG A 236 GLU A 261 GLU A 262 ASP A 265
SITE 1 AC2 5 ASP A 89 GLY A 92 ASP A 190 EDO A 408
SITE 2 AC2 5 HOH A 506
SITE 1 AC3 5 LEU A 5 ARG A 7 ASP A 17 ARG A 236
SITE 2 AC3 5 GLU A 262
SITE 1 AC4 4 ALA A 283 PRO A 284 ASP A 285 ALA A 286
SITE 1 AC5 7 ASN A 12 ARG A 61 LYS A 79 PGE A 413
SITE 2 AC5 7 HOH A 542 HOH A 593 HOH A 720
SITE 1 AC6 7 ARG A 43 HIS A 44 MET A 184 GLU A 185
SITE 2 AC6 7 GLU A 188 HOH A 575 HOH A 618
SITE 1 AC7 3 ARG A 271 HOH A 512 HOH A 518
SITE 1 AC8 3 HIS A 141 PEG A 402 HOH A 615
SITE 1 AC9 3 HIS A 48 HOH A 606 HOH A 714
SITE 1 AD1 5 LYS A 68 HOH A 532 HOH A 550 HOH A 563
SITE 2 AD1 5 HOH A 602
SITE 1 AD2 6 PRO A 77 TRP A 103 SER A 212 PRO A 213
SITE 2 AD2 6 ILE A 214 HOH A 510
SITE 1 AD3 9 GLY A 82 LEU A 162 HIS A 166 GLY A 170
SITE 2 AD3 9 MET A 173 EDO A 405 HOH A 593 HOH A 636
SITE 3 AD3 9 HOH A 697
SITE 1 AD4 4 GLY A 293 PHE A 294 ALA A 296 HIS A 298
CRYST1 41.200 84.180 157.450 90.00 90.00 90.00 C 2 2 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 0.024272 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011879 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006351 0.00000
TER 2536 HIS A 298
MASTER 364 0 14 16 8 0 21 6 2740 1 75 24
END |