HEADER OXIDOREDUCTASE 18-JAN-05 1YKJ
TITLE A45G P-HYDROXYBENZOATE HYDROXYLASE WITH P-HYDROXYBENZOATE BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P-HYDROXYBENZOATE HYDROXYLASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: 4-HYDROXYBENZOATE 3-MONOOXYGENASE, PHBH;
COMPND 5 EC: 1.14.13.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: POBA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM105;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PIE130 (A DERIVATIVE OF PUC18)
KEYWDS PHBH, CATALYSIS, CONFORMATIONS, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.J.COLE,D.L.GATTI,B.ENTSCH,D.P.BALLOU
REVDAT 5 23-AUG-23 1YKJ 1 REMARK
REVDAT 4 20-OCT-21 1YKJ 1 REMARK SEQADV
REVDAT 3 16-NOV-11 1YKJ 1 VERSN HETATM
REVDAT 2 24-FEB-09 1YKJ 1 VERSN
REVDAT 1 26-JUL-05 1YKJ 0
JRNL AUTH L.J.COLE,D.L.GATTI,B.ENTSCH,D.P.BALLOU
JRNL TITL REMOVAL OF A METHYL GROUP CAUSES GLOBAL CHANGES IN
JRNL TITL 2 P-HYDROXYBENZOATE HYDROXYLASE.
JRNL REF BIOCHEMISTRY V. 44 8047 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15924424
JRNL DOI 10.1021/BI050108X
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 446344.110
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 59975
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 SET) : 0.201
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.200
REMARK 3 FREE R VALUE TEST SET COUNT : 6131
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.003
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.50
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8709
REMARK 3 BIN R VALUE (WORKING SET) : 0.2830
REMARK 3 BIN FREE R VALUE : 0.3220
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 10.40
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 1008
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6212
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 204
REMARK 3 SOLVENT ATOMS : 542
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 26.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.32000
REMARK 3 B22 (A**2) : 1.77000
REMARK 3 B33 (A**2) : -3.09000
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.23
REMARK 3 ESD FROM SIGMAA (A) : 0.27
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.31
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.30
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.017
REMARK 3 BOND ANGLES (DEGREES) : 1.900
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 1.220
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 3.530 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 4.680 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 5.390 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 7.110 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.40
REMARK 3 BSOL : 83.65
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : DNA-RNA_REP.PARAM
REMARK 3 PARAMETER FILE 3 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 4 : ION.PARAM
REMARK 3 PARAMETER FILE 5 : PHB_FAD_PYS.PARA
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : DNA-RNA.TOP
REMARK 3 TOPOLOGY FILE 3 : WATER.TOP
REMARK 3 TOPOLOGY FILE 4 : ION.TOP
REMARK 3 TOPOLOGY FILE 5 : PHB_FAD_PYS.TOPH
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1YKJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-05.
REMARK 100 THE DEPOSITION ID IS D_1000031619.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU FR-D
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : OSMIC CONFOCAL
REMARK 200 OPTICS : OSMIC CONFOCAL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR (MSC/RIGAKU)
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76039
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.740
REMARK 200 RESOLUTION RANGE LOW (A) : 31.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.0
REMARK 200 DATA REDUNDANCY : 11.89
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : 0.09000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1IUW
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, TRIS-SULFATE, FAD,
REMARK 280 EDTA, GLUTATHION, SODIUM SULFITE, P-HYDROXYBENZOATE, PH 8.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 310K
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 34.93000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.94850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.93000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.94850
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: 8900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30060 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -180.0 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21340 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 56560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -369.0 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 BIOMT1 2 -1.000000 0.000000 0.000000 139.72000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 85.89700
REMARK 350 BIOMT3 2 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 B3447 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 ASP B 2068
REMARK 465 GLY B 2069
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 ARG B2063 CG CD NE CZ NH1 NH2
REMARK 470 ARG B2064 CG CD NE CZ NH1 NH2
REMARK 470 MET B2065 CG SD CE
REMARK 470 ARG B2067 CG CD NE CZ NH1 NH2
REMARK 470 LEU B2070 CG CD1 CD2
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 OD2 ASP B 2233 O HOH B 3016 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OD1 ASP A 1357 OE2 GLU B 2172 2765 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 A1179 NE - CZ - NH1 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG B2147 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG B2147 NE - CZ - NH2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 LEU B2255 CA - CB - CG ANGL. DEV. = 14.5 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 ARG A1044 -135.04 54.77
REMARK 500 PRO A1182 27.65 -79.11
REMARK 500 SER A1212 -164.81 -126.26
REMARK 500 HIS A1278 113.33 -175.26
REMARK 500 GLU A1319 5.06 -171.52
REMARK 500 ASP A1355 73.42 32.19
REMARK 500 GLU A1391 -141.24 -74.83
REMARK 500 ILE A1393 138.00 78.42
REMARK 500 ARG B2044 -130.76 52.40
REMARK 500 VAL B2061 -122.12 -112.24
REMARK 500 ASP B2062 77.69 16.49
REMARK 500 ARG B2064 75.03 -118.90
REMARK 500 MET B2065 0.36 -69.38
REMARK 500 ALA B2066 -83.68 -111.93
REMARK 500 ALA B2080 66.72 35.18
REMARK 500 ASP B2087 82.33 -68.57
REMARK 500 TYR B2100 118.21 -164.62
REMARK 500 PRO B2182 41.90 -78.35
REMARK 500 ASP B2191 55.65 -91.09
REMARK 500 PRO B2275 -164.65 -79.59
REMARK 500 HIS B2278 114.62 -163.87
REMARK 500 GLU B2323 -19.17 -45.32
REMARK 500 TYR B2390 105.81 -59.03
REMARK 500 GLU B2391 156.30 -39.83
REMARK 500 ILE B2393 -176.14 62.12
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 PSL IS PYROSULFATE (S2O7(2-)). THE MAP IS CLEAR,
REMARK 600 HOWEVER PYROSULFATE WAS NOT ADDED TO THE HOLDING
REMARK 600 SOLUTION. IT COULD HAVE BEEN A CONTAMINATION FROM
REMARK 600 AMMONIUM SULFATE. IT COULD ALSO BE PYROPHOSPHATE,
REMARK 600 POSSIBLY ORIGINATING FROM A DEGRADATION OF FAD.
REMARK 600 HOWEVER, IT IS IMPOSSIBLE TO DISCRIMINATE BETWEEN
REMARK 600 PYROSULFATE OR PYROPHOSPHATE BASED ON THE MAP OR
REMARK 600 THE REFINEMENT).
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 708
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 709
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 711
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 712
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 713
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 1395
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 2395
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHB A 1396
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHB B 2396
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSL B 714
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSL B 715
DBREF 1YKJ A 1001 1394 UNP P20586 PHHY_PSEAE 1 394
DBREF 1YKJ B 2001 2394 UNP P20586 PHHY_PSEAE 1 394
SEQADV 1YKJ GLY A 1045 UNP P20586 ALA 45 ENGINEERED MUTATION
SEQADV 1YKJ GLY B 2045 UNP P20586 ALA 45 ENGINEERED MUTATION
SEQRES 1 A 394 MET LYS THR GLN VAL ALA ILE ILE GLY ALA GLY PRO SER
SEQRES 2 A 394 GLY LEU LEU LEU GLY GLN LEU LEU HIS LYS ALA GLY ILE
SEQRES 3 A 394 ASP ASN VAL ILE LEU GLU ARG GLN THR PRO ASP TYR VAL
SEQRES 4 A 394 LEU GLY ARG ILE ARG GLY GLY VAL LEU GLU GLN GLY MET
SEQRES 5 A 394 VAL ASP LEU LEU ARG GLU ALA GLY VAL ASP ARG ARG MET
SEQRES 6 A 394 ALA ARG ASP GLY LEU VAL HIS GLU GLY VAL GLU ILE ALA
SEQRES 7 A 394 PHE ALA GLY GLN ARG ARG ARG ILE ASP LEU LYS ARG LEU
SEQRES 8 A 394 SER GLY GLY LYS THR VAL THR VAL TYR GLY GLN THR GLU
SEQRES 9 A 394 VAL THR ARG ASP LEU MET GLU ALA ARG GLU ALA CYS GLY
SEQRES 10 A 394 ALA THR THR VAL TYR GLN ALA ALA GLU VAL ARG LEU HIS
SEQRES 11 A 394 ASP LEU GLN GLY GLU ARG PRO TYR VAL THR PHE GLU ARG
SEQRES 12 A 394 ASP GLY GLU ARG LEU ARG LEU ASP CYS ASP TYR ILE ALA
SEQRES 13 A 394 GLY CYS ASP GLY PHE HIS GLY ILE SER ARG GLN SER ILE
SEQRES 14 A 394 PRO ALA GLU ARG LEU LYS VAL PHE GLU ARG VAL TYR PRO
SEQRES 15 A 394 PHE GLY TRP LEU GLY LEU LEU ALA ASP THR PRO PRO VAL
SEQRES 16 A 394 SER HIS GLU LEU ILE TYR ALA ASN HIS PRO ARG GLY PHE
SEQRES 17 A 394 ALA LEU CYS SER GLN ARG SER ALA THR ARG SER ARG TYR
SEQRES 18 A 394 TYR VAL GLN VAL PRO LEU SER GLU LYS VAL GLU ASP TRP
SEQRES 19 A 394 SER ASP GLU ARG PHE TRP THR GLU LEU LYS ALA ARG LEU
SEQRES 20 A 394 PRO SER GLU VAL ALA GLU LYS LEU VAL THR GLY PRO SER
SEQRES 21 A 394 LEU GLU LYS SER ILE ALA PRO LEU ARG SER PHE VAL VAL
SEQRES 22 A 394 GLU PRO MET GLN HIS GLY ARG LEU PHE LEU ALA GLY ASP
SEQRES 23 A 394 ALA ALA HIS ILE VAL PRO PRO THR GLY ALA LYS GLY LEU
SEQRES 24 A 394 ASN LEU ALA ALA SER ASP VAL SER THR LEU TYR ARG LEU
SEQRES 25 A 394 LEU LEU LYS ALA TYR ARG GLU GLY ARG GLY GLU LEU LEU
SEQRES 26 A 394 GLU ARG TYR SER ALA ILE CYS LEU ARG ARG ILE TRP LYS
SEQRES 27 A 394 ALA GLU ARG PHE SER TRP TRP MET THR SER VAL LEU HIS
SEQRES 28 A 394 ARG PHE PRO ASP THR ASP ALA PHE SER GLN ARG ILE GLN
SEQRES 29 A 394 GLN THR GLU LEU GLU TYR TYR LEU GLY SER GLU ALA GLY
SEQRES 30 A 394 LEU ALA THR ILE ALA GLU ASN TYR VAL GLY LEU PRO TYR
SEQRES 31 A 394 GLU GLU ILE GLU
SEQRES 1 B 394 MET LYS THR GLN VAL ALA ILE ILE GLY ALA GLY PRO SER
SEQRES 2 B 394 GLY LEU LEU LEU GLY GLN LEU LEU HIS LYS ALA GLY ILE
SEQRES 3 B 394 ASP ASN VAL ILE LEU GLU ARG GLN THR PRO ASP TYR VAL
SEQRES 4 B 394 LEU GLY ARG ILE ARG GLY GLY VAL LEU GLU GLN GLY MET
SEQRES 5 B 394 VAL ASP LEU LEU ARG GLU ALA GLY VAL ASP ARG ARG MET
SEQRES 6 B 394 ALA ARG ASP GLY LEU VAL HIS GLU GLY VAL GLU ILE ALA
SEQRES 7 B 394 PHE ALA GLY GLN ARG ARG ARG ILE ASP LEU LYS ARG LEU
SEQRES 8 B 394 SER GLY GLY LYS THR VAL THR VAL TYR GLY GLN THR GLU
SEQRES 9 B 394 VAL THR ARG ASP LEU MET GLU ALA ARG GLU ALA CYS GLY
SEQRES 10 B 394 ALA THR THR VAL TYR GLN ALA ALA GLU VAL ARG LEU HIS
SEQRES 11 B 394 ASP LEU GLN GLY GLU ARG PRO TYR VAL THR PHE GLU ARG
SEQRES 12 B 394 ASP GLY GLU ARG LEU ARG LEU ASP CYS ASP TYR ILE ALA
SEQRES 13 B 394 GLY CYS ASP GLY PHE HIS GLY ILE SER ARG GLN SER ILE
SEQRES 14 B 394 PRO ALA GLU ARG LEU LYS VAL PHE GLU ARG VAL TYR PRO
SEQRES 15 B 394 PHE GLY TRP LEU GLY LEU LEU ALA ASP THR PRO PRO VAL
SEQRES 16 B 394 SER HIS GLU LEU ILE TYR ALA ASN HIS PRO ARG GLY PHE
SEQRES 17 B 394 ALA LEU CYS SER GLN ARG SER ALA THR ARG SER ARG TYR
SEQRES 18 B 394 TYR VAL GLN VAL PRO LEU SER GLU LYS VAL GLU ASP TRP
SEQRES 19 B 394 SER ASP GLU ARG PHE TRP THR GLU LEU LYS ALA ARG LEU
SEQRES 20 B 394 PRO SER GLU VAL ALA GLU LYS LEU VAL THR GLY PRO SER
SEQRES 21 B 394 LEU GLU LYS SER ILE ALA PRO LEU ARG SER PHE VAL VAL
SEQRES 22 B 394 GLU PRO MET GLN HIS GLY ARG LEU PHE LEU ALA GLY ASP
SEQRES 23 B 394 ALA ALA HIS ILE VAL PRO PRO THR GLY ALA LYS GLY LEU
SEQRES 24 B 394 ASN LEU ALA ALA SER ASP VAL SER THR LEU TYR ARG LEU
SEQRES 25 B 394 LEU LEU LYS ALA TYR ARG GLU GLY ARG GLY GLU LEU LEU
SEQRES 26 B 394 GLU ARG TYR SER ALA ILE CYS LEU ARG ARG ILE TRP LYS
SEQRES 27 B 394 ALA GLU ARG PHE SER TRP TRP MET THR SER VAL LEU HIS
SEQRES 28 B 394 ARG PHE PRO ASP THR ASP ALA PHE SER GLN ARG ILE GLN
SEQRES 29 B 394 GLN THR GLU LEU GLU TYR TYR LEU GLY SER GLU ALA GLY
SEQRES 30 B 394 LEU ALA THR ILE ALA GLU ASN TYR VAL GLY LEU PRO TYR
SEQRES 31 B 394 GLU GLU ILE GLU
HET SO4 A 701 5
HET SO4 A 704 5
HET SO4 A 705 5
HET SO4 A 708 5
HET SO4 A 709 5
HET FAD A1395 53
HET PHB A1396 10
HET SO4 B 702 5
HET SO4 B 703 5
HET SO4 B 706 5
HET SO4 B 707 5
HET SO4 B 711 5
HET SO4 B 712 5
HET SO4 B 713 5
HET FAD B2395 53
HET PHB B2396 10
HET PSL B 714 9
HET PSL B 715 9
HETNAM SO4 SULFATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM PHB P-HYDROXYBENZOIC ACID
HETNAM PSL PYROSULFATE
FORMUL 3 SO4 12(O4 S 2-)
FORMUL 8 FAD 2(C27 H33 N9 O15 P2)
FORMUL 9 PHB 2(C7 H6 O3)
FORMUL 19 PSL 2(O7 S2 2-)
FORMUL 21 HOH *542(H2 O)
HELIX 1 1 GLY A 1011 ALA A 1024 1 14
HELIX 2 2 THR A 1035 LEU A 1040 1 6
HELIX 3 3 GLN A 1050 ALA A 1059 1 10
HELIX 4 4 ASP A 1062 GLY A 1069 1 8
HELIX 5 5 LEU A 1088 GLY A 1093 1 6
HELIX 6 6 GLY A 1101 GLY A 1117 1 17
HELIX 7 7 SER A 1165 ILE A 1169 5 5
HELIX 8 8 PRO A 1170 LEU A 1174 5 5
HELIX 9 9 LYS A 1230 TRP A 1234 5 5
HELIX 10 10 SER A 1235 LEU A 1247 1 13
HELIX 11 11 PRO A 1248 LEU A 1255 1 8
HELIX 12 12 GLY A 1285 ALA A 1287 5 3
HELIX 13 13 PRO A 1292 ALA A 1296 5 5
HELIX 14 14 LYS A 1297 ARG A 1318 1 22
HELIX 15 15 ARG A 1321 GLU A 1326 5 6
HELIX 16 16 ARG A 1327 HIS A 1351 1 25
HELIX 17 17 ASP A 1357 SER A 1374 1 18
HELIX 18 18 SER A 1374 VAL A 1386 1 13
HELIX 19 19 GLY B 2011 ALA B 2024 1 14
HELIX 20 20 THR B 2035 GLY B 2041 1 7
HELIX 21 21 GLU B 2049 ALA B 2059 1 11
HELIX 22 22 ASP B 2087 SER B 2092 1 6
HELIX 23 23 GLY B 2101 ALA B 2115 1 15
HELIX 24 24 SER B 2165 ILE B 2169 5 5
HELIX 25 25 PRO B 2170 LEU B 2174 5 5
HELIX 26 26 LYS B 2230 TRP B 2234 5 5
HELIX 27 27 SER B 2235 LEU B 2247 1 13
HELIX 28 28 PRO B 2248 LYS B 2254 1 7
HELIX 29 29 GLY B 2285 ALA B 2287 5 3
HELIX 30 30 PRO B 2292 ALA B 2296 5 5
HELIX 31 31 LYS B 2297 GLY B 2320 1 24
HELIX 32 32 ARG B 2321 GLU B 2326 5 6
HELIX 33 33 ARG B 2327 HIS B 2351 1 25
HELIX 34 34 ASP B 2357 LEU B 2372 1 16
HELIX 35 35 SER B 2374 VAL B 2386 1 13
SHEET 1 A 6 THR A1119 VAL A1121 0
SHEET 2 A 6 ASN A1028 LEU A1031 1 N ILE A1030 O VAL A1121
SHEET 3 A 6 VAL A1005 ILE A1008 1 N ILE A1007 O VAL A1029
SHEET 4 A 6 TYR A1154 GLY A1157 1 O ALA A1156 N ILE A1008
SHEET 5 A 6 LEU A1281 LEU A1283 1 O PHE A1282 N GLY A1157
SHEET 6 A 6 GLN A1277 HIS A1278 -1 N HIS A1278 O LEU A1281
SHEET 1 B 3 VAL A1047 GLU A1049 0
SHEET 2 B 3 VAL A1097 VAL A1099 -1 O THR A1098 N LEU A1048
SHEET 3 B 3 LEU A1070 HIS A1072 -1 N LEU A1070 O VAL A1099
SHEET 1 C 8 ARG A1083 ASP A1087 0
SHEET 2 C 8 GLY A1074 ALA A1078 -1 N ILE A1077 O ARG A1084
SHEET 3 C 8 ILE A1200 ALA A1202 1 O TYR A1201 N ALA A1078
SHEET 4 C 8 ALA A1209 GLN A1213 -1 O ALA A1209 N ALA A1202
SHEET 5 C 8 SER A1219 VAL A1225 -1 O ARG A1220 N SER A1212
SHEET 6 C 8 LYS A1175 ALA A1190 -1 N ALA A1190 O SER A1219
SHEET 7 C 8 SER A1260 GLU A1274 -1 O ALA A1266 N TRP A1185
SHEET 8 C 8 HIS A1289 ILE A1290 -1 O ILE A1290 N PHE A1271
SHEET 1 D 3 ALA A1125 HIS A1130 0
SHEET 2 D 3 TYR A1138 ARG A1143 -1 O GLU A1142 N ALA A1125
SHEET 3 D 3 GLU A1146 ASP A1151 -1 O LEU A1150 N VAL A1139
SHEET 1 E 6 THR B2119 VAL B2121 0
SHEET 2 E 6 ASN B2028 LEU B2031 1 N ILE B2030 O VAL B2121
SHEET 3 E 6 VAL B2005 ILE B2008 1 N ILE B2007 O VAL B2029
SHEET 4 E 6 TYR B2154 GLY B2157 1 O ALA B2156 N ALA B2006
SHEET 5 E 6 LEU B2281 LEU B2283 1 O PHE B2282 N GLY B2157
SHEET 6 E 6 GLN B2277 HIS B2278 -1 N HIS B2278 O LEU B2281
SHEET 1 F 3 VAL B2047 LEU B2048 0
SHEET 2 F 3 VAL B2097 VAL B2099 -1 O THR B2098 N LEU B2048
SHEET 3 F 3 VAL B2071 GLU B2073 -1 N VAL B2071 O VAL B2099
SHEET 1 G 8 GLN B2082 ILE B2086 0
SHEET 2 G 8 VAL B2075 PHE B2079 -1 N VAL B2075 O ILE B2086
SHEET 3 G 8 LEU B2199 ASN B2203 1 O TYR B2201 N ALA B2078
SHEET 4 G 8 ALA B2209 SER B2215 -1 O ALA B2209 N ALA B2202
SHEET 5 G 8 ARG B2218 VAL B2225 -1 O ARG B2218 N ARG B2214
SHEET 6 G 8 LYS B2175 ALA B2190 -1 N GLY B2184 O VAL B2225
SHEET 7 G 8 SER B2260 GLU B2274 -1 O LEU B2261 N LEU B2189
SHEET 8 G 8 HIS B2289 ILE B2290 -1 O ILE B2290 N PHE B2271
SHEET 1 H 3 ALA B2125 HIS B2130 0
SHEET 2 H 3 TYR B2138 ARG B2143 -1 O GLU B2142 N ALA B2125
SHEET 3 H 3 GLU B2146 ASP B2151 -1 O LEU B2148 N PHE B2141
CISPEP 1 GLU A 1274 PRO A 1275 0 -0.74
CISPEP 2 GLU B 2274 PRO B 2275 0 -0.90
SITE 1 AC1 6 VAL A1176 HOH A3059 HOH A3408 HOH A3555
SITE 2 AC1 6 ASP B2357 ALA B2358
SITE 1 AC2 9 ARG B2085 ASP B2087 LEU B2088 LYS B2089
SITE 2 AC2 9 ARG B2090 HOH B3322 HOH B3415 HOH B3417
SITE 3 AC2 9 HOH B3473
SITE 1 AC3 5 PRO B2248 SER B2249 HOH B3241 HOH B3507
SITE 2 AC3 5 HOH B3545
SITE 1 AC4 6 SER A1235 ASP A1236 LYS A1263 HOH A3106
SITE 2 AC4 6 HOH A3158 HOH A3359
SITE 1 AC5 6 VAL A1071 HIS A1072 GLU A1073 GLY A1074
SITE 2 AC5 6 ARG A1085 GLU A1198
SITE 1 AC6 5 ASP B2131 GLY B2134 GLU B2135 ARG B2136
SITE 2 AC6 5 SER B2228
SITE 1 AC7 9 ARG B2042 ILE B2043 ARG B2044 ARG B2220
SITE 2 AC7 9 GLU B2262 SER B2264 HOH B3079 HOH B3163
SITE 3 AC7 9 HOH B3297
SITE 1 AC8 2 TYR A1038 ARG A1042
SITE 1 AC9 8 ARG A1042 ILE A1043 ARG A1044 ARG A1220
SITE 2 AC9 8 GLU A1262 SER A1264 HOH A3296 HOH A3515
SITE 1 BC1 7 GLN B2277 HIS B2278 GLY B2279 HOH B3045
SITE 2 BC1 7 HOH B3111 HOH B3227 HOH B3350
SITE 1 BC2 5 SER B2235 ASP B2236 LYS B2263 HOH B3239
SITE 2 BC2 5 HOH B3395
SITE 1 BC3 5 GLN B2133 PRO B2170 ARG B2173 HIS B2278
SITE 2 BC3 5 HOH B3434
SITE 1 BC4 38 ILE A1008 GLY A1009 GLY A1011 PRO A1012
SITE 2 BC4 38 SER A1013 LEU A1031 GLU A1032 ARG A1033
SITE 3 BC4 38 GLN A1034 VAL A1039 ARG A1042 ARG A1044
SITE 4 BC4 38 GLY A1045 GLY A1046 VAL A1047 GLN A1102
SITE 5 BC4 38 VAL A1127 CYS A1158 ASP A1159 GLY A1160
SITE 6 BC4 38 GLY A1163 ILE A1164 GLY A1285 ASP A1286
SITE 7 BC4 38 PRO A1293 ALA A1296 LYS A1297 GLY A1298
SITE 8 BC4 38 LEU A1299 ASN A1300 PHB A1396 HOH A3008
SITE 9 BC4 38 HOH A3024 HOH A3035 HOH A3050 HOH A3293
SITE 10 BC4 38 HOH A3431 HOH A3467
SITE 1 BC5 37 ILE B2008 GLY B2009 GLY B2011 PRO B2012
SITE 2 BC5 37 SER B2013 GLU B2032 ARG B2033 GLN B2034
SITE 3 BC5 37 VAL B2039 ARG B2042 ARG B2044 GLY B2045
SITE 4 BC5 37 GLY B2046 VAL B2047 GLN B2102 CYS B2158
SITE 5 BC5 37 ASP B2159 GLY B2160 GLY B2163 ASP B2286
SITE 6 BC5 37 PRO B2293 ALA B2296 LYS B2297 GLY B2298
SITE 7 BC5 37 LEU B2299 ASN B2300 PHB B2396 HOH B3005
SITE 8 BC5 37 HOH B3007 HOH B3017 HOH B3019 HOH B3020
SITE 9 BC5 37 HOH B3023 HOH B3030 HOH B3033 HOH B3125
SITE 10 BC5 37 HOH B3440
SITE 1 BC6 15 ARG A1044 GLY A1045 GLY A1046 TRP A1185
SITE 2 BC6 15 LEU A1199 TYR A1201 LEU A1210 SER A1212
SITE 3 BC6 15 ARG A1214 ARG A1220 TYR A1222 PRO A1293
SITE 4 BC6 15 THR A1294 ALA A1296 FAD A1395
SITE 1 BC7 13 ARG B2044 GLY B2045 GLY B2046 TYR B2201
SITE 2 BC7 13 LEU B2210 SER B2212 ARG B2214 ARG B2220
SITE 3 BC7 13 TYR B2222 PRO B2293 THR B2294 ALA B2296
SITE 4 BC7 13 FAD B2395
SITE 1 BC8 7 ARG B2128 HIS B2162 PRO B2267 ARG B2269
SITE 2 BC8 7 HOH B3190 HOH B3424 HOH B3506
SITE 1 BC9 9 ARG B2033 GLN B2034 ALA B2125 GLU B2126
SITE 2 BC9 9 ARG B2128 HOH B3019 HOH B3436 HOH B3440
SITE 3 BC9 9 HOH B3471
CRYST1 69.860 85.897 146.074 90.00 90.00 90.00 P 21 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014314 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011642 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006846 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
