HEADER OXIDOREDUCTASE 16-JAN-07 2OK7
TITLE FERREDOXIN-NADP+ REDUCTASE FROM PLASMODIUM FALCIPARUM WITH 2'P-AMP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE FERREDOXIN--NADP REDUCTASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: FERREDOXIN--NADP REDUCTASE, PUTATIVE;
COMPND 5 EC: 1.18.1.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7;
SOURCE 3 ORGANISM_TAXID: 36329;
SOURCE 4 STRAIN: ISOLATE 3D7;
SOURCE 5 GENE: ORF PFF1115W;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS DISULFIDE-STABILIZED DIMER, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MILANI,E.MASTRANGELO,M.BOLOGNESI
REVDAT 4 30-AUG-23 2OK7 1 REMARK LINK
REVDAT 3 24-FEB-09 2OK7 1 VERSN
REVDAT 2 13-MAR-07 2OK7 1 JRNL
REVDAT 1 13-FEB-07 2OK7 0
JRNL AUTH M.MILANI,E.BALCONI,A.ALIVERTI,E.MASTRANGELO,F.SEEBER,
JRNL AUTH 2 M.BOLOGNESI,G.ZANETTI
JRNL TITL FERREDOXIN-NADP(+) REDUCTASE FROM PLASMODIUM FALCIPARUM
JRNL TITL 2 UNDERGOES NADP(+)-DEPENDENT DIMERIZATION AND INACTIVATION:
JRNL TITL 3 FUNCTIONAL AND CRYSTALLOGRAPHIC ANALYSIS.
JRNL REF J.MOL.BIOL. V. 367 501 2007
JRNL REFN ISSN 0022-2836
JRNL PMID 17258767
JRNL DOI 10.1016/J.JMB.2007.01.005
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 58273
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) : 0.263
REMARK 3 R VALUE (WORKING SET) : 0.260
REMARK 3 FREE R VALUE : 0.321
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3082
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4266
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.16
REMARK 3 BIN R VALUE (WORKING SET) : 0.3370
REMARK 3 BIN FREE R VALUE SET COUNT : 227
REMARK 3 BIN FREE R VALUE : 0.4050
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12949
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 481
REMARK 3 SOLVENT ATOMS : 228
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.44000
REMARK 3 B22 (A**2) : 1.44000
REMARK 3 B33 (A**2) : -2.16000
REMARK 3 B12 (A**2) : 0.72000
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): 1.392
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.429
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.879
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.817
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 13794 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 18729 ; 1.412 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1532 ; 5.933 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 677 ;38.177 ;24.446
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2279 ;17.435 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;21.843 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1967 ; 0.087 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 10323 ; 0.011 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 5657 ; 0.130 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 8977 ; 0.300 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 791 ; 0.143 ; 0.500
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): 87 ; 0.088 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 22 ; 0.191 ; 0.500
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): 7748 ; 5.013 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12526 ; 6.893 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6046 ;10.231 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6203 ;11.769 ; 6.000
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 : 1.40
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 2OK7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000041238.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-DEC-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 61398
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : 0.10200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.70
REMARK 200 R MERGE FOR SHELL (I) : 0.47600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: 1JB9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000 25%, BUFFER NA CACODYLATE, NA
REMARK 280 ACETATE 0.2 M, PH 6., MICROBATCH, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.60233
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 89.20467
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 6940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 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: 6470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: 3
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: 6520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23750 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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 LYS A 1
REMARK 465 GLU A 2
REMARK 465 GLU A 3
REMARK 465 ASN A 4
REMARK 465 GLU A 62
REMARK 465 LEU A 63
REMARK 465 ASP A 64
REMARK 465 ASN A 65
REMARK 465 ASN A 66
REMARK 465 PRO A 67
REMARK 465 ASN A 68
REMARK 465 ASN A 69
REMARK 465 GLN A 70
REMARK 465 ILE A 71
REMARK 465 ASN A 72
REMARK 465 LYS A 73
REMARK 465 ASP A 74
REMARK 465 HIS A 75
REMARK 465 ASN A 76
REMARK 465 ILE A 77
REMARK 465 ILE A 78
REMARK 465 ASN A 79
REMARK 465 THR A 80
REMARK 465 THR A 81
REMARK 465 ASN A 82
REMARK 465 HIS A 83
REMARK 465 THR A 84
REMARK 465 ASN A 85
REMARK 465 HIS A 86
REMARK 465 ASN A 87
REMARK 465 ASN A 88
REMARK 465 ILE A 89
REMARK 465 ALA A 90
REMARK 465 LEU A 91
REMARK 465 SER A 92
REMARK 465 HIS A 93
REMARK 465 ILE A 94
REMARK 465 THR A 126
REMARK 465 GLU A 127
REMARK 465 ASN A 128
REMARK 465 ALA A 129
REMARK 465 PRO A 130
REMARK 465 ASN A 131
REMARK 465 ILE A 132
REMARK 465 THR A 133
REMARK 465 ASN A 202
REMARK 465 ARG A 203
REMARK 465 SER A 299
REMARK 465 HIS A 300
REMARK 465 ASP A 301
REMARK 465 GLN A 302
REMARK 465 PHE A 303
REMARK 465 ASP A 304
REMARK 465 GLU A 305
REMARK 465 LYS B 1
REMARK 465 GLU B 2
REMARK 465 GLU B 3
REMARK 465 ASN B 4
REMARK 465 GLU B 62
REMARK 465 LEU B 63
REMARK 465 ASP B 64
REMARK 465 ASN B 65
REMARK 465 ASN B 66
REMARK 465 PRO B 67
REMARK 465 ASN B 68
REMARK 465 ASN B 69
REMARK 465 GLN B 70
REMARK 465 ILE B 71
REMARK 465 ASN B 72
REMARK 465 LYS B 73
REMARK 465 ASP B 74
REMARK 465 HIS B 75
REMARK 465 ASN B 76
REMARK 465 ILE B 77
REMARK 465 ILE B 78
REMARK 465 ASN B 79
REMARK 465 THR B 80
REMARK 465 THR B 81
REMARK 465 ASN B 82
REMARK 465 HIS B 83
REMARK 465 THR B 84
REMARK 465 ASN B 85
REMARK 465 HIS B 86
REMARK 465 ASN B 87
REMARK 465 ASN B 88
REMARK 465 ILE B 89
REMARK 465 ALA B 90
REMARK 465 LEU B 91
REMARK 465 SER B 92
REMARK 465 HIS B 93
REMARK 465 ILE B 94
REMARK 465 GLN B 125
REMARK 465 THR B 126
REMARK 465 GLU B 127
REMARK 465 ASN B 128
REMARK 465 ALA B 129
REMARK 465 PRO B 130
REMARK 465 ASN B 131
REMARK 465 ILE B 132
REMARK 465 ASN B 204
REMARK 465 SER B 205
REMARK 465 ASN B 206
REMARK 465 SER B 299
REMARK 465 HIS B 300
REMARK 465 ASP B 301
REMARK 465 GLN B 302
REMARK 465 PHE B 303
REMARK 465 ASP B 304
REMARK 465 GLU B 305
REMARK 465 LYS C 1
REMARK 465 GLU C 2
REMARK 465 GLU C 3
REMARK 465 GLU C 62
REMARK 465 LEU C 63
REMARK 465 ASP C 64
REMARK 465 ASN C 65
REMARK 465 ASN C 66
REMARK 465 PRO C 67
REMARK 465 ASN C 68
REMARK 465 ASN C 69
REMARK 465 GLN C 70
REMARK 465 ILE C 71
REMARK 465 ASN C 72
REMARK 465 LYS C 73
REMARK 465 ASP C 74
REMARK 465 HIS C 75
REMARK 465 ASN C 76
REMARK 465 ILE C 77
REMARK 465 ILE C 78
REMARK 465 ASN C 79
REMARK 465 THR C 80
REMARK 465 THR C 81
REMARK 465 ASN C 82
REMARK 465 HIS C 83
REMARK 465 THR C 84
REMARK 465 ASN C 85
REMARK 465 HIS C 86
REMARK 465 ASN C 87
REMARK 465 ASN C 88
REMARK 465 ILE C 89
REMARK 465 ALA C 90
REMARK 465 LEU C 91
REMARK 465 SER C 92
REMARK 465 HIS C 93
REMARK 465 ILE C 94
REMARK 465 LYS C 95
REMARK 465 LYS C 96
REMARK 465 THR C 126
REMARK 465 GLU C 127
REMARK 465 ASN C 128
REMARK 465 ALA C 129
REMARK 465 PRO C 130
REMARK 465 ASN C 131
REMARK 465 ILE C 132
REMARK 465 HIS C 300
REMARK 465 ASP C 301
REMARK 465 GLN C 302
REMARK 465 PHE C 303
REMARK 465 ASP C 304
REMARK 465 LYS D 1
REMARK 465 GLU D 2
REMARK 465 GLU D 3
REMARK 465 ASN D 4
REMARK 465 ASN D 65
REMARK 465 ASN D 66
REMARK 465 PRO D 67
REMARK 465 ASN D 68
REMARK 465 ASN D 69
REMARK 465 GLN D 70
REMARK 465 ILE D 71
REMARK 465 ASN D 72
REMARK 465 LYS D 73
REMARK 465 ASP D 74
REMARK 465 HIS D 75
REMARK 465 ASN D 76
REMARK 465 ILE D 77
REMARK 465 ILE D 78
REMARK 465 ASN D 79
REMARK 465 THR D 80
REMARK 465 THR D 81
REMARK 465 ASN D 82
REMARK 465 HIS D 83
REMARK 465 THR D 84
REMARK 465 ASN D 85
REMARK 465 HIS D 86
REMARK 465 ASN D 87
REMARK 465 ASN D 88
REMARK 465 ILE D 89
REMARK 465 ALA D 90
REMARK 465 LEU D 91
REMARK 465 SER D 92
REMARK 465 HIS D 93
REMARK 465 ILE D 94
REMARK 465 LYS D 95
REMARK 465 GLN D 125
REMARK 465 THR D 126
REMARK 465 GLU D 127
REMARK 465 ASN D 128
REMARK 465 ALA D 129
REMARK 465 PRO D 130
REMARK 465 ASN D 131
REMARK 465 ILE D 132
REMARK 465 GLN D 250
REMARK 465 ASN D 251
REMARK 465 SER D 252
REMARK 465 ASP D 253
REMARK 465 ALA D 254
REMARK 465 SER D 299
REMARK 465 HIS D 300
REMARK 465 ASP D 301
REMARK 465 GLN D 302
REMARK 465 PHE D 303
REMARK 465 ASP D 304
REMARK 465 LYS E 1
REMARK 465 GLU E 2
REMARK 465 GLU E 3
REMARK 465 ASN E 4
REMARK 465 GLU E 62
REMARK 465 LEU E 63
REMARK 465 ASP E 64
REMARK 465 ASN E 65
REMARK 465 ASN E 66
REMARK 465 PRO E 67
REMARK 465 ASN E 68
REMARK 465 ASN E 69
REMARK 465 GLN E 70
REMARK 465 ILE E 71
REMARK 465 ASN E 72
REMARK 465 LYS E 73
REMARK 465 ASP E 74
REMARK 465 HIS E 75
REMARK 465 ASN E 76
REMARK 465 ILE E 77
REMARK 465 ILE E 78
REMARK 465 ASN E 79
REMARK 465 THR E 80
REMARK 465 THR E 81
REMARK 465 ASN E 82
REMARK 465 HIS E 83
REMARK 465 THR E 84
REMARK 465 ASN E 85
REMARK 465 HIS E 86
REMARK 465 ASN E 87
REMARK 465 ASN E 88
REMARK 465 ILE E 89
REMARK 465 ALA E 90
REMARK 465 LEU E 91
REMARK 465 SER E 92
REMARK 465 HIS E 93
REMARK 465 ILE E 94
REMARK 465 LYS E 95
REMARK 465 LYS E 96
REMARK 465 GLN E 125
REMARK 465 THR E 126
REMARK 465 GLU E 127
REMARK 465 ASN E 128
REMARK 465 ALA E 129
REMARK 465 PRO E 130
REMARK 465 ASN E 131
REMARK 465 ILE E 132
REMARK 465 THR E 133
REMARK 465 LYS E 249
REMARK 465 GLN E 250
REMARK 465 ASN E 251
REMARK 465 SER E 252
REMARK 465 ASP E 253
REMARK 465 SER E 299
REMARK 465 HIS E 300
REMARK 465 ASP E 301
REMARK 465 GLN E 302
REMARK 465 PHE E 303
REMARK 465 ASP E 304
REMARK 465 GLU E 305
REMARK 465 LYS E 306
REMARK 465 LYS E 307
REMARK 465 LYS F 1
REMARK 465 GLU F 2
REMARK 465 GLU F 3
REMARK 465 ASN F 4
REMARK 465 ASN F 5
REMARK 465 LEU F 63
REMARK 465 ASP F 64
REMARK 465 ASN F 65
REMARK 465 ASN F 66
REMARK 465 PRO F 67
REMARK 465 ASN F 68
REMARK 465 ASN F 69
REMARK 465 GLN F 70
REMARK 465 ILE F 71
REMARK 465 ASN F 72
REMARK 465 LYS F 73
REMARK 465 ASP F 74
REMARK 465 HIS F 75
REMARK 465 ASN F 76
REMARK 465 ILE F 77
REMARK 465 ILE F 78
REMARK 465 ASN F 79
REMARK 465 THR F 80
REMARK 465 THR F 81
REMARK 465 ASN F 82
REMARK 465 HIS F 83
REMARK 465 THR F 84
REMARK 465 ASN F 85
REMARK 465 HIS F 86
REMARK 465 ASN F 87
REMARK 465 ASN F 88
REMARK 465 ILE F 89
REMARK 465 ALA F 90
REMARK 465 LEU F 91
REMARK 465 SER F 92
REMARK 465 HIS F 93
REMARK 465 ILE F 94
REMARK 465 LYS F 95
REMARK 465 LYS F 96
REMARK 465 GLN F 125
REMARK 465 THR F 126
REMARK 465 GLU F 127
REMARK 465 ASN F 128
REMARK 465 ALA F 129
REMARK 465 PRO F 130
REMARK 465 ASN F 131
REMARK 465 ILE F 132
REMARK 465 THR F 133
REMARK 465 ASN F 206
REMARK 465 GLN F 250
REMARK 465 ASN F 251
REMARK 465 SER F 252
REMARK 465 ASP F 253
REMARK 465 SER F 299
REMARK 465 HIS F 300
REMARK 465 ASP F 301
REMARK 465 GLN F 302
REMARK 465 PHE F 303
REMARK 465 ASP F 304
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 A 98 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 306 CG CD CE NZ
REMARK 470 LYS B 96 CG CD CE NZ
REMARK 470 ARG B 98 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 112 CG CD OE1 OE2
REMARK 470 LYS B 306 CG CD CE NZ
REMARK 470 GLN C 97 CG CD OE1 NE2
REMARK 470 ARG C 98 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 250 CG CD OE1 NE2
REMARK 470 ASN C 251 CG OD1 ND2
REMARK 470 SER C 252 OG
REMARK 470 ASP C 253 CG OD1 OD2
REMARK 470 THR C 255 CG2
REMARK 470 SER C 299 OG
REMARK 470 GLU C 305 CG CD OE1 OE2
REMARK 470 LYS D 96 CG CD CE NZ
REMARK 470 GLN D 97 CG CD OE1 NE2
REMARK 470 ARG D 98 CG CD NE CZ NH1 NH2
REMARK 470 ILE D 167 CG1 CG2 CD1
REMARK 470 LYS D 249 CG CD CE NZ
REMARK 470 LYS D 278 CB CG CD CE NZ
REMARK 470 GLU D 305 CG CD OE1 OE2
REMARK 470 GLN E 97 CG CD OE1 NE2
REMARK 470 ARG E 98 CG CD NE CZ NH1 NH2
REMARK 470 LYS E 298 CG CD CE NZ
REMARK 470 LYS E 308 CG CD CE NZ
REMARK 470 ASN F 61 CG OD1 ND2
REMARK 470 GLU F 62 CG CD OE1 OE2
REMARK 470 GLN F 97 CG CD OE1 NE2
REMARK 470 ARG F 98 CG CD NE CZ NH1 NH2
REMARK 470 GLU F 112 CG CD OE1 OE2
REMARK 470 ILE F 167 CG1 CG2 CD1
REMARK 470 GLN F 168 CG CD OE1 NE2
REMARK 470 LYS F 278 CB CG CD CE NZ
REMARK 470 GLU F 305 CG CD OE1 OE2
REMARK 470 LYS F 306 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 LEU B 9 CG LEU B 9 CD1 -0.281
REMARK 500 LEU D 9 CG LEU D 9 CD2 -0.280
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 LEU B 9 CB - CG - CD1 ANGL. DEV. = 10.8 DEGREES
REMARK 500 LEU D 9 CB - CG - CD2 ANGL. DEV. = 10.6 DEGREES
REMARK 500 TYR D 60 CB - CG - CD2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 LYS F 306 C - N - CA ANGL. DEV. = -16.9 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 A 98 75.06 -104.34
REMARK 500 ASN A 199 50.63 -142.66
REMARK 500 GLN A 250 19.82 58.72
REMARK 500 ASN A 251 106.57 -178.56
REMARK 500 ARG A 266 45.88 -107.02
REMARK 500 THR B 11 -167.25 -118.14
REMARK 500 GLN B 97 72.93 -154.46
REMARK 500 GLN B 250 -76.23 -109.11
REMARK 500 ALA B 254 -162.19 -63.85
REMARK 500 THR B 255 -167.10 -66.95
REMARK 500 TYR B 258 -166.22 -110.91
REMARK 500 PRO C 29 -34.24 -31.87
REMARK 500 GLU C 124 -87.49 -71.59
REMARK 500 ALA C 156 123.01 174.75
REMARK 500 ASN C 199 46.23 -143.08
REMARK 500 ASP C 253 86.16 -69.87
REMARK 500 ARG C 266 44.90 -104.84
REMARK 500 TYR D 59 104.04 55.96
REMARK 500 TYR D 60 56.93 -160.00
REMARK 500 ASN D 61 22.07 -149.87
REMARK 500 ARG D 98 -90.55 -73.96
REMARK 500 CYS D 99 68.97 61.77
REMARK 500 TYR D 258 -168.78 -105.87
REMARK 500 LYS D 306 41.77 -103.02
REMARK 500 ASN E 43 14.46 58.35
REMARK 500 ALA E 156 120.86 -173.79
REMARK 500 PHE E 160 56.85 -92.21
REMARK 500 ALA E 194 70.93 46.14
REMARK 500 ARG E 203 -86.42 -81.24
REMARK 500 TYR E 236 59.80 -141.56
REMARK 500 SER E 256 115.51 -36.39
REMARK 500 ARG E 266 60.12 -114.55
REMARK 500 PRO F 29 -51.99 -21.87
REMARK 500 ASN F 43 19.70 58.84
REMARK 500 ALA F 156 74.34 -169.18
REMARK 500 ALA F 166 -80.23 -78.80
REMARK 500 ARG F 203 -76.25 -66.09
REMARK 500 THR F 255 -84.32 -73.04
REMARK 500 SER F 256 -59.46 -127.00
REMARK 500 PHE F 257 71.88 59.79
REMARK 500 LYS F 278 50.95 74.39
REMARK 500 LEU F 297 10.96 -153.65
REMARK 500 LYS F 306 117.32 178.30
REMARK 500 LYS F 308 26.15 -53.89
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 NA A9001 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A2P A 416 O4P
REMARK 620 2 HOH A9028 O 69.6
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 9001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A2P A 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A2P B 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A2P C 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A2P D 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD E 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A2P E 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD F 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A2P F 416
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2OK8 RELATED DB: PDB
DBREF 2OK7 A 1 316 UNP Q6LF82 Q6LF82_PLAF7 56 371
DBREF 2OK7 B 1 316 UNP Q6LF82 Q6LF82_PLAF7 56 371
DBREF 2OK7 C 1 316 UNP Q6LF82 Q6LF82_PLAF7 56 371
DBREF 2OK7 D 1 316 UNP Q6LF82 Q6LF82_PLAF7 56 371
DBREF 2OK7 E 1 316 UNP Q6LF82 Q6LF82_PLAF7 56 371
DBREF 2OK7 F 1 316 UNP Q6LF82 Q6LF82_PLAF7 56 371
SEQRES 1 A 316 LYS GLU GLU ASN ASN PHE ILE ASN LEU TYR THR VAL LYS
SEQRES 2 A 316 ASN PRO LEU LYS CYS LYS ILE VAL ASP LYS ILE ASN LEU
SEQRES 3 A 316 VAL ARG PRO ASN SER PRO ASN GLU VAL TYR HIS LEU GLU
SEQRES 4 A 316 ILE ASN HIS ASN GLY LEU PHE LYS TYR LEU GLU GLY HIS
SEQRES 5 A 316 THR CYS GLY ILE ILE PRO TYR TYR ASN GLU LEU ASP ASN
SEQRES 6 A 316 ASN PRO ASN ASN GLN ILE ASN LYS ASP HIS ASN ILE ILE
SEQRES 7 A 316 ASN THR THR ASN HIS THR ASN HIS ASN ASN ILE ALA LEU
SEQRES 8 A 316 SER HIS ILE LYS LYS GLN ARG CYS ALA ARG LEU TYR SER
SEQRES 9 A 316 ILE SER SER SER ASN ASN MET GLU ASN LEU SER VAL ALA
SEQRES 10 A 316 ILE LYS ILE HIS LYS TYR GLU GLN THR GLU ASN ALA PRO
SEQRES 11 A 316 ASN ILE THR ASN TYR GLY TYR CYS SER GLY PHE ILE LYS
SEQRES 12 A 316 ASN LEU LYS ILE ASN ASP ASP ILE TYR LEU THR GLY ALA
SEQRES 13 A 316 HIS GLY TYR PHE ASN LEU PRO ASN ASP ALA ILE GLN LYS
SEQRES 14 A 316 ASN THR ASN PHE ILE PHE ILE ALA THR GLY THR GLY ILE
SEQRES 15 A 316 SER PRO TYR ILE SER PHE LEU LYS LYS LEU PHE ALA TYR
SEQRES 16 A 316 ASP LYS ASN ASN LEU TYR ASN ARG ASN SER ASN TYR THR
SEQRES 17 A 316 GLY TYR ILE THR ILE TYR TYR GLY VAL TYR ASN GLU ASP
SEQRES 18 A 316 SER ILE LEU TYR LEU ASN GLU LEU GLU TYR PHE GLN LYS
SEQRES 19 A 316 MET TYR PRO ASN ASN ILE ASN ILE HIS TYR VAL PHE SER
SEQRES 20 A 316 TYR LYS GLN ASN SER ASP ALA THR SER PHE TYR VAL GLN
SEQRES 21 A 316 ASP GLU ILE TYR LYS ARG LYS THR GLU PHE LEU ASN LEU
SEQRES 22 A 316 PHE ASN ASN TYR LYS CYS GLU LEU TYR ILE CYS GLY HIS
SEQRES 23 A 316 LYS SER ILE ARG TYR LYS VAL MET ASP ILE LEU LYS SER
SEQRES 24 A 316 HIS ASP GLN PHE ASP GLU LYS LYS LYS LYS ARG VAL HIS
SEQRES 25 A 316 VAL GLU VAL TYR
SEQRES 1 B 316 LYS GLU GLU ASN ASN PHE ILE ASN LEU TYR THR VAL LYS
SEQRES 2 B 316 ASN PRO LEU LYS CYS LYS ILE VAL ASP LYS ILE ASN LEU
SEQRES 3 B 316 VAL ARG PRO ASN SER PRO ASN GLU VAL TYR HIS LEU GLU
SEQRES 4 B 316 ILE ASN HIS ASN GLY LEU PHE LYS TYR LEU GLU GLY HIS
SEQRES 5 B 316 THR CYS GLY ILE ILE PRO TYR TYR ASN GLU LEU ASP ASN
SEQRES 6 B 316 ASN PRO ASN ASN GLN ILE ASN LYS ASP HIS ASN ILE ILE
SEQRES 7 B 316 ASN THR THR ASN HIS THR ASN HIS ASN ASN ILE ALA LEU
SEQRES 8 B 316 SER HIS ILE LYS LYS GLN ARG CYS ALA ARG LEU TYR SER
SEQRES 9 B 316 ILE SER SER SER ASN ASN MET GLU ASN LEU SER VAL ALA
SEQRES 10 B 316 ILE LYS ILE HIS LYS TYR GLU GLN THR GLU ASN ALA PRO
SEQRES 11 B 316 ASN ILE THR ASN TYR GLY TYR CYS SER GLY PHE ILE LYS
SEQRES 12 B 316 ASN LEU LYS ILE ASN ASP ASP ILE TYR LEU THR GLY ALA
SEQRES 13 B 316 HIS GLY TYR PHE ASN LEU PRO ASN ASP ALA ILE GLN LYS
SEQRES 14 B 316 ASN THR ASN PHE ILE PHE ILE ALA THR GLY THR GLY ILE
SEQRES 15 B 316 SER PRO TYR ILE SER PHE LEU LYS LYS LEU PHE ALA TYR
SEQRES 16 B 316 ASP LYS ASN ASN LEU TYR ASN ARG ASN SER ASN TYR THR
SEQRES 17 B 316 GLY TYR ILE THR ILE TYR TYR GLY VAL TYR ASN GLU ASP
SEQRES 18 B 316 SER ILE LEU TYR LEU ASN GLU LEU GLU TYR PHE GLN LYS
SEQRES 19 B 316 MET TYR PRO ASN ASN ILE ASN ILE HIS TYR VAL PHE SER
SEQRES 20 B 316 TYR LYS GLN ASN SER ASP ALA THR SER PHE TYR VAL GLN
SEQRES 21 B 316 ASP GLU ILE TYR LYS ARG LYS THR GLU PHE LEU ASN LEU
SEQRES 22 B 316 PHE ASN ASN TYR LYS CYS GLU LEU TYR ILE CYS GLY HIS
SEQRES 23 B 316 LYS SER ILE ARG TYR LYS VAL MET ASP ILE LEU LYS SER
SEQRES 24 B 316 HIS ASP GLN PHE ASP GLU LYS LYS LYS LYS ARG VAL HIS
SEQRES 25 B 316 VAL GLU VAL TYR
SEQRES 1 C 316 LYS GLU GLU ASN ASN PHE ILE ASN LEU TYR THR VAL LYS
SEQRES 2 C 316 ASN PRO LEU LYS CYS LYS ILE VAL ASP LYS ILE ASN LEU
SEQRES 3 C 316 VAL ARG PRO ASN SER PRO ASN GLU VAL TYR HIS LEU GLU
SEQRES 4 C 316 ILE ASN HIS ASN GLY LEU PHE LYS TYR LEU GLU GLY HIS
SEQRES 5 C 316 THR CYS GLY ILE ILE PRO TYR TYR ASN GLU LEU ASP ASN
SEQRES 6 C 316 ASN PRO ASN ASN GLN ILE ASN LYS ASP HIS ASN ILE ILE
SEQRES 7 C 316 ASN THR THR ASN HIS THR ASN HIS ASN ASN ILE ALA LEU
SEQRES 8 C 316 SER HIS ILE LYS LYS GLN ARG CYS ALA ARG LEU TYR SER
SEQRES 9 C 316 ILE SER SER SER ASN ASN MET GLU ASN LEU SER VAL ALA
SEQRES 10 C 316 ILE LYS ILE HIS LYS TYR GLU GLN THR GLU ASN ALA PRO
SEQRES 11 C 316 ASN ILE THR ASN TYR GLY TYR CYS SER GLY PHE ILE LYS
SEQRES 12 C 316 ASN LEU LYS ILE ASN ASP ASP ILE TYR LEU THR GLY ALA
SEQRES 13 C 316 HIS GLY TYR PHE ASN LEU PRO ASN ASP ALA ILE GLN LYS
SEQRES 14 C 316 ASN THR ASN PHE ILE PHE ILE ALA THR GLY THR GLY ILE
SEQRES 15 C 316 SER PRO TYR ILE SER PHE LEU LYS LYS LEU PHE ALA TYR
SEQRES 16 C 316 ASP LYS ASN ASN LEU TYR ASN ARG ASN SER ASN TYR THR
SEQRES 17 C 316 GLY TYR ILE THR ILE TYR TYR GLY VAL TYR ASN GLU ASP
SEQRES 18 C 316 SER ILE LEU TYR LEU ASN GLU LEU GLU TYR PHE GLN LYS
SEQRES 19 C 316 MET TYR PRO ASN ASN ILE ASN ILE HIS TYR VAL PHE SER
SEQRES 20 C 316 TYR LYS GLN ASN SER ASP ALA THR SER PHE TYR VAL GLN
SEQRES 21 C 316 ASP GLU ILE TYR LYS ARG LYS THR GLU PHE LEU ASN LEU
SEQRES 22 C 316 PHE ASN ASN TYR LYS CYS GLU LEU TYR ILE CYS GLY HIS
SEQRES 23 C 316 LYS SER ILE ARG TYR LYS VAL MET ASP ILE LEU LYS SER
SEQRES 24 C 316 HIS ASP GLN PHE ASP GLU LYS LYS LYS LYS ARG VAL HIS
SEQRES 25 C 316 VAL GLU VAL TYR
SEQRES 1 D 316 LYS GLU GLU ASN ASN PHE ILE ASN LEU TYR THR VAL LYS
SEQRES 2 D 316 ASN PRO LEU LYS CYS LYS ILE VAL ASP LYS ILE ASN LEU
SEQRES 3 D 316 VAL ARG PRO ASN SER PRO ASN GLU VAL TYR HIS LEU GLU
SEQRES 4 D 316 ILE ASN HIS ASN GLY LEU PHE LYS TYR LEU GLU GLY HIS
SEQRES 5 D 316 THR CYS GLY ILE ILE PRO TYR TYR ASN GLU LEU ASP ASN
SEQRES 6 D 316 ASN PRO ASN ASN GLN ILE ASN LYS ASP HIS ASN ILE ILE
SEQRES 7 D 316 ASN THR THR ASN HIS THR ASN HIS ASN ASN ILE ALA LEU
SEQRES 8 D 316 SER HIS ILE LYS LYS GLN ARG CYS ALA ARG LEU TYR SER
SEQRES 9 D 316 ILE SER SER SER ASN ASN MET GLU ASN LEU SER VAL ALA
SEQRES 10 D 316 ILE LYS ILE HIS LYS TYR GLU GLN THR GLU ASN ALA PRO
SEQRES 11 D 316 ASN ILE THR ASN TYR GLY TYR CYS SER GLY PHE ILE LYS
SEQRES 12 D 316 ASN LEU LYS ILE ASN ASP ASP ILE TYR LEU THR GLY ALA
SEQRES 13 D 316 HIS GLY TYR PHE ASN LEU PRO ASN ASP ALA ILE GLN LYS
SEQRES 14 D 316 ASN THR ASN PHE ILE PHE ILE ALA THR GLY THR GLY ILE
SEQRES 15 D 316 SER PRO TYR ILE SER PHE LEU LYS LYS LEU PHE ALA TYR
SEQRES 16 D 316 ASP LYS ASN ASN LEU TYR ASN ARG ASN SER ASN TYR THR
SEQRES 17 D 316 GLY TYR ILE THR ILE TYR TYR GLY VAL TYR ASN GLU ASP
SEQRES 18 D 316 SER ILE LEU TYR LEU ASN GLU LEU GLU TYR PHE GLN LYS
SEQRES 19 D 316 MET TYR PRO ASN ASN ILE ASN ILE HIS TYR VAL PHE SER
SEQRES 20 D 316 TYR LYS GLN ASN SER ASP ALA THR SER PHE TYR VAL GLN
SEQRES 21 D 316 ASP GLU ILE TYR LYS ARG LYS THR GLU PHE LEU ASN LEU
SEQRES 22 D 316 PHE ASN ASN TYR LYS CYS GLU LEU TYR ILE CYS GLY HIS
SEQRES 23 D 316 LYS SER ILE ARG TYR LYS VAL MET ASP ILE LEU LYS SER
SEQRES 24 D 316 HIS ASP GLN PHE ASP GLU LYS LYS LYS LYS ARG VAL HIS
SEQRES 25 D 316 VAL GLU VAL TYR
SEQRES 1 E 316 LYS GLU GLU ASN ASN PHE ILE ASN LEU TYR THR VAL LYS
SEQRES 2 E 316 ASN PRO LEU LYS CYS LYS ILE VAL ASP LYS ILE ASN LEU
SEQRES 3 E 316 VAL ARG PRO ASN SER PRO ASN GLU VAL TYR HIS LEU GLU
SEQRES 4 E 316 ILE ASN HIS ASN GLY LEU PHE LYS TYR LEU GLU GLY HIS
SEQRES 5 E 316 THR CYS GLY ILE ILE PRO TYR TYR ASN GLU LEU ASP ASN
SEQRES 6 E 316 ASN PRO ASN ASN GLN ILE ASN LYS ASP HIS ASN ILE ILE
SEQRES 7 E 316 ASN THR THR ASN HIS THR ASN HIS ASN ASN ILE ALA LEU
SEQRES 8 E 316 SER HIS ILE LYS LYS GLN ARG CYS ALA ARG LEU TYR SER
SEQRES 9 E 316 ILE SER SER SER ASN ASN MET GLU ASN LEU SER VAL ALA
SEQRES 10 E 316 ILE LYS ILE HIS LYS TYR GLU GLN THR GLU ASN ALA PRO
SEQRES 11 E 316 ASN ILE THR ASN TYR GLY TYR CYS SER GLY PHE ILE LYS
SEQRES 12 E 316 ASN LEU LYS ILE ASN ASP ASP ILE TYR LEU THR GLY ALA
SEQRES 13 E 316 HIS GLY TYR PHE ASN LEU PRO ASN ASP ALA ILE GLN LYS
SEQRES 14 E 316 ASN THR ASN PHE ILE PHE ILE ALA THR GLY THR GLY ILE
SEQRES 15 E 316 SER PRO TYR ILE SER PHE LEU LYS LYS LEU PHE ALA TYR
SEQRES 16 E 316 ASP LYS ASN ASN LEU TYR ASN ARG ASN SER ASN TYR THR
SEQRES 17 E 316 GLY TYR ILE THR ILE TYR TYR GLY VAL TYR ASN GLU ASP
SEQRES 18 E 316 SER ILE LEU TYR LEU ASN GLU LEU GLU TYR PHE GLN LYS
SEQRES 19 E 316 MET TYR PRO ASN ASN ILE ASN ILE HIS TYR VAL PHE SER
SEQRES 20 E 316 TYR LYS GLN ASN SER ASP ALA THR SER PHE TYR VAL GLN
SEQRES 21 E 316 ASP GLU ILE TYR LYS ARG LYS THR GLU PHE LEU ASN LEU
SEQRES 22 E 316 PHE ASN ASN TYR LYS CYS GLU LEU TYR ILE CYS GLY HIS
SEQRES 23 E 316 LYS SER ILE ARG TYR LYS VAL MET ASP ILE LEU LYS SER
SEQRES 24 E 316 HIS ASP GLN PHE ASP GLU LYS LYS LYS LYS ARG VAL HIS
SEQRES 25 E 316 VAL GLU VAL TYR
SEQRES 1 F 316 LYS GLU GLU ASN ASN PHE ILE ASN LEU TYR THR VAL LYS
SEQRES 2 F 316 ASN PRO LEU LYS CYS LYS ILE VAL ASP LYS ILE ASN LEU
SEQRES 3 F 316 VAL ARG PRO ASN SER PRO ASN GLU VAL TYR HIS LEU GLU
SEQRES 4 F 316 ILE ASN HIS ASN GLY LEU PHE LYS TYR LEU GLU GLY HIS
SEQRES 5 F 316 THR CYS GLY ILE ILE PRO TYR TYR ASN GLU LEU ASP ASN
SEQRES 6 F 316 ASN PRO ASN ASN GLN ILE ASN LYS ASP HIS ASN ILE ILE
SEQRES 7 F 316 ASN THR THR ASN HIS THR ASN HIS ASN ASN ILE ALA LEU
SEQRES 8 F 316 SER HIS ILE LYS LYS GLN ARG CYS ALA ARG LEU TYR SER
SEQRES 9 F 316 ILE SER SER SER ASN ASN MET GLU ASN LEU SER VAL ALA
SEQRES 10 F 316 ILE LYS ILE HIS LYS TYR GLU GLN THR GLU ASN ALA PRO
SEQRES 11 F 316 ASN ILE THR ASN TYR GLY TYR CYS SER GLY PHE ILE LYS
SEQRES 12 F 316 ASN LEU LYS ILE ASN ASP ASP ILE TYR LEU THR GLY ALA
SEQRES 13 F 316 HIS GLY TYR PHE ASN LEU PRO ASN ASP ALA ILE GLN LYS
SEQRES 14 F 316 ASN THR ASN PHE ILE PHE ILE ALA THR GLY THR GLY ILE
SEQRES 15 F 316 SER PRO TYR ILE SER PHE LEU LYS LYS LEU PHE ALA TYR
SEQRES 16 F 316 ASP LYS ASN ASN LEU TYR ASN ARG ASN SER ASN TYR THR
SEQRES 17 F 316 GLY TYR ILE THR ILE TYR TYR GLY VAL TYR ASN GLU ASP
SEQRES 18 F 316 SER ILE LEU TYR LEU ASN GLU LEU GLU TYR PHE GLN LYS
SEQRES 19 F 316 MET TYR PRO ASN ASN ILE ASN ILE HIS TYR VAL PHE SER
SEQRES 20 F 316 TYR LYS GLN ASN SER ASP ALA THR SER PHE TYR VAL GLN
SEQRES 21 F 316 ASP GLU ILE TYR LYS ARG LYS THR GLU PHE LEU ASN LEU
SEQRES 22 F 316 PHE ASN ASN TYR LYS CYS GLU LEU TYR ILE CYS GLY HIS
SEQRES 23 F 316 LYS SER ILE ARG TYR LYS VAL MET ASP ILE LEU LYS SER
SEQRES 24 F 316 HIS ASP GLN PHE ASP GLU LYS LYS LYS LYS ARG VAL HIS
SEQRES 25 F 316 VAL GLU VAL TYR
HET NA A9001 1
HET FAD A 415 53
HET A2P A 416 27
HET FAD B 415 53
HET A2P B 416 27
HET FAD C 415 53
HET A2P C 416 27
HET FAD D 415 53
HET A2P D 416 27
HET FAD E 415 53
HET A2P E 416 27
HET FAD F 415 53
HET A2P F 416 27
HETNAM NA SODIUM ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM A2P ADENOSINE-2'-5'-DIPHOSPHATE
FORMUL 7 NA NA 1+
FORMUL 8 FAD 6(C27 H33 N9 O15 P2)
FORMUL 9 A2P 6(C10 H15 N5 O10 P2)
FORMUL 20 HOH *228(H2 O)
HELIX 1 1 GLY A 136 ASN A 144 1 9
HELIX 2 2 ASP A 165 ASN A 170 1 6
HELIX 3 3 ILE A 182 PHE A 193 1 12
HELIX 4 4 ASP A 196 LEU A 200 5 5
HELIX 5 5 ASN A 219 ILE A 223 5 5
HELIX 6 6 TYR A 225 TYR A 236 1 12
HELIX 7 7 TYR A 258 ARG A 266 1 9
HELIX 8 8 ARG A 266 TYR A 277 1 12
HELIX 9 9 SER A 288 LYS A 298 1 11
HELIX 10 10 LYS A 307 LYS A 309 5 3
HELIX 11 11 GLY B 136 ASN B 144 1 9
HELIX 12 12 ASP B 165 ASN B 170 1 6
HELIX 13 13 ILE B 182 PHE B 193 1 12
HELIX 14 14 ASN B 219 ILE B 223 5 5
HELIX 15 15 TYR B 225 TYR B 236 1 12
HELIX 16 16 TYR B 258 ARG B 266 1 9
HELIX 17 17 ARG B 266 TYR B 277 1 12
HELIX 18 18 SER B 288 LYS B 298 1 11
HELIX 19 19 LYS B 307 LYS B 309 5 3
HELIX 20 20 GLY C 136 ASN C 144 1 9
HELIX 21 21 ASP C 165 ASN C 170 1 6
HELIX 22 22 ILE C 182 PHE C 193 1 12
HELIX 23 23 ASN C 219 ILE C 223 5 5
HELIX 24 24 TYR C 225 TYR C 236 1 12
HELIX 25 25 TYR C 258 ARG C 266 1 9
HELIX 26 26 ARG C 266 TYR C 277 1 12
HELIX 27 27 SER C 288 SER C 299 1 12
HELIX 28 28 LYS C 307 LYS C 309 5 3
HELIX 29 29 GLY D 136 ASN D 144 1 9
HELIX 30 30 ILE D 182 PHE D 193 1 12
HELIX 31 31 ASN D 219 ILE D 223 5 5
HELIX 32 32 TYR D 225 TYR D 236 1 12
HELIX 33 33 TYR D 258 ARG D 266 1 9
HELIX 34 34 ARG D 266 TYR D 277 1 12
HELIX 35 35 HIS D 286 LYS D 298 1 13
HELIX 36 36 LYS D 307 LYS D 309 5 3
HELIX 37 37 GLY E 136 ASN E 144 1 9
HELIX 38 38 ASP E 165 ASN E 170 1 6
HELIX 39 39 ILE E 182 PHE E 193 1 12
HELIX 40 40 TYR E 225 TYR E 236 1 12
HELIX 41 41 TYR E 258 ARG E 266 1 9
HELIX 42 42 ARG E 266 TYR E 277 1 12
HELIX 43 43 LYS E 287 LYS E 298 1 12
HELIX 44 44 GLY F 136 LEU F 145 1 10
HELIX 45 45 ILE F 182 PHE F 193 1 12
HELIX 46 46 ASN F 219 ILE F 223 5 5
HELIX 47 47 TYR F 225 TYR F 236 1 12
HELIX 48 48 TYR F 258 ARG F 266 1 9
HELIX 49 49 ARG F 266 ASN F 276 1 11
HELIX 50 50 SER F 288 ILE F 296 1 9
HELIX 51 51 LYS F 307 LYS F 309 5 3
SHEET 1 A 6 ARG A 101 SER A 104 0
SHEET 2 A 6 THR A 53 ILE A 57 -1 N CYS A 54 O TYR A 103
SHEET 3 A 6 ASP A 150 LEU A 153 -1 O TYR A 152 N ILE A 57
SHEET 4 A 6 LEU A 16 ASN A 25 -1 N LEU A 16 O LEU A 153
SHEET 5 A 6 VAL A 35 ASN A 41 -1 O HIS A 37 N ILE A 24
SHEET 6 A 6 LEU A 114 LYS A 119 -1 O LEU A 114 N ILE A 40
SHEET 1 B 5 ILE A 240 PHE A 246 0
SHEET 2 B 5 ILE A 211 VAL A 217 1 N ILE A 213 O HIS A 243
SHEET 3 B 5 PHE A 173 THR A 178 1 N PHE A 173 O THR A 212
SHEET 4 B 5 GLU A 280 GLY A 285 1 O TYR A 282 N ILE A 176
SHEET 5 B 5 VAL A 311 VAL A 315 1 O HIS A 312 N ILE A 283
SHEET 1 C 6 ARG B 101 SER B 104 0
SHEET 2 C 6 THR B 53 ILE B 56 -1 N CYS B 54 O TYR B 103
SHEET 3 C 6 ASP B 150 HIS B 157 -1 O HIS B 157 N THR B 53
SHEET 4 C 6 LEU B 16 ASN B 25 -1 N CYS B 18 O ILE B 151
SHEET 5 C 6 VAL B 35 ASN B 41 -1 O HIS B 37 N ILE B 24
SHEET 6 C 6 LEU B 114 LYS B 119 -1 O ILE B 118 N TYR B 36
SHEET 1 D 2 LYS B 122 TYR B 123 0
SHEET 2 D 2 ASN B 134 TYR B 135 -1 O ASN B 134 N TYR B 123
SHEET 1 E 5 ILE B 240 PHE B 246 0
SHEET 2 E 5 ILE B 211 VAL B 217 1 N ILE B 213 O HIS B 243
SHEET 3 E 5 PHE B 173 THR B 178 1 N ALA B 177 O TYR B 214
SHEET 4 E 5 GLU B 280 GLY B 285 1 O CYS B 284 N ILE B 176
SHEET 5 E 5 VAL B 311 VAL B 315 1 O GLU B 314 N ILE B 283
SHEET 1 F 6 ARG C 101 SER C 104 0
SHEET 2 F 6 THR C 53 ILE C 57 -1 N CYS C 54 O TYR C 103
SHEET 3 F 6 ASP C 150 HIS C 157 -1 O HIS C 157 N THR C 53
SHEET 4 F 6 LEU C 16 ASN C 25 -1 N CYS C 18 O ILE C 151
SHEET 5 F 6 VAL C 35 ASN C 41 -1 O HIS C 37 N ILE C 24
SHEET 6 F 6 LEU C 114 LYS C 119 -1 O LEU C 114 N ILE C 40
SHEET 1 G 2 LYS C 122 TYR C 123 0
SHEET 2 G 2 ASN C 134 TYR C 135 -1 O ASN C 134 N TYR C 123
SHEET 1 H 5 ILE C 240 PHE C 246 0
SHEET 2 H 5 ILE C 211 VAL C 217 1 N ILE C 213 O HIS C 243
SHEET 3 H 5 PHE C 173 THR C 178 1 N PHE C 173 O THR C 212
SHEET 4 H 5 GLU C 280 GLY C 285 1 O TYR C 282 N ILE C 176
SHEET 5 H 5 VAL C 311 VAL C 315 1 O GLU C 314 N ILE C 283
SHEET 1 I 6 ARG D 101 SER D 104 0
SHEET 2 I 6 THR D 53 ILE D 57 -1 N CYS D 54 O TYR D 103
SHEET 3 I 6 ASP D 150 HIS D 157 -1 O TYR D 152 N ILE D 57
SHEET 4 I 6 LEU D 16 ASN D 25 -1 N CYS D 18 O ILE D 151
SHEET 5 I 6 VAL D 35 ASN D 41 -1 O HIS D 37 N ILE D 24
SHEET 6 I 6 LEU D 114 LYS D 119 -1 O LEU D 114 N ILE D 40
SHEET 1 J 2 LYS D 122 TYR D 123 0
SHEET 2 J 2 ASN D 134 TYR D 135 -1 O ASN D 134 N TYR D 123
SHEET 1 K 5 ILE D 240 PHE D 246 0
SHEET 2 K 5 ILE D 211 VAL D 217 1 N ILE D 213 O HIS D 243
SHEET 3 K 5 PHE D 173 THR D 178 1 N PHE D 175 O TYR D 214
SHEET 4 K 5 GLU D 280 GLY D 285 1 O TYR D 282 N ILE D 176
SHEET 5 K 5 VAL D 311 VAL D 315 1 O HIS D 312 N ILE D 283
SHEET 1 L 6 ARG E 101 SER E 104 0
SHEET 2 L 6 THR E 53 ILE E 57 -1 N ILE E 56 O ARG E 101
SHEET 3 L 6 ASP E 150 HIS E 157 -1 O HIS E 157 N THR E 53
SHEET 4 L 6 LEU E 16 ASN E 25 -1 N CYS E 18 O ILE E 151
SHEET 5 L 6 GLU E 34 ASN E 41 -1 O HIS E 37 N ILE E 24
SHEET 6 L 6 LEU E 114 ILE E 120 -1 O ILE E 120 N GLU E 34
SHEET 1 M 5 ILE E 240 PHE E 246 0
SHEET 2 M 5 ILE E 211 VAL E 217 1 N ILE E 213 O HIS E 243
SHEET 3 M 5 PHE E 173 THR E 178 1 N PHE E 175 O TYR E 214
SHEET 4 M 5 GLU E 280 GLY E 285 1 O GLU E 280 N ILE E 174
SHEET 5 M 5 VAL E 311 VAL E 315 1 O HIS E 312 N ILE E 283
SHEET 1 N 6 ARG F 101 SER F 104 0
SHEET 2 N 6 THR F 53 ILE F 56 -1 N CYS F 54 O TYR F 103
SHEET 3 N 6 ASP F 150 HIS F 157 -1 O HIS F 157 N THR F 53
SHEET 4 N 6 LEU F 16 ASN F 25 -1 N LEU F 16 O LEU F 153
SHEET 5 N 6 VAL F 35 ASN F 41 -1 O HIS F 37 N ILE F 24
SHEET 6 N 6 LEU F 114 LYS F 119 -1 O ILE F 118 N TYR F 36
SHEET 1 O 5 ILE F 240 PHE F 246 0
SHEET 2 O 5 ILE F 211 VAL F 217 1 N TYR F 215 O VAL F 245
SHEET 3 O 5 PHE F 173 THR F 178 1 N ALA F 177 O GLY F 216
SHEET 4 O 5 GLU F 280 GLY F 285 1 O TYR F 282 N ILE F 176
SHEET 5 O 5 VAL F 311 VAL F 315 1 O GLU F 314 N ILE F 283
SSBOND 1 CYS A 99 CYS B 99 1555 1555 2.03
SSBOND 2 CYS C 99 CYS D 99 1555 1555 2.04
SSBOND 3 CYS E 99 CYS F 99 1555 1555 2.03
LINK O4P A2P A 416 NA NA A9001 1555 1555 2.70
LINK NA NA A9001 O HOH A9028 1555 1555 2.98
SITE 1 AC1 4 THR A 178 HIS A 286 A2P A 416 HOH A9028
SITE 1 AC2 22 ARG A 101 LEU A 102 TYR A 103 SER A 104
SITE 2 AC2 22 ALA A 117 ILE A 118 LYS A 119 HIS A 121
SITE 3 AC2 22 LYS A 122 TYR A 123 GLY A 136 TYR A 137
SITE 4 AC2 22 CYS A 138 SER A 139 THR A 180 TYR A 316
SITE 5 AC2 22 HOH A9003 HOH A9007 HOH A9011 HOH A9039
SITE 6 AC2 22 LEU B 102 FAD B 415
SITE 1 AC3 15 LYS A 119 GLY A 216 VAL A 217 TYR A 218
SITE 2 AC3 15 SER A 247 TYR A 258 GLN A 260 HIS A 286
SITE 3 AC3 15 SER A 288 NA A9001 HOH A9035 TYR B 258
SITE 4 AC3 15 LYS B 287 SER B 288 A2P B 416
SITE 1 AC4 21 LEU A 102 FAD A 415 ARG B 101 LEU B 102
SITE 2 AC4 21 TYR B 103 SER B 104 ALA B 117 ILE B 118
SITE 3 AC4 21 LYS B 119 HIS B 121 TYR B 123 GLY B 136
SITE 4 AC4 21 TYR B 137 CYS B 138 SER B 139 THR B 180
SITE 5 AC4 21 TYR B 316 HOH B 433 HOH B 436 HOH B 452
SITE 6 AC4 21 HOH B 463
SITE 1 AC5 13 TYR A 258 SER A 288 A2P A 416 GLY B 179
SITE 2 AC5 13 GLY B 216 VAL B 217 TYR B 218 SER B 247
SITE 3 AC5 13 TYR B 258 GLN B 260 HIS B 286 SER B 288
SITE 4 AC5 13 HOH B 437
SITE 1 AC6 24 ARG C 101 LEU C 102 TYR C 103 SER C 104
SITE 2 AC6 24 ALA C 117 ILE C 118 LYS C 119 HIS C 121
SITE 3 AC6 24 TYR C 123 GLY C 136 TYR C 137 CYS C 138
SITE 4 AC6 24 SER C 139 THR C 180 GLU C 314 TYR C 316
SITE 5 AC6 24 HOH C 419 HOH C 423 HOH C 441 HOH C 449
SITE 6 AC6 24 HOH C 454 HOH C 457 LEU D 102 FAD D 415
SITE 1 AC7 16 LYS C 119 GLY C 216 VAL C 217 TYR C 218
SITE 2 AC7 16 SER C 247 TYR C 258 GLN C 260 HIS C 286
SITE 3 AC7 16 SER C 288 HOH C 428 HOH C 438 HOH C 446
SITE 4 AC7 16 TYR D 258 LYS D 287 SER D 288 A2P D 416
SITE 1 AC8 19 LEU C 102 FAD C 415 ARG D 101 LEU D 102
SITE 2 AC8 19 TYR D 103 SER D 104 ALA D 117 ILE D 118
SITE 3 AC8 19 LYS D 119 HIS D 121 TYR D 123 GLY D 136
SITE 4 AC8 19 TYR D 137 CYS D 138 SER D 139 THR D 180
SITE 5 AC8 19 TYR D 316 HOH D 436 HOH D 445
SITE 1 AC9 14 TYR C 258 LYS C 287 SER C 288 A2P C 416
SITE 2 AC9 14 GLY D 216 VAL D 217 TYR D 218 SER D 247
SITE 3 AC9 14 TYR D 258 GLN D 260 HIS D 286 SER D 288
SITE 4 AC9 14 HOH D 424 HOH D 433
SITE 1 BC1 18 ARG E 101 LEU E 102 TYR E 103 SER E 104
SITE 2 BC1 18 ALA E 117 ILE E 118 LYS E 119 HIS E 121
SITE 3 BC1 18 TYR E 123 GLY E 136 TYR E 137 CYS E 138
SITE 4 BC1 18 SER E 139 THR E 180 TYR E 316 HOH E 424
SITE 5 BC1 18 LEU F 102 FAD F 415
SITE 1 BC2 15 LYS E 119 THR E 178 GLY E 179 GLY E 216
SITE 2 BC2 15 VAL E 217 TYR E 218 SER E 247 TYR E 258
SITE 3 BC2 15 GLN E 260 HIS E 286 SER E 288 TYR F 258
SITE 4 BC2 15 LYS F 287 SER F 288 A2P F 416
SITE 1 BC3 17 LEU E 102 FAD E 415 ARG F 101 LEU F 102
SITE 2 BC3 17 TYR F 103 SER F 104 ALA F 117 LYS F 119
SITE 3 BC3 17 HIS F 121 TYR F 123 GLY F 136 TYR F 137
SITE 4 BC3 17 CYS F 138 SER F 139 THR F 180 TYR F 316
SITE 5 BC3 17 HOH F 429
SITE 1 BC4 16 TYR E 258 LYS E 287 SER E 288 TYR E 291
SITE 2 BC4 16 LYS E 292 A2P E 416 LYS F 119 THR F 178
SITE 3 BC4 16 GLY F 216 VAL F 217 TYR F 218 SER F 247
SITE 4 BC4 16 TYR F 258 HIS F 286 SER F 288 HOH F 426
CRYST1 123.129 123.129 133.807 90.00 90.00 120.00 P 31 18
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 0.008122 0.004689 0.000000 0.00000
SCALE2 0.000000 0.009378 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007473 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
