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HEADER HYDROLASE 09-MAY-18 6GI2
TITLE CRYSTAL STRUCTURE OF THE FERRIC ENTEROBACTIN ESTERASE (PFEE)
TITLE 2 MUTANT(S157A) FROM PSEUDOMONAS AERUGINOSA IN COMPLEX WITH TRIS-
TITLE 3 CATECHOL VECTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FERRIC ENTEROBACTIN ESTERASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 STRAIN: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228
SOURCE 5 / 1C / PRS 101 / PAO1;
SOURCE 6 GENE: PA2689;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PFEE, PA2689, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.MOYNIE,J.H.NAISMITH
REVDAT 1 20-JUN-18 6GI2 0
JRNL AUTH L.MOYNIE,J.H.NAISMITH,I.SCHALK
JRNL TITL A KEY ROLE FOR PFEE ESTERASE IN IRON ACQUISITION VIA THE
JRNL TITL 2 SIDEROPHORE ENTEROBACTIN IN P. AERUGINOSA
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.49 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0189
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) : 1.49
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 65.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 90838
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) : 0.174
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.199
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 4849
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) : 1.49
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.52
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6681
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2790
REMARK 3 BIN FREE R VALUE SET COUNT : 355
REMARK 3 BIN FREE R VALUE : 0.3000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4010
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 126
REMARK 3 SOLVENT ATOMS : 260
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 26.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.76000
REMARK 3 B22 (A**2) : -0.16000
REMARK 3 B33 (A**2) : -1.60000
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): 0.065
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.067
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.047
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.290
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.962
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4325 ; 0.013 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 4056 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5868 ; 1.423 ; 2.002
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9274 ; 0.754 ; 3.004
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 532 ; 6.505 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 194 ;32.335 ;21.237
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 638 ;13.090 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 61 ;18.664 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 615 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4914 ; 0.014 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 983 ; 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): 2128 ; 2.899 ; 2.298
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2129 ; 2.898 ; 2.298
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2660 ; 4.039 ; 3.422
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2661 ; 4.038 ; 3.422
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2197 ; 4.278 ; 2.794
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2197 ; 4.277 ; 2.794
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3209 ; 6.409 ; 4.003
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4778 ; 7.750 ;27.470
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4779 ; 7.750 ;27.473
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 11 275 B 11 275 15868 0.11 0.05
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 6GI2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1200009979.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-APR-17
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 : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9686
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 95776
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.480
REMARK 200 RESOLUTION RANGE LOW (A) : 129.870
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.200
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.48
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.51
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 7.10
REMARK 200 R MERGE FOR SHELL (I) : 0.79600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 2.200
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: 6GI0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 2000, SODIUM ACETATE,
REMARK 280 POTASSIUM NITRATE, VAPOR DIFFUSION, TEMPERATURE 294K
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 28.89700
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 64.93350
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.30100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 64.93350
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.89700
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.30100
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 GLY A -2
REMARK 465 ALA A -1
REMARK 465 MET A 0
REMARK 465 ASN A 1
REMARK 465 PRO A 2
REMARK 465 ASP A 3
REMARK 465 PRO A 4
REMARK 465 GLU A 5
REMARK 465 ALA A 6
REMARK 465 THR A 7
REMARK 465 MET A 8
REMARK 465 ASP A 9
REMARK 465 ARG A 10
REMARK 465 ALA A 111
REMARK 465 ASP A 112
REMARK 465 GLY A 223
REMARK 465 SER A 224
REMARK 465 LEU A 225
REMARK 465 LYS A 226
REMARK 465 ALA A 227
REMARK 465 ARG A 277
REMARK 465 GLN A 278
REMARK 465 ARG A 279
REMARK 465 GLY B -2
REMARK 465 ALA B -1
REMARK 465 MET B 0
REMARK 465 ASN B 1
REMARK 465 PRO B 2
REMARK 465 ASP B 3
REMARK 465 PRO B 4
REMARK 465 GLU B 5
REMARK 465 PRO B 108
REMARK 465 GLY B 109
REMARK 465 GLN B 110
REMARK 465 ALA B 111
REMARK 465 ASP B 112
REMARK 465 SER B 224
REMARK 465 LEU B 225
REMARK 465 LYS B 226
REMARK 465 ALA B 227
REMARK 465 GLN B 278
REMARK 465 ARG B 279
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 437 O HOH A 466 2.05
REMARK 500 O HOH A 437 O HOH A 470 2.11
REMARK 500 OAH 8SW A 302 O HOH A 401 2.14
REMARK 500 O HOH B 507 O HOH B 519 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ARG A 150 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 89 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG B 89 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 150 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG B 150 NE - CZ - NH2 ANGL. DEV. = -4.5 DEGREES
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 157 -116.21 65.52
REMARK 500 ARG A 170 54.56 -143.38
REMARK 500 ALA B 157 -117.24 66.18
REMARK 500 ARG B 170 57.45 -143.70
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE A 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 8SW A 302 OAJ
REMARK 620 2 8SW A 302 OAI 91.3
REMARK 620 3 8SW A 302 OAM 74.8 110.3
REMARK 620 4 8SW A 302 OAL 152.4 77.2 85.7
REMARK 620 5 8SW A 302 OAH 88.6 89.8 153.8 115.9
REMARK 620 6 8SW A 302 OAK 109.7 154.3 90.0 89.3 76.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FE B 301 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 8SW B 302 OAI
REMARK 620 2 8SW B 302 OAL 78.3
REMARK 620 3 8SW B 302 OAH 88.5 111.5
REMARK 620 4 8SW B 302 OAK 158.1 87.8 80.9
REMARK 620 5 8SW B 302 OAM 104.1 84.5 161.7 91.1
REMARK 620 6 8SW B 302 OAJ 91.1 155.1 90.4 108.0 76.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8SW A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FE B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8SW B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 306
DBREF 6GI2 A 2 279 UNP Q9I0F2 Q9I0F2_PSEAE 27 304
DBREF 6GI2 B 2 279 UNP Q9I0F2 Q9I0F2_PSEAE 27 304
SEQADV 6GI2 GLY A -2 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI2 ALA A -1 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI2 MET A 0 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI2 ASN A 1 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI2 ALA A 157 UNP Q9I0F2 SER 182 ENGINEERED MUTATION
SEQADV 6GI2 GLY B -2 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI2 ALA B -1 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI2 MET B 0 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI2 ASN B 1 UNP Q9I0F2 EXPRESSION TAG
SEQADV 6GI2 ALA B 157 UNP Q9I0F2 SER 182 ENGINEERED MUTATION
SEQRES 1 A 282 GLY ALA MET ASN PRO ASP PRO GLU ALA THR MET ASP ARG
SEQRES 2 A 282 SER LEU LEU GLN ARG GLN ASP LEU PRO TYR ARG PHE SER
SEQRES 3 A 282 ALA VAL ASP LEU ASP SER VAL ASP GLY GLN ARG HIS TYR
SEQRES 4 A 282 ARG LEU TRP LEU GLY ARG PRO LEU GLN ALA PRO PRO ALA
SEQRES 5 A 282 ALA GLY TYR PRO VAL VAL TRP MET LEU ASP GLY ASN ALA
SEQRES 6 A 282 ALA VAL GLY ALA LEU ASP GLU SER THR LEU ARG ARG LEU
SEQRES 7 A 282 ALA ASP GLY ASP ALA PRO LEU LEU VAL ALA ILE GLY TYR
SEQRES 8 A 282 ARG THR PRO LEU ARG ILE ASP ARG ALA GLY ARG THR PHE
SEQRES 9 A 282 ASP TYR THR PRO ALA SER PRO GLY GLN ALA ASP GLN ARG
SEQRES 10 A 282 ASP PRO LEU ASN GLY LEU PRO SER GLY GLY ALA ASP ALA
SEQRES 11 A 282 PHE LEU ASP LEU LEU ARG ASP GLY MET ARG PRO ALA VAL
SEQRES 12 A 282 ALA ALA GLN ALA PRO LEU ASP THR ALA ARG GLN THR LEU
SEQRES 13 A 282 TRP GLY HIS ALA TYR GLY GLY LEU LEU VAL LEU HIS ALA
SEQRES 14 A 282 LEU PHE THR ARG PRO GLY GLU PHE ALA ARG TYR ALA ALA
SEQRES 15 A 282 ALA SER PRO SER LEU TRP TRP ARG ASP GLY ALA ILE LEU
SEQRES 16 A 282 GLY GLU ARG ALA GLY LEU GLU GLN ARG LEU ARG GLY LYS
SEQRES 17 A 282 ARG ALA GLU LEU LEU LEU TRP ARG GLY SER ALA GLU PRO
SEQRES 18 A 282 ALA SER PRO ARG GLY SER LEU LYS ALA GLU PRO GLY GLN
SEQRES 19 A 282 ALA MET ALA ARG LEU VAL ASP ASP LEU ARG ARG VAL ALA
SEQRES 20 A 282 GLY LEU THR LEU ASP PHE GLN PRO LEU ASP GLY LEU GLY
SEQRES 21 A 282 HIS GLY GLU THR LEU GLY ALA SER LEU ARG LEU LEU LEU
SEQRES 22 A 282 ALA ARG PRO ALA VAL GLU ARG GLN ARG
SEQRES 1 B 282 GLY ALA MET ASN PRO ASP PRO GLU ALA THR MET ASP ARG
SEQRES 2 B 282 SER LEU LEU GLN ARG GLN ASP LEU PRO TYR ARG PHE SER
SEQRES 3 B 282 ALA VAL ASP LEU ASP SER VAL ASP GLY GLN ARG HIS TYR
SEQRES 4 B 282 ARG LEU TRP LEU GLY ARG PRO LEU GLN ALA PRO PRO ALA
SEQRES 5 B 282 ALA GLY TYR PRO VAL VAL TRP MET LEU ASP GLY ASN ALA
SEQRES 6 B 282 ALA VAL GLY ALA LEU ASP GLU SER THR LEU ARG ARG LEU
SEQRES 7 B 282 ALA ASP GLY ASP ALA PRO LEU LEU VAL ALA ILE GLY TYR
SEQRES 8 B 282 ARG THR PRO LEU ARG ILE ASP ARG ALA GLY ARG THR PHE
SEQRES 9 B 282 ASP TYR THR PRO ALA SER PRO GLY GLN ALA ASP GLN ARG
SEQRES 10 B 282 ASP PRO LEU ASN GLY LEU PRO SER GLY GLY ALA ASP ALA
SEQRES 11 B 282 PHE LEU ASP LEU LEU ARG ASP GLY MET ARG PRO ALA VAL
SEQRES 12 B 282 ALA ALA GLN ALA PRO LEU ASP THR ALA ARG GLN THR LEU
SEQRES 13 B 282 TRP GLY HIS ALA TYR GLY GLY LEU LEU VAL LEU HIS ALA
SEQRES 14 B 282 LEU PHE THR ARG PRO GLY GLU PHE ALA ARG TYR ALA ALA
SEQRES 15 B 282 ALA SER PRO SER LEU TRP TRP ARG ASP GLY ALA ILE LEU
SEQRES 16 B 282 GLY GLU ARG ALA GLY LEU GLU GLN ARG LEU ARG GLY LYS
SEQRES 17 B 282 ARG ALA GLU LEU LEU LEU TRP ARG GLY SER ALA GLU PRO
SEQRES 18 B 282 ALA SER PRO ARG GLY SER LEU LYS ALA GLU PRO GLY GLN
SEQRES 19 B 282 ALA MET ALA ARG LEU VAL ASP ASP LEU ARG ARG VAL ALA
SEQRES 20 B 282 GLY LEU THR LEU ASP PHE GLN PRO LEU ASP GLY LEU GLY
SEQRES 21 B 282 HIS GLY GLU THR LEU GLY ALA SER LEU ARG LEU LEU LEU
SEQRES 22 B 282 ALA ARG PRO ALA VAL GLU ARG GLN ARG
HET FE A 301 1
HET 8SW A 302 50
HET NO3 A 303 4
HET EDO A 304 4
HET FE B 301 1
HET 8SW B 302 50
HET NO3 B 303 4
HET EDO B 304 4
HET EDO B 305 4
HET EDO B 306 4
HETNAM FE FE (III) ION
HETNAM 8SW ~{N}-[2-[[(2~{S})-2-[[2,3-BIS(OXIDANYL)
HETNAM 2 8SW PHENYL]CARBONYLAMINO]-3-[[(2~{S})-2-[[2,3-
HETNAM 3 8SW BIS(OXIDANYL)PHENYL]CARBONYLAMINO]-3-OXIDANYLIDENE-3-
HETNAM 4 8SW (PROP-2-YNYLAMINO)PROPYL]AMINO]-3-OXIDANYLIDENE-
HETNAM 5 8SW PROPYL]AMINO]-2-OXIDANYLIDENE-ETHYL]-2,3-
HETNAM 6 8SW BIS(OXIDANYL)BENZAMIDE
HETNAM NO3 NITRATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 FE 2(FE 3+)
FORMUL 4 8SW 2(C32 H32 N6 O12)
FORMUL 5 NO3 2(N O3 1-)
FORMUL 6 EDO 4(C2 H6 O2)
FORMUL 13 HOH *260(H2 O)
HELIX 1 AA1 ASP A 59 ALA A 66 1 8
HELIX 2 AA2 ASP A 68 ALA A 76 1 9
HELIX 3 AA3 ASP A 95 THR A 104 1 10
HELIX 4 AA4 GLY A 124 GLY A 135 1 12
HELIX 5 AA5 GLY A 135 ALA A 144 1 10
HELIX 6 AA6 ALA A 157 ARG A 170 1 14
HELIX 7 AA7 GLY A 189 ARG A 195 1 7
HELIX 8 AA8 GLY A 197 LEU A 202 1 6
HELIX 9 AA9 GLY A 230 ARG A 241 1 12
HELIX 10 AB1 GLU A 260 ARG A 272 1 13
HELIX 11 AB2 ARG B 10 ARG B 15 1 6
HELIX 12 AB3 ASP B 59 LEU B 67 1 9
HELIX 13 AB4 ASP B 68 ALA B 76 1 9
HELIX 14 AB5 ASP B 95 TYR B 103 1 9
HELIX 15 AB6 GLY B 124 GLY B 135 1 12
HELIX 16 AB7 GLY B 135 ALA B 142 1 8
HELIX 17 AB8 ALA B 157 ARG B 170 1 14
HELIX 18 AB9 TRP B 185 ASP B 188 5 4
HELIX 19 AC1 GLY B 189 GLU B 194 1 6
HELIX 20 AC2 GLY B 197 LEU B 202 1 6
HELIX 21 AC3 GLY B 230 ARG B 241 1 12
HELIX 22 AC4 GLU B 260 ARG B 272 1 13
SHEET 1 AA1 8 TYR A 20 ASP A 28 0
SHEET 2 AA1 8 HIS A 35 PRO A 43 -1 O LEU A 40 N SER A 23
SHEET 3 AA1 8 LEU A 82 TYR A 88 -1 O LEU A 83 N GLY A 41
SHEET 4 AA1 8 TYR A 52 MET A 57 1 N PRO A 53 O LEU A 82
SHEET 5 AA1 8 LEU A 146 HIS A 156 1 O THR A 152 N TRP A 56
SHEET 6 AA1 8 ARG A 176 ALA A 180 1 O ALA A 180 N GLY A 155
SHEET 7 AA1 8 ALA A 207 GLY A 214 1 O LEU A 210 N ALA A 179
SHEET 8 AA1 8 LEU A 246 LEU A 253 1 O GLN A 251 N LEU A 211
SHEET 1 AA2 8 TYR B 20 ASP B 28 0
SHEET 2 AA2 8 HIS B 35 PRO B 43 -1 O LEU B 38 N VAL B 25
SHEET 3 AA2 8 LEU B 82 TYR B 88 -1 O LEU B 83 N GLY B 41
SHEET 4 AA2 8 TYR B 52 MET B 57 1 N MET B 57 O ILE B 86
SHEET 5 AA2 8 LEU B 146 HIS B 156 1 O THR B 152 N TRP B 56
SHEET 6 AA2 8 ARG B 176 ALA B 180 1 O ALA B 178 N LEU B 153
SHEET 7 AA2 8 ALA B 207 GLY B 214 1 O LEU B 210 N TYR B 177
SHEET 8 AA2 8 LEU B 246 LEU B 253 1 O GLN B 251 N LEU B 211
LINK FE FE A 301 OAJ 8SW A 302 1555 1555 2.19
LINK FE FE A 301 OAI 8SW A 302 1555 1555 2.03
LINK FE FE A 301 OAM 8SW A 302 1555 1555 2.09
LINK FE FE A 301 OAL 8SW A 302 1555 1555 2.09
LINK FE FE A 301 OAH 8SW A 302 1555 1555 2.07
LINK FE FE A 301 OAK 8SW A 302 1555 1555 2.12
LINK FE FE B 301 OAI 8SW B 302 1555 1555 2.13
LINK FE FE B 301 OAL 8SW B 302 1555 1555 2.13
LINK FE FE B 301 OAH 8SW B 302 1555 1555 2.06
LINK FE FE B 301 OAK 8SW B 302 1555 1555 1.95
LINK FE FE B 301 OAM 8SW B 302 1555 1555 2.10
LINK FE FE B 301 OAJ 8SW B 302 1555 1555 2.13
SITE 1 AC1 1 8SW A 302
SITE 1 AC2 25 ARG A 96 ARG A 99 LEU A 117 ALA A 157
SITE 2 AC2 25 TYR A 158 SER A 183 TRP A 185 PRO A 218
SITE 3 AC2 25 PRO A 221 HIS A 258 FE A 301 HOH A 401
SITE 4 AC2 25 HOH A 415 HOH A 437 HOH A 457 HOH A 462
SITE 5 AC2 25 HOH A 466 HOH A 469 HOH A 470 HOH A 486
SITE 6 AC2 25 HOH A 509 GLY B 193 ARG B 195 ALA B 196
SITE 7 AC2 25 ASP B 239
SITE 1 AC3 6 ALA A 264 ARG A 267 LEU A 268 ALA B 264
SITE 2 AC3 6 ARG B 267 LEU B 268
SITE 1 AC4 4 SER A 29 VAL A 30 HOH A 406 HOH B 421
SITE 1 AC5 1 8SW B 302
SITE 1 AC6 13 GLN A 16 ASP A 17 LEU B 117 ALA B 157
SITE 2 AC6 13 TYR B 158 TRP B 185 PRO B 218 PRO B 221
SITE 3 AC6 13 HIS B 258 FE B 301 EDO B 305 HOH B 401
SITE 4 AC6 13 HOH B 468
SITE 1 AC7 7 ARG B 213 ALA B 219 GLY B 230 GLN B 231
SITE 2 AC7 7 ALA B 232 MET B 233 HOH B 426
SITE 1 AC8 8 PRO B 81 LEU B 270 ARG B 272 PRO B 273
SITE 2 AC8 8 ALA B 274 HOH B 405 HOH B 445 HOH B 476
SITE 1 AC9 10 SER B 181 PRO B 182 TRP B 185 ARG B 213
SITE 2 AC9 10 GLU B 217 PRO B 218 HIS B 258 8SW B 302
SITE 3 AC9 10 HOH B 401 HOH B 430
SITE 1 AD1 5 ARG B 74 LEU B 270 ALA B 271 HOH B 406
SITE 2 AD1 5 HOH B 443
CRYST1 57.794 76.602 129.867 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 0.017303 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013054 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007700 0.00000
TER 2027 GLU A 276
TER 4090 ARG B 277
MASTER 418 0 10 22 16 0 25 6 4396 2 128 44
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