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HEADER HYDROLASE 19-JUN-18 6GUO
TITLE SIDEROPHORE HYDROLASE ESTA FROM ASPERGILLUS NIDULANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE SIDEROPHORE-DEGRADING ESTERASE (EUROFUNG);
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: ESTA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ASPERGILLUS NIDULANS;
SOURCE 3 ORGANISM_TAXID: 162425;
SOURCE 4 GENE: ANIA_07801;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ALPHA/BETA-HYDROLASE, SIDEROPHORE, HYDROLYSIS, FUNGI, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.ECKER,H.HAAS,M.GROLL,E.M.HUBER
REVDAT 1 15-AUG-18 6GUO 0
JRNL AUTH F.ECKER,H.HAAS,M.GROLL,E.HUBER
JRNL TITL IRON SCAVENGING IN ASPERGILLUS SPECIES: STRUCTURAL AND
JRNL TITL 2 BIOCHEMICAL INSIGHTS INTO FUNGAL SIDEROPHORE ESTERASES.
JRNL REF ANGEW. CHEM. INT. ED. ENGL. 2018
JRNL REFN ESSN 1521-3773
JRNL PMID 30070018
JRNL DOI 10.1002/ANIE.201807093
REMARK 2
REMARK 2 RESOLUTION. 1.75 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) : 1.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 123129
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) : 0.165
REMARK 3 R VALUE (WORKING SET) : 0.163
REMARK 3 FREE R VALUE : 0.203
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 6478
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) : 1.75
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.80
REMARK 3 REFLECTION IN BIN (WORKING SET) : 8975
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.2420
REMARK 3 BIN FREE R VALUE SET COUNT : 472
REMARK 3 BIN FREE R VALUE : 0.2810
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 9393
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 1056
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.45
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.52000
REMARK 3 B22 (A**2) : 0.26000
REMARK 3 B33 (A**2) : 0.26000
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): 0.182
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.107
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.909
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.968
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 9857 ; 0.006 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 8950 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 13384 ; 1.153 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 20746 ; 0.881 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1233 ; 5.247 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 450 ;31.603 ;22.222
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1531 ;12.235 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 93 ;15.663 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1408 ; 0.063 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11108 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 2221 ; 0.001 ; 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): 4851 ; 1.478 ; 2.528
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 4850 ; 1.478 ; 2.528
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6075 ; 1.795 ; 3.781
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 6076 ; 1.795 ; 3.781
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5006 ; 1.612 ; 2.887
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 5006 ; 1.612 ; 2.887
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 7298 ; 1.885 ; 4.200
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 11281 ; 2.961 ;30.776
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 11059 ; 2.734 ;30.299
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 18807 ; 1.713 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 647 ;26.426 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 18954 ;10.663 ; 5.000
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
REMARK 4
REMARK 4 6GUO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1200010581.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUN-16
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 : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 129886
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.750
REMARK 200 RESOLUTION RANGE LOW (A) : 45.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 4.400
REMARK 200 R MERGE (I) : 0.09200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.55600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.400
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: 6GUD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5 0.25 M NACL 20 %
REMARK 280 PEG3350, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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+1/2,Y+1/2,-Z
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 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 52.78500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 118.09500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 52.78500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 118.09500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -67.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6720 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -46.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 52.78500
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 118.09500
REMARK 350 BIOMT3 2 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 GLY A 0
REMARK 465 SER A 1
REMARK 465 PRO A 118
REMARK 465 ASP A 119
REMARK 465 ALA A 209
REMARK 465 ALA A 210
REMARK 465 LEU A 211
REMARK 465 GLY B 0
REMARK 465 SER B 1
REMARK 465 GLY B 117
REMARK 465 PRO B 118
REMARK 465 ASP B 119
REMARK 465 GLY B 120
REMARK 465 SER B 121
REMARK 465 GLY C 0
REMARK 465 SER C 1
REMARK 465 GLY C 117
REMARK 465 PRO C 118
REMARK 465 ASP C 119
REMARK 465 GLY C 120
REMARK 465 GLY D 0
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 14 46.04 -84.77
REMARK 500 SER A 164 -119.72 61.78
REMARK 500 SER A 164 -120.04 62.39
REMARK 500 ALA B 14 48.26 -85.53
REMARK 500 SER B 164 -118.61 66.13
REMARK 500 SER B 164 -118.25 63.12
REMARK 500 ALA C 14 42.84 -85.90
REMARK 500 SER C 164 -121.04 59.70
REMARK 500 LYS C 177 60.00 -146.23
REMARK 500 ALA D 14 46.88 -87.28
REMARK 500 SER D 164 -119.78 63.63
REMARK 500 SER D 164 -119.58 65.05
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 PGE A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 403
DBREF 6GUO A 2 303 UNP Q5AV79 Q5AV79_EMENI 2 303
DBREF 6GUO B 2 303 UNP Q5AV79 Q5AV79_EMENI 2 303
DBREF 6GUO C 2 303 UNP Q5AV79 Q5AV79_EMENI 2 303
DBREF 6GUO D 2 303 UNP Q5AV79 Q5AV79_EMENI 2 303
SEQADV 6GUO GLY A 0 UNP Q5AV79 EXPRESSION TAG
SEQADV 6GUO SER A 1 UNP Q5AV79 EXPRESSION TAG
SEQADV 6GUO GLY B 0 UNP Q5AV79 EXPRESSION TAG
SEQADV 6GUO SER B 1 UNP Q5AV79 EXPRESSION TAG
SEQADV 6GUO GLY C 0 UNP Q5AV79 EXPRESSION TAG
SEQADV 6GUO SER C 1 UNP Q5AV79 EXPRESSION TAG
SEQADV 6GUO GLY D 0 UNP Q5AV79 EXPRESSION TAG
SEQADV 6GUO SER D 1 UNP Q5AV79 EXPRESSION TAG
SEQRES 1 A 304 GLY SER THR HIS TRP ALA PHE SER PRO ILE GLN PRO GLY
SEQRES 2 A 304 ALA ALA ARG ASN MET ALA ALA TRP GLN ILE ALA GLY LYS
SEQRES 3 A 304 LYS ASP GLY PRO TYR GLN ILE ASP VAL SER TRP PRO LEU
SEQRES 4 A 304 THR TRP SER GLU SER GLY ASP ALA SER GLY LYS SER ALA
SEQRES 5 A 304 ASN ALA VAL TYR LEU VAL ASP GLY ASN ALA LEU PHE LEU
SEQRES 6 A 304 THR ALA THR GLU THR LEU ARG ARG ARG GLU SER HIS ARG
SEQRES 7 A 304 PRO SER GLU THR GLY THR VAL VAL ILE ALA ILE GLY TYR
SEQRES 8 A 304 PRO ILE THR ASP SER VAL PHE SER PRO ARG ARG SER TYR
SEQRES 9 A 304 ASP LEU THR PRO PRO CYS ASP HIS TYR ILE PRO PRO GLU
SEQRES 10 A 304 GLY PRO ASP GLY SER PRO LYS PRO GLU ALA HIS GLY GLY
SEQRES 11 A 304 ALA ASP GLU PHE LEU THR PHE ILE ALA GLU ILE VAL ARG
SEQRES 12 A 304 PRO PHE VAL GLU LEU LYS VAL PHE PRO ARG VAL SER PHE
SEQRES 13 A 304 GLY ARG THR ALA LEU PHE GLY HIS SER TYR GLY GLY LEU
SEQRES 14 A 304 PHE ALA LEU HIS ALA LEU PHE THR LYS PRO SER SER PHE
SEQRES 15 A 304 ASP VAL TYR LEU ALA ALA SER PRO SER ILE TRP TRP ASN
SEQRES 16 A 304 ASN ARG SER ILE LEU THR GLU ALA ARG ARG PHE ILE SER
SEQRES 17 A 304 GLY ALA ALA LEU PHE SER SER ALA HIS PRO VAL LEU ARG
SEQRES 18 A 304 LEU SER PHE GLY SER ARG GLU GLN TYR PRO VAL ARG GLN
SEQRES 19 A 304 ARG VAL GLU SER ASP GLU MET PHE LYS ARG ARG GLN ARG
SEQRES 20 A 304 ALA ALA GLU GLN ARG ARG MET ASN ASP ASN CYS GLU GLU
SEQRES 21 A 304 LEU TYR SER GLU LEU LEU ALA SER GLY ARG LEU CYS LYS
SEQRES 22 A 304 LEU GLU VAL LYS GLU TYR LEU ASP GLU ASP HIS GLY SER
SEQRES 23 A 304 VAL ILE GLY PRO ALA LEU SER GLY GLY ILE MET PHE LEU
SEQRES 24 A 304 SER ASN LEU SER ALA
SEQRES 1 B 304 GLY SER THR HIS TRP ALA PHE SER PRO ILE GLN PRO GLY
SEQRES 2 B 304 ALA ALA ARG ASN MET ALA ALA TRP GLN ILE ALA GLY LYS
SEQRES 3 B 304 LYS ASP GLY PRO TYR GLN ILE ASP VAL SER TRP PRO LEU
SEQRES 4 B 304 THR TRP SER GLU SER GLY ASP ALA SER GLY LYS SER ALA
SEQRES 5 B 304 ASN ALA VAL TYR LEU VAL ASP GLY ASN ALA LEU PHE LEU
SEQRES 6 B 304 THR ALA THR GLU THR LEU ARG ARG ARG GLU SER HIS ARG
SEQRES 7 B 304 PRO SER GLU THR GLY THR VAL VAL ILE ALA ILE GLY TYR
SEQRES 8 B 304 PRO ILE THR ASP SER VAL PHE SER PRO ARG ARG SER TYR
SEQRES 9 B 304 ASP LEU THR PRO PRO CYS ASP HIS TYR ILE PRO PRO GLU
SEQRES 10 B 304 GLY PRO ASP GLY SER PRO LYS PRO GLU ALA HIS GLY GLY
SEQRES 11 B 304 ALA ASP GLU PHE LEU THR PHE ILE ALA GLU ILE VAL ARG
SEQRES 12 B 304 PRO PHE VAL GLU LEU LYS VAL PHE PRO ARG VAL SER PHE
SEQRES 13 B 304 GLY ARG THR ALA LEU PHE GLY HIS SER TYR GLY GLY LEU
SEQRES 14 B 304 PHE ALA LEU HIS ALA LEU PHE THR LYS PRO SER SER PHE
SEQRES 15 B 304 ASP VAL TYR LEU ALA ALA SER PRO SER ILE TRP TRP ASN
SEQRES 16 B 304 ASN ARG SER ILE LEU THR GLU ALA ARG ARG PHE ILE SER
SEQRES 17 B 304 GLY ALA ALA LEU PHE SER SER ALA HIS PRO VAL LEU ARG
SEQRES 18 B 304 LEU SER PHE GLY SER ARG GLU GLN TYR PRO VAL ARG GLN
SEQRES 19 B 304 ARG VAL GLU SER ASP GLU MET PHE LYS ARG ARG GLN ARG
SEQRES 20 B 304 ALA ALA GLU GLN ARG ARG MET ASN ASP ASN CYS GLU GLU
SEQRES 21 B 304 LEU TYR SER GLU LEU LEU ALA SER GLY ARG LEU CYS LYS
SEQRES 22 B 304 LEU GLU VAL LYS GLU TYR LEU ASP GLU ASP HIS GLY SER
SEQRES 23 B 304 VAL ILE GLY PRO ALA LEU SER GLY GLY ILE MET PHE LEU
SEQRES 24 B 304 SER ASN LEU SER ALA
SEQRES 1 C 304 GLY SER THR HIS TRP ALA PHE SER PRO ILE GLN PRO GLY
SEQRES 2 C 304 ALA ALA ARG ASN MET ALA ALA TRP GLN ILE ALA GLY LYS
SEQRES 3 C 304 LYS ASP GLY PRO TYR GLN ILE ASP VAL SER TRP PRO LEU
SEQRES 4 C 304 THR TRP SER GLU SER GLY ASP ALA SER GLY LYS SER ALA
SEQRES 5 C 304 ASN ALA VAL TYR LEU VAL ASP GLY ASN ALA LEU PHE LEU
SEQRES 6 C 304 THR ALA THR GLU THR LEU ARG ARG ARG GLU SER HIS ARG
SEQRES 7 C 304 PRO SER GLU THR GLY THR VAL VAL ILE ALA ILE GLY TYR
SEQRES 8 C 304 PRO ILE THR ASP SER VAL PHE SER PRO ARG ARG SER TYR
SEQRES 9 C 304 ASP LEU THR PRO PRO CYS ASP HIS TYR ILE PRO PRO GLU
SEQRES 10 C 304 GLY PRO ASP GLY SER PRO LYS PRO GLU ALA HIS GLY GLY
SEQRES 11 C 304 ALA ASP GLU PHE LEU THR PHE ILE ALA GLU ILE VAL ARG
SEQRES 12 C 304 PRO PHE VAL GLU LEU LYS VAL PHE PRO ARG VAL SER PHE
SEQRES 13 C 304 GLY ARG THR ALA LEU PHE GLY HIS SER TYR GLY GLY LEU
SEQRES 14 C 304 PHE ALA LEU HIS ALA LEU PHE THR LYS PRO SER SER PHE
SEQRES 15 C 304 ASP VAL TYR LEU ALA ALA SER PRO SER ILE TRP TRP ASN
SEQRES 16 C 304 ASN ARG SER ILE LEU THR GLU ALA ARG ARG PHE ILE SER
SEQRES 17 C 304 GLY ALA ALA LEU PHE SER SER ALA HIS PRO VAL LEU ARG
SEQRES 18 C 304 LEU SER PHE GLY SER ARG GLU GLN TYR PRO VAL ARG GLN
SEQRES 19 C 304 ARG VAL GLU SER ASP GLU MET PHE LYS ARG ARG GLN ARG
SEQRES 20 C 304 ALA ALA GLU GLN ARG ARG MET ASN ASP ASN CYS GLU GLU
SEQRES 21 C 304 LEU TYR SER GLU LEU LEU ALA SER GLY ARG LEU CYS LYS
SEQRES 22 C 304 LEU GLU VAL LYS GLU TYR LEU ASP GLU ASP HIS GLY SER
SEQRES 23 C 304 VAL ILE GLY PRO ALA LEU SER GLY GLY ILE MET PHE LEU
SEQRES 24 C 304 SER ASN LEU SER ALA
SEQRES 1 D 304 GLY SER THR HIS TRP ALA PHE SER PRO ILE GLN PRO GLY
SEQRES 2 D 304 ALA ALA ARG ASN MET ALA ALA TRP GLN ILE ALA GLY LYS
SEQRES 3 D 304 LYS ASP GLY PRO TYR GLN ILE ASP VAL SER TRP PRO LEU
SEQRES 4 D 304 THR TRP SER GLU SER GLY ASP ALA SER GLY LYS SER ALA
SEQRES 5 D 304 ASN ALA VAL TYR LEU VAL ASP GLY ASN ALA LEU PHE LEU
SEQRES 6 D 304 THR ALA THR GLU THR LEU ARG ARG ARG GLU SER HIS ARG
SEQRES 7 D 304 PRO SER GLU THR GLY THR VAL VAL ILE ALA ILE GLY TYR
SEQRES 8 D 304 PRO ILE THR ASP SER VAL PHE SER PRO ARG ARG SER TYR
SEQRES 9 D 304 ASP LEU THR PRO PRO CYS ASP HIS TYR ILE PRO PRO GLU
SEQRES 10 D 304 GLY PRO ASP GLY SER PRO LYS PRO GLU ALA HIS GLY GLY
SEQRES 11 D 304 ALA ASP GLU PHE LEU THR PHE ILE ALA GLU ILE VAL ARG
SEQRES 12 D 304 PRO PHE VAL GLU LEU LYS VAL PHE PRO ARG VAL SER PHE
SEQRES 13 D 304 GLY ARG THR ALA LEU PHE GLY HIS SER TYR GLY GLY LEU
SEQRES 14 D 304 PHE ALA LEU HIS ALA LEU PHE THR LYS PRO SER SER PHE
SEQRES 15 D 304 ASP VAL TYR LEU ALA ALA SER PRO SER ILE TRP TRP ASN
SEQRES 16 D 304 ASN ARG SER ILE LEU THR GLU ALA ARG ARG PHE ILE SER
SEQRES 17 D 304 GLY ALA ALA LEU PHE SER SER ALA HIS PRO VAL LEU ARG
SEQRES 18 D 304 LEU SER PHE GLY SER ARG GLU GLN TYR PRO VAL ARG GLN
SEQRES 19 D 304 ARG VAL GLU SER ASP GLU MET PHE LYS ARG ARG GLN ARG
SEQRES 20 D 304 ALA ALA GLU GLN ARG ARG MET ASN ASP ASN CYS GLU GLU
SEQRES 21 D 304 LEU TYR SER GLU LEU LEU ALA SER GLY ARG LEU CYS LYS
SEQRES 22 D 304 LEU GLU VAL LYS GLU TYR LEU ASP GLU ASP HIS GLY SER
SEQRES 23 D 304 VAL ILE GLY PRO ALA LEU SER GLY GLY ILE MET PHE LEU
SEQRES 24 D 304 SER ASN LEU SER ALA
HET PGE A 401 10
HET PGE A 402 10
HET CL A 403 1
HET CL A 404 1
HET PGE B 401 10
HET PGE B 402 10
HET CL B 403 1
HET CL B 404 1
HET PGE C 401 10
HET GOL C 402 6
HET CL C 403 1
HET PGE D 401 10
HET PGE D 402 10
HET CL D 403 1
HETNAM PGE TRIETHYLENE GLYCOL
HETNAM CL CHLORIDE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 PGE 7(C6 H14 O4)
FORMUL 7 CL 6(CL 1-)
FORMUL 14 GOL C3 H8 O3
FORMUL 19 HOH *1056(H2 O)
HELIX 1 AA1 ASP A 58 ARG A 77 1 20
HELIX 2 AA2 ARG A 100 THR A 106 1 7
HELIX 3 AA3 GLY A 129 ILE A 140 1 12
HELIX 4 AA4 ILE A 140 LYS A 148 1 9
HELIX 5 AA5 SER A 164 LYS A 177 1 14
HELIX 6 AA6 TRP A 192 SER A 197 1 6
HELIX 7 AA7 SER A 197 GLY A 208 1 12
HELIX 8 AA8 SER A 237 ARG A 252 1 16
HELIX 9 AA9 ARG A 252 GLY A 268 1 17
HELIX 10 AB1 VAL A 286 LEU A 301 1 16
HELIX 11 AB2 ASP B 58 ARG B 77 1 20
HELIX 12 AB3 ARG B 100 THR B 106 1 7
HELIX 13 AB4 GLY B 129 ILE B 140 1 12
HELIX 14 AB5 ILE B 140 LYS B 148 1 9
HELIX 15 AB6 SER B 164 LYS B 177 1 14
HELIX 16 AB7 PRO B 178 PHE B 181 5 4
HELIX 17 AB8 TRP B 192 SER B 197 1 6
HELIX 18 AB9 SER B 197 GLY B 208 1 12
HELIX 19 AC1 SER B 237 ARG B 252 1 16
HELIX 20 AC2 ARG B 252 GLY B 268 1 17
HELIX 21 AC3 VAL B 286 SER B 302 1 17
HELIX 22 AC4 ASP C 58 ARG C 77 1 20
HELIX 23 AC5 ARG C 100 THR C 106 1 7
HELIX 24 AC6 GLY C 129 ILE C 140 1 12
HELIX 25 AC7 ILE C 140 LYS C 148 1 9
HELIX 26 AC8 SER C 164 LYS C 177 1 14
HELIX 27 AC9 PRO C 178 PHE C 181 5 4
HELIX 28 AD1 TRP C 192 SER C 197 1 6
HELIX 29 AD2 SER C 197 GLY C 208 1 12
HELIX 30 AD3 SER C 237 ARG C 252 1 16
HELIX 31 AD4 ARG C 252 GLY C 268 1 17
HELIX 32 AD5 VAL C 286 LEU C 301 1 16
HELIX 33 AD6 ASP D 58 ARG D 77 1 20
HELIX 34 AD7 ARG D 100 THR D 106 1 7
HELIX 35 AD8 GLY D 129 ILE D 140 1 12
HELIX 36 AD9 ILE D 140 LYS D 148 1 9
HELIX 37 AE1 SER D 164 LYS D 177 1 14
HELIX 38 AE2 PRO D 178 PHE D 181 5 4
HELIX 39 AE3 TRP D 192 SER D 197 1 6
HELIX 40 AE4 SER D 197 GLY D 208 1 12
HELIX 41 AE5 SER D 237 ARG D 252 1 16
HELIX 42 AE6 ARG D 252 GLY D 268 1 17
HELIX 43 AE7 VAL D 286 SER D 302 1 17
SHEET 1 AA1 9 ALA A 5 ILE A 9 0
SHEET 2 AA1 9 MET B 17 ALA B 23 -1 O GLN B 21 N SER A 7
SHEET 3 AA1 9 TYR B 30 SER B 35 -1 O TYR B 30 N ILE B 22
SHEET 4 AA1 9 GLY B 82 GLY B 89 -1 O GLY B 89 N GLN B 31
SHEET 5 AA1 9 ALA B 51 VAL B 57 1 N LEU B 56 O ILE B 88
SHEET 6 AA1 9 PHE B 155 HIS B 163 1 O ALA B 159 N TYR B 55
SHEET 7 AA1 9 VAL B 183 ALA B 187 1 O LEU B 185 N LEU B 160
SHEET 8 AA1 9 VAL B 218 GLY B 224 1 O VAL B 218 N TYR B 184
SHEET 9 AA1 9 LYS B 272 TYR B 278 1 O GLU B 274 N LEU B 221
SHEET 1 AA2 9 LYS A 272 TYR A 278 0
SHEET 2 AA2 9 VAL A 218 GLY A 224 1 N PHE A 223 O TYR A 278
SHEET 3 AA2 9 VAL A 183 ALA A 187 1 N TYR A 184 O VAL A 218
SHEET 4 AA2 9 PHE A 155 HIS A 163 1 N LEU A 160 O LEU A 185
SHEET 5 AA2 9 ALA A 51 VAL A 57 1 N TYR A 55 O ALA A 159
SHEET 6 AA2 9 GLY A 82 GLY A 89 1 O ILE A 88 N LEU A 56
SHEET 7 AA2 9 TYR A 30 SER A 35 -1 N ASP A 33 O ALA A 87
SHEET 8 AA2 9 MET A 17 ALA A 23 -1 N ALA A 18 O VAL A 34
SHEET 9 AA2 9 ALA B 5 ILE B 9 -1 O SER B 7 N GLN A 21
SHEET 1 AA3 8 MET C 17 ILE C 22 0
SHEET 2 AA3 8 TYR C 30 SER C 35 -1 O VAL C 34 N ALA C 18
SHEET 3 AA3 8 GLY C 82 GLY C 89 -1 O ALA C 87 N ASP C 33
SHEET 4 AA3 8 ALA C 51 VAL C 57 1 N LEU C 56 O ILE C 88
SHEET 5 AA3 8 PHE C 155 HIS C 163 1 O ALA C 159 N TYR C 55
SHEET 6 AA3 8 VAL C 183 ALA C 187 1 O LEU C 185 N LEU C 160
SHEET 7 AA3 8 VAL C 218 GLY C 224 1 O VAL C 218 N TYR C 184
SHEET 8 AA3 8 LYS C 272 TYR C 278 1 O GLU C 274 N LEU C 221
SHEET 1 AA4 8 MET D 17 ILE D 22 0
SHEET 2 AA4 8 TYR D 30 SER D 35 -1 O VAL D 34 N ALA D 18
SHEET 3 AA4 8 GLY D 82 GLY D 89 -1 O GLY D 89 N GLN D 31
SHEET 4 AA4 8 ALA D 51 VAL D 57 1 N LEU D 56 O ILE D 88
SHEET 5 AA4 8 PHE D 155 HIS D 163 1 O ALA D 159 N TYR D 55
SHEET 6 AA4 8 VAL D 183 ALA D 187 1 O LEU D 185 N LEU D 160
SHEET 7 AA4 8 VAL D 218 GLY D 224 1 O VAL D 218 N TYR D 184
SHEET 8 AA4 8 LYS D 272 TYR D 278 1 O GLU D 274 N LEU D 221
CISPEP 1 GLN A 10 PRO A 11 0 2.19
CISPEP 2 GLN B 10 PRO B 11 0 -1.96
CISPEP 3 GLN C 10 PRO C 11 0 0.89
CISPEP 4 GLN D 10 PRO D 11 0 -1.54
SITE 1 AC1 5 GLU A 42 SER A 43 LYS A 148 VAL A 149
SITE 2 AC1 5 HOH A 525
SITE 1 AC2 5 HIS A 76 PHE B 97 ARG B 101 HIS B 163
SITE 2 AC2 5 HIS B 283
SITE 1 AC3 4 ASN A 52 ARG A 157 LEU A 298 SER A 302
SITE 1 AC4 5 VAL A 231 GLN A 233 ARG A 244 HOH A 510
SITE 2 AC4 5 HOH A 514
SITE 1 AC5 7 TRP B 20 GLU B 42 SER B 43 PHE B 144
SITE 2 AC5 7 LYS B 148 HOH B 502 HOH B 533
SITE 1 AC6 7 PHE A 97 HIS A 163 HIS A 283 GLY A 284
SITE 2 AC6 7 HIS B 76 HOH B 566 HOH B 630
SITE 1 AC7 5 PRO B 230 VAL B 231 ARG B 244 HOH B 633
SITE 2 AC7 5 HOH B 690
SITE 1 AC8 6 ARG A 234 HOH A 769 ASN B 300 LEU B 301
SITE 2 AC8 6 HOH B 567 HOH B 654
SITE 1 AC9 6 PHE C 97 HIS C 283 GLY C 284 ILE C 287
SITE 2 AC9 6 HOH C 620 HIS D 76
SITE 1 AD1 4 ALA C 18 TRP C 36 SER C 43 HOH C 581
SITE 1 AD2 5 PRO C 230 VAL C 231 ARG C 244 HOH C 539
SITE 2 AD2 5 HOH C 598
SITE 1 AD3 3 TRP D 20 SER D 43 HOH D 588
SITE 1 AD4 5 HIS C 76 PHE D 97 ARG D 101 SER D 164
SITE 2 AD4 5 HOH D 656
SITE 1 AD5 4 PRO D 230 VAL D 231 ARG D 244 HOH D 676
CRYST1 105.570 236.190 51.610 90.00 90.00 90.00 P 21 21 2 16
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 0.009472 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004234 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019376 0.00000
TER 2348 ALA A 303
TER 4738 ALA B 303
TER 7101 ALA C 303
TER 9509 ALA D 303
MASTER 369 0 14 43 34 0 24 610531 4 76 96
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