HEADER OXIDOREDUCTASE 18-DEC-12 3ZGJ
TITLE S221M V223F Y359A MUTANT OF 4-HYDROXYMANDELATE SYNTHASE FROM
TITLE 2 STREPTOMYCES COELICOLOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 4-HYDROXYPHENYLPYRUVIC ACID DIOXYGENASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 4-HYDROXYMANDELATE SYNTHASE;
COMPND 5 EC: 1.13.11.46;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;
SOURCE 3 ORGANISM_TAXID: 100226;
SOURCE 4 STRAIN: A3(2);
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS OXIDOREDUCTASE, DIOXYGENASE, NON-HEME IRON OXYGENASE, BENZYLIC
KEYWDS 2 HYDROXYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.PRATTER,G.STRAGANZ,G.GROGAN
REVDAT 2 20-DEC-23 3ZGJ 1 REMARK LINK
REVDAT 1 30-OCT-13 3ZGJ 0
JRNL AUTH S.PRATTER,C.KONSTANTINOVICS,C.L.M.DIGIURO,E.LEITNER,D.KUMAR,
JRNL AUTH 2 S.P.DE VISSER,G.GROGAN,G.STRAGANZ
JRNL TITL INVERSION OF ENANTIOSELECTIVITY OF A MONONUCLEAR NON-HEME
JRNL TITL 2 IRON(II)-DEPENDENT HYDROXYLASE BY TUNING THE INTERPLAY OF
JRNL TITL 3 METAL CENTER GEOMETRY AND PROTEIN STRUCTURE
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 52 9677 2013
JRNL REFN ISSN 1433-7851
JRNL PMID 23881738
JRNL DOI 10.1002/ANGE.201304633
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 54.95
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 57014
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3049
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4191
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2190
REMARK 3 BIN FREE R VALUE SET COUNT : 196
REMARK 3 BIN FREE R VALUE : 0.2730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5051
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 531
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.81
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.68000
REMARK 3 B22 (A**2) : -0.68000
REMARK 3 B33 (A**2) : 1.37000
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): 0.140
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.134
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.268
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5197 ; 0.021 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7090 ; 2.002 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 665 ; 6.715 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 236 ;33.114 ;22.669
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 727 ;14.576 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 49 ;18.129 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 798 ; 0.156 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4083 ; 0.012 ; 0.021
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): 2675 ; 3.494 ; 3.249
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3332 ; 4.683 ; 4.837
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2522 ; 4.594 ; 3.574
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 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
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 3ZGJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-DEC-12.
REMARK 100 THE DEPOSITION ID IS D_1290055174.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I02
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97950
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57014
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 61.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.90
REMARK 200 R MERGE FOR SHELL (I) : 0.49000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2R5V
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 MICROLITRE 10 MG ML-1 HMS VARIANT,
REMARK 280 PREINCUBATED WITH 1.25 MM COCL2 AND 2.5 MM R-MANDELATE) PLUS 1
REMARK 280 MICROLITRE MOTHER LIQUOR. THE BEST CRYSTALS WERE ROUTINELY
REMARK 280 OBTAINED IN CRYSTAL DROPS CONTAINING 0.05 M TRIS/CL PH 9.0, 0.1
REMARK 280 M MGCL2, 7.5% (W/V) PEG 4K AND 2.5% (V/V) 2-METHYL-1,4-
REMARK 280 PENTANEDIOL., PH 8.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 PRO A 3
REMARK 465 PRO A 4
REMARK 465 PHE A 5
REMARK 465 PRO A 6
REMARK 465 PHE A 7
REMARK 465 LEU A 8
REMARK 465 HIS A 9
REMARK 465 TRP A 10
REMARK 465 ARG A 11
REMARK 465 ALA A 12
REMARK 465 ALA A 13
REMARK 465 MET A 14
REMARK 465 PRO A 122
REMARK 465 SER A 123
REMARK 465 HIS A 124
REMARK 465 ARG A 125
REMARK 465 ALA A 126
REMARK 465 GLY A 127
REMARK 465 GLN A 128
REMARK 465 ASP A 129
REMARK 465 ALA A 130
REMARK 465 TRP A 131
REMARK 465 ALA A 149
REMARK 465 ASP A 150
REMARK 465 GLY A 151
REMARK 465 ASP A 152
REMARK 465 GLY A 153
REMARK 465 ALA A 154
REMARK 465 GLY A 155
REMARK 465 THR A 295
REMARK 465 GLU A 296
REMARK 465 ARG A 297
REMARK 465 VAL A 298
REMARK 465 GLY A 299
REMARK 465 ALA A 300
REMARK 465 MET A 301
REMARK 465 ALA A 302
REMARK 465 ASP A 303
REMARK 465 VAL A 368
REMARK 465 ALA A 369
REMARK 465 GLY A 370
REMARK 465 ARG A 371
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 PRO B 3
REMARK 465 PRO B 4
REMARK 465 PHE B 5
REMARK 465 PRO B 6
REMARK 465 PHE B 7
REMARK 465 LEU B 8
REMARK 465 HIS B 9
REMARK 465 TRP B 10
REMARK 465 ARG B 11
REMARK 465 ALA B 12
REMARK 465 ALA B 13
REMARK 465 ALA B 149
REMARK 465 ASP B 150
REMARK 465 GLY B 151
REMARK 465 ASP B 152
REMARK 465 GLY B 153
REMARK 465 ALA B 154
REMARK 465 GLY B 155
REMARK 465 ARG B 297
REMARK 465 VAL B 298
REMARK 465 GLY B 299
REMARK 465 ALA B 300
REMARK 465 VAL B 368
REMARK 465 ALA B 369
REMARK 465 GLY B 370
REMARK 465 ARG B 371
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ASP A 78 CG OD1 OD2
REMARK 470 ARG A 103 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 118 CG CD OE1 NE2
REMARK 470 LEU A 156 CG CD1 CD2
REMARK 470 ARG A 172 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 196 CG CD OE1 OE2
REMARK 470 GLU A 216 CG CD OE1 OE2
REMARK 470 ARG A 285 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 306 CG CD OE1 OE2
REMARK 470 ARG A 317 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 319 CG CD OE1 OE2
REMARK 470 ARG A 366 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 367 CG CD OE1 OE2
REMARK 470 MET B 14 CG SD CE
REMARK 470 GLU B 86 CG CD OE1 OE2
REMARK 470 ASP B 129 CG OD1 OD2
REMARK 470 GLU B 216 CG CD OE1 OE2
REMARK 470 GLU B 296 CG CD OE1 OE2
REMARK 470 MET B 301 CG SD CE
REMARK 470 ASP B 303 CG OD1 OD2
REMARK 470 TYR B 322 CG CD1 CD2 CE1 CE2 CZ OH
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 2079 O HOH B 2249 2.01
REMARK 500 O HOH A 2073 O HOH A 2079 2.05
REMARK 500 NH2 ARG B 30 O HOH B 2023 2.09
REMARK 500 O HOH A 2079 O HOH A 2142 2.11
REMARK 500 OD1 ASP B 38 O HOH B 2043 2.13
REMARK 500 OE2 GLU A 310 O HOH A 2194 2.16
REMARK 500 O HOH A 2079 O HOH B 2251 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 ASP A 162 N - CA - CB ANGL. DEV. = -20.7 DEGREES
REMARK 500 LEU A 166 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 ASP A 240 CB - CG - OD1 ANGL. DEV. = 6.4 DEGREES
REMARK 500 ASP A 240 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 LEU B 24 CA - CB - CG ANGL. DEV. = 14.3 DEGREES
REMARK 500 ASP B 94 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP B 101 CB - CG - OD1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG B 161 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG B 161 NE - CZ - NH2 ANGL. DEV. = -6.5 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 112 1.76 -64.47
REMARK 500 PRO A 120 69.59 -52.63
REMARK 500 ARG A 242 -169.99 -122.57
REMARK 500 THR A 336 -87.91 -104.91
REMARK 500 ASN A 345 69.04 -113.58
REMARK 500 TYR B 206 129.90 -39.27
REMARK 500 THR B 295 46.37 120.56
REMARK 500 ASP B 318 -165.08 -112.28
REMARK 500 THR B 336 -91.38 -101.03
REMARK 500 ASN B 345 66.32 -118.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2035 DISTANCE = 6.50 ANGSTROMS
REMARK 525 HOH B2069 DISTANCE = 6.12 ANGSTROMS
REMARK 525 HOH B2165 DISTANCE = 7.13 ANGSTROMS
REMARK 525 HOH B2309 DISTANCE = 6.71 ANGSTROMS
REMARK 525 HOH B2310 DISTANCE = 7.03 ANGSTROMS
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 CO A1368 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 181 NE2
REMARK 620 2 HIS A 261 NE2 114.1
REMARK 620 3 GLU A 340 OE1 96.6 89.2
REMARK 620 4 RMN A1369 O8 92.5 87.4 171.0
REMARK 620 5 RMN A1369 O12 112.7 132.4 94.0 82.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CO B1368 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 181 NE2
REMARK 620 2 HIS B 261 NE2 116.7
REMARK 620 3 GLU B 340 OE1 104.0 95.8
REMARK 620 4 RMN B1369 O12 114.0 123.9 93.8
REMARK 620 5 RMN B1369 O8 93.1 87.9 158.4 66.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO B 1368
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO A 1368
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RMN B 1369
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RMN A 1369
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 SER221MET VAL223PHE TYR359ALA MUTATIONS
DBREF 3ZGJ A 1 371 UNP Q9Z4X7 Q9Z4X7_STRCO 1 371
DBREF 3ZGJ B 1 371 UNP Q9Z4X7 Q9Z4X7_STRCO 1 371
SEQADV 3ZGJ MET A 221 UNP Q9Z4X7 SER 221 ENGINEERED MUTATION
SEQADV 3ZGJ PHE A 223 UNP Q9Z4X7 VAL 223 ENGINEERED MUTATION
SEQADV 3ZGJ ALA A 359 UNP Q9Z4X7 TYR 359 ENGINEERED MUTATION
SEQADV 3ZGJ MET B 221 UNP Q9Z4X7 SER 221 ENGINEERED MUTATION
SEQADV 3ZGJ PHE B 223 UNP Q9Z4X7 VAL 223 ENGINEERED MUTATION
SEQADV 3ZGJ ALA B 359 UNP Q9Z4X7 TYR 359 ENGINEERED MUTATION
SEQRES 1 A 371 MET LEU PRO PRO PHE PRO PHE LEU HIS TRP ARG ALA ALA
SEQRES 2 A 371 MET PRO PRO SER ASP ILE ALA TYR ALA GLU LEU TYR VAL
SEQRES 3 A 371 ALA ASP ASP ARG GLU ALA SER GLY PHE LEU VAL ASP SER
SEQRES 4 A 371 LEU GLY PHE VAL PRO LEU ALA VAL ALA GLY PRO ALA THR
SEQRES 5 A 371 GLY THR HIS ASP ARG ARG SER THR VAL LEU ARG SER GLY
SEQRES 6 A 371 GLU VAL THR LEU VAL VAL THR GLN ALA LEU ALA PRO ASP
SEQRES 7 A 371 THR PRO VAL ALA ARG TYR VAL GLU ARG HIS GLY ASP SER
SEQRES 8 A 371 ILE ALA ASP LEU ALA PHE GLY CYS ASP ASP VAL ARG SER
SEQRES 9 A 371 CYS PHE ASP ARG ALA VAL LEU ALA GLY ALA GLU ALA LEU
SEQRES 10 A 371 GLN ALA PRO THR PRO SER HIS ARG ALA GLY GLN ASP ALA
SEQRES 11 A 371 TRP PHE ALA THR VAL SER GLY PHE GLY ASP ILE ARG HIS
SEQRES 12 A 371 THR LEU VAL PRO ALA ALA ASP GLY ASP GLY ALA GLY LEU
SEQRES 13 A 371 LEU PRO PRO ASP ARG ASP TRP ALA LEU LEU PRO ALA ALA
SEQRES 14 A 371 THR GLY ARG THR GLY PRO ARG PRO LEU LEU ASP HIS VAL
SEQRES 15 A 371 ALA VAL CYS LEU GLU SER GLY THR LEU ARG SER THR ALA
SEQRES 16 A 371 GLU PHE TYR GLU ALA ALA PHE ASP MET PRO TYR TYR SER
SEQRES 17 A 371 SER GLU TYR ILE GLU VAL GLY GLU GLN ALA MET ASP MET
SEQRES 18 A 371 ILE PHE VAL ARG ASN ALA GLY GLY GLY ILE THR PHE THR
SEQRES 19 A 371 LEU ILE GLU PRO ASP ASP THR ARG VAL PRO GLY GLN ILE
SEQRES 20 A 371 ASP GLN PHE LEU SER ALA HIS ASP GLY PRO GLY VAL GLN
SEQRES 21 A 371 HIS LEU ALA PHE LEU VAL ASP ASP ILE VAL GLY SER VAL
SEQRES 22 A 371 ARG SER LEU GLY ASP ARG GLY VAL ALA PHE LEU ARG THR
SEQRES 23 A 371 PRO GLY ALA TYR TYR ASP LEU LEU THR GLU ARG VAL GLY
SEQRES 24 A 371 ALA MET ALA ASP ALA ILE GLU ASP LEU ARG GLU THR ASN
SEQRES 25 A 371 VAL LEU ALA ASP ARG ASP GLU TRP GLY TYR LEU LEU GLN
SEQRES 26 A 371 ILE PHE THR ARG SER PRO TYR PRO ARG GLY THR LEU PHE
SEQRES 27 A 371 TYR GLU TYR ILE GLN ARG ASN GLY ALA ARG GLY PHE GLY
SEQRES 28 A 371 SER SER ASN ILE LYS ALA LEU ALA GLU ALA VAL GLU ARG
SEQRES 29 A 371 GLU ARG GLU VAL ALA GLY ARG
SEQRES 1 B 371 MET LEU PRO PRO PHE PRO PHE LEU HIS TRP ARG ALA ALA
SEQRES 2 B 371 MET PRO PRO SER ASP ILE ALA TYR ALA GLU LEU TYR VAL
SEQRES 3 B 371 ALA ASP ASP ARG GLU ALA SER GLY PHE LEU VAL ASP SER
SEQRES 4 B 371 LEU GLY PHE VAL PRO LEU ALA VAL ALA GLY PRO ALA THR
SEQRES 5 B 371 GLY THR HIS ASP ARG ARG SER THR VAL LEU ARG SER GLY
SEQRES 6 B 371 GLU VAL THR LEU VAL VAL THR GLN ALA LEU ALA PRO ASP
SEQRES 7 B 371 THR PRO VAL ALA ARG TYR VAL GLU ARG HIS GLY ASP SER
SEQRES 8 B 371 ILE ALA ASP LEU ALA PHE GLY CYS ASP ASP VAL ARG SER
SEQRES 9 B 371 CYS PHE ASP ARG ALA VAL LEU ALA GLY ALA GLU ALA LEU
SEQRES 10 B 371 GLN ALA PRO THR PRO SER HIS ARG ALA GLY GLN ASP ALA
SEQRES 11 B 371 TRP PHE ALA THR VAL SER GLY PHE GLY ASP ILE ARG HIS
SEQRES 12 B 371 THR LEU VAL PRO ALA ALA ASP GLY ASP GLY ALA GLY LEU
SEQRES 13 B 371 LEU PRO PRO ASP ARG ASP TRP ALA LEU LEU PRO ALA ALA
SEQRES 14 B 371 THR GLY ARG THR GLY PRO ARG PRO LEU LEU ASP HIS VAL
SEQRES 15 B 371 ALA VAL CYS LEU GLU SER GLY THR LEU ARG SER THR ALA
SEQRES 16 B 371 GLU PHE TYR GLU ALA ALA PHE ASP MET PRO TYR TYR SER
SEQRES 17 B 371 SER GLU TYR ILE GLU VAL GLY GLU GLN ALA MET ASP MET
SEQRES 18 B 371 ILE PHE VAL ARG ASN ALA GLY GLY GLY ILE THR PHE THR
SEQRES 19 B 371 LEU ILE GLU PRO ASP ASP THR ARG VAL PRO GLY GLN ILE
SEQRES 20 B 371 ASP GLN PHE LEU SER ALA HIS ASP GLY PRO GLY VAL GLN
SEQRES 21 B 371 HIS LEU ALA PHE LEU VAL ASP ASP ILE VAL GLY SER VAL
SEQRES 22 B 371 ARG SER LEU GLY ASP ARG GLY VAL ALA PHE LEU ARG THR
SEQRES 23 B 371 PRO GLY ALA TYR TYR ASP LEU LEU THR GLU ARG VAL GLY
SEQRES 24 B 371 ALA MET ALA ASP ALA ILE GLU ASP LEU ARG GLU THR ASN
SEQRES 25 B 371 VAL LEU ALA ASP ARG ASP GLU TRP GLY TYR LEU LEU GLN
SEQRES 26 B 371 ILE PHE THR ARG SER PRO TYR PRO ARG GLY THR LEU PHE
SEQRES 27 B 371 TYR GLU TYR ILE GLN ARG ASN GLY ALA ARG GLY PHE GLY
SEQRES 28 B 371 SER SER ASN ILE LYS ALA LEU ALA GLU ALA VAL GLU ARG
SEQRES 29 B 371 GLU ARG GLU VAL ALA GLY ARG
HET CO A1368 1
HET RMN A1369 11
HET CO B1368 1
HET RMN B1369 11
HETNAM CO COBALT (II) ION
HETNAM RMN (R)-MANDELIC ACID
FORMUL 3 CO 2(CO 2+)
FORMUL 4 RMN 2(C8 H8 O3)
FORMUL 7 HOH *531(H2 O)
HELIX 1 1 ASP A 28 SER A 39 1 12
HELIX 2 2 GLY A 49 GLY A 53 5 5
HELIX 3 3 THR A 79 GLY A 89 1 11
HELIX 4 4 ASP A 101 ALA A 112 1 12
HELIX 5 5 PRO A 167 GLY A 171 5 5
HELIX 6 6 THR A 190 ASP A 203 1 14
HELIX 7 7 GLY A 245 ASP A 255 1 11
HELIX 8 8 ASP A 268 ARG A 279 1 12
HELIX 9 9 PRO A 287 LEU A 294 1 8
HELIX 10 10 ALA A 304 ASN A 312 1 9
HELIX 11 11 GLY A 351 GLU A 367 1 17
HELIX 12 12 ASP B 28 SER B 39 1 12
HELIX 13 13 GLY B 49 GLY B 53 5 5
HELIX 14 14 THR B 79 GLY B 89 1 11
HELIX 15 15 ASP B 101 ALA B 112 1 12
HELIX 16 16 PRO B 167 GLY B 171 5 5
HELIX 17 17 THR B 190 ASP B 203 1 14
HELIX 18 18 GLY B 245 HIS B 254 1 10
HELIX 19 19 ASP B 268 ARG B 279 1 12
HELIX 20 20 PRO B 287 LEU B 294 1 8
HELIX 21 21 MET B 301 ASN B 312 1 12
HELIX 22 22 GLY B 351 GLU B 367 1 17
SHEET 1 AA 9 ALA A 116 GLN A 118 0
SHEET 2 AA 9 ALA A 133 SER A 136 -1 O THR A 134 N LEU A 117
SHEET 3 AA 9 ARG A 142 PRO A 147 -1 O HIS A 143 N VAL A 135
SHEET 4 AA 9 SER A 91 CYS A 99 1 O ALA A 93 N ARG A 142
SHEET 5 AA 9 ASP A 18 VAL A 26 -1 O ASP A 18 N GLY A 98
SHEET 6 AA 9 VAL A 67 ALA A 74 1 O THR A 68 N ALA A 22
SHEET 7 AA 9 ARG A 57 SER A 64 -1 O ARG A 58 N GLN A 73
SHEET 8 AA 9 VAL A 43 ALA A 48 -1 O VAL A 43 N ARG A 63
SHEET 9 AA 9 ALA A 164 LEU A 165 -1 O ALA A 164 N VAL A 47
SHEET 1 AB 8 TYR A 206 VAL A 214 0
SHEET 2 AB 8 GLN A 217 ARG A 225 -1 O GLN A 217 N VAL A 214
SHEET 3 AB 8 THR A 232 PRO A 238 -1 O PHE A 233 N VAL A 224
SHEET 4 AB 8 LEU A 178 CYS A 185 1 O VAL A 182 N THR A 234
SHEET 5 AB 8 GLY A 258 LEU A 265 -1 O GLY A 258 N CYS A 185
SHEET 6 AB 8 PHE A 338 ARG A 344 1 O PHE A 338 N LEU A 262
SHEET 7 AB 8 GLY A 321 PHE A 327 -1 O LEU A 324 N GLN A 343
SHEET 8 AB 8 LEU A 314 ASP A 318 -1 O LEU A 314 N GLN A 325
SHEET 1 BA 9 ALA B 116 PRO B 122 0
SHEET 2 BA 9 TRP B 131 SER B 136 -1 O PHE B 132 N THR B 121
SHEET 3 BA 9 ARG B 142 PRO B 147 -1 O HIS B 143 N VAL B 135
SHEET 4 BA 9 SER B 91 CYS B 99 1 O ALA B 93 N ARG B 142
SHEET 5 BA 9 ASP B 18 VAL B 26 -1 O ASP B 18 N GLY B 98
SHEET 6 BA 9 VAL B 67 ALA B 74 1 O THR B 68 N ALA B 22
SHEET 7 BA 9 ARG B 57 SER B 64 -1 O ARG B 58 N GLN B 73
SHEET 8 BA 9 VAL B 43 ALA B 48 -1 O VAL B 43 N ARG B 63
SHEET 9 BA 9 ALA B 164 LEU B 165 -1 O ALA B 164 N VAL B 47
SHEET 1 BB 8 TYR B 206 VAL B 214 0
SHEET 2 BB 8 GLN B 217 ARG B 225 -1 O GLN B 217 N VAL B 214
SHEET 3 BB 8 THR B 232 PRO B 238 -1 O PHE B 233 N VAL B 224
SHEET 4 BB 8 LEU B 178 CYS B 185 1 O VAL B 182 N THR B 234
SHEET 5 BB 8 GLY B 258 LEU B 265 -1 O GLY B 258 N CYS B 185
SHEET 6 BB 8 PHE B 338 ARG B 344 1 O PHE B 338 N LEU B 262
SHEET 7 BB 8 GLY B 321 PHE B 327 -1 O LEU B 324 N GLN B 343
SHEET 8 BB 8 LEU B 314 ASP B 318 -1 O LEU B 314 N GLN B 325
SSBOND 1 CYS B 99 CYS B 105 1555 1555 2.29
LINK NE2 HIS A 181 CO CO A1368 1555 1555 2.08
LINK NE2 HIS A 261 CO CO A1368 1555 1555 2.11
LINK OE1 GLU A 340 CO CO A1368 1555 1555 2.06
LINK CO CO A1368 O8 RMN A1369 1555 1555 2.34
LINK CO CO A1368 O12 RMN A1369 1555 1555 2.06
LINK NE2 HIS B 181 CO CO B1368 1555 1555 2.05
LINK NE2 HIS B 261 CO CO B1368 1555 1555 2.07
LINK OE1 GLU B 340 CO CO B1368 1555 1555 1.77
LINK CO CO B1368 O12 RMN B1369 1555 1555 2.10
LINK CO CO B1368 O8 RMN B1369 1555 1555 2.33
CISPEP 1 ARG A 176 PRO A 177 0 -5.99
CISPEP 2 ARG B 176 PRO B 177 0 -2.46
SITE 1 AC1 4 HIS B 181 HIS B 261 GLU B 340 RMN B1369
SITE 1 AC2 4 HIS A 181 HIS A 261 GLU A 340 RMN A1369
SITE 1 AC3 10 HIS B 181 THR B 234 ILE B 236 HIS B 261
SITE 2 AC3 10 GLN B 325 GLU B 340 PHE B 350 ILE B 355
SITE 3 AC3 10 CO B1368 HOH B2232
SITE 1 AC4 8 HIS A 181 THR A 234 HIS A 261 GLN A 325
SITE 2 AC4 8 GLU A 340 PHE A 350 ILE A 355 CO A1368
CRYST1 122.870 122.870 54.860 90.00 90.00 90.00 P 4 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 0.008139 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008139 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018228 0.00000
(ATOM LINES ARE NOT SHOWN.)
END