HEADER OXIDOREDUCTASE 07-MAY-11 3AYJ
TITLE X-RAY CRYSTAL STRUCTURES OF L-PHENYLALANINE OXIDASE (DEAMINATING AND
TITLE 2 DECABOXYLATING) FROM PSEUDOMONAS SP. P501. STRUCTURES OF THE ENZYME-
TITLE 3 LIGAND COMPLEX AND CATALYTIC MECHANISM
CAVEAT 3AYJ MET A 570 HAS BAD GEOMETRY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRO-ENZYME OF L-PHENYLALANINE OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.13.12.9;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS;
SOURCE 3 ORGANISM_TAXID: 266807;
SOURCE 4 STRAIN: P-501;
SOURCE 5 GENE: PROPAO;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS L-PHENYLALANINE OXIDASE, AMINO ACID OXIDASE, FLAVOENZYME, L-PHE
KEYWDS 2 BINDING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.IDA,M.SUGURO,H.SUZUKI
REVDAT 3 01-NOV-23 3AYJ 1 REMARK SEQADV
REVDAT 2 19-JUN-13 3AYJ 1 JRNL
REVDAT 1 31-AUG-11 3AYJ 0
JRNL AUTH K.IDA,M.SUGURO,H.SUZUKI
JRNL TITL HIGH RESOLUTION X-RAY CRYSTAL STRUCTURES OF L-PHENYLALANINE
JRNL TITL 2 OXIDASE (DEAMINATING AND DECARBOXYLATING) FROM PSEUDOMONAS
JRNL TITL 3 SP. P-501. STRUCTURES OF THE ENZYME-LIGAND COMPLEX AND
JRNL TITL 4 CATALYTIC MECHANISM
JRNL REF J.BIOCHEM. V. 150 659 2011
JRNL REFN ISSN 0021-924X
JRNL PMID 21841183
JRNL DOI 10.1093/JB/MVR103
REMARK 2
REMARK 2 RESOLUTION. 1.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 584957
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) : 0.112
REMARK 3 R VALUE (WORKING SET) : 0.111
REMARK 3 FREE R VALUE : 0.131
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 30827
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) : 1.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 42333
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.85
REMARK 3 BIN R VALUE (WORKING SET) : 0.1640
REMARK 3 BIN FREE R VALUE SET COUNT : 2190
REMARK 3 BIN FREE R VALUE : 0.1760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10424
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 152
REMARK 3 SOLVENT ATOMS : 2337
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.41000
REMARK 3 B22 (A**2) : 0.10000
REMARK 3 B33 (A**2) : -0.52000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.022
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.013
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.592
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.984
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.981
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10852 ; 0.025 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7121 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14830 ; 2.154 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17228 ; 1.141 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1362 ; 6.525 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 468 ;35.276 ;23.248
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1560 ;11.623 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 72 ;22.252 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1638 ; 0.134 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 12256 ; 0.013 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2269 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2571 ; 0.267 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 8341 ; 0.225 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 5474 ; 0.191 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 5426 ; 0.092 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 1707 ; 0.239 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.037 ; 0.200
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): 23 ; 0.380 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 62 ; 0.249 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 99 ; 0.309 ; 0.200
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): 8582 ; 2.640 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2770 ; 0.848 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10904 ; 3.150 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4824 ; 4.628 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3926 ; 5.854 ; 4.500
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): 22346 ; 2.306 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 2337 ;19.062 ; 5.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 17697 ; 7.176 ; 5.000
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 3AYJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAY-11.
REMARK 100 THE DEPOSITION ID IS D_1000029855.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUL-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 615937
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 29.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 5.300
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.1
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.39800
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: NULL
REMARK 200 STARTING MODEL: 2YR4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH7.5, 1.0M AMMONIUM
REMARK 280 SULFATE, PH 7.50, VAPOR DIFFUSION, TEMPERATURE 297K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 50.49250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.22900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 56.47050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.22900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 50.49250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 56.47050
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: 7090 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42490 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 1
REMARK 465 VAL A 2
REMARK 465 THR A 3
REMARK 465 VAL A 4
REMARK 465 ILE A 5
REMARK 465 PRO A 6
REMARK 465 ARG A 7
REMARK 465 LEU A 8
REMARK 465 LEU A 9
REMARK 465 GLY A 10
REMARK 465 LEU A 11
REMARK 465 LYS A 12
REMARK 465 ASP A 13
REMARK 465 GLU A 14
REMARK 465 LYS A 15
REMARK 465 PRO A 105
REMARK 465 GLY A 106
REMARK 465 ILE A 107
REMARK 465 LYS A 108
REMARK 465 GLU A 522
REMARK 465 ASP A 523
REMARK 465 GLY A 524
REMARK 465 GLN A 525
REMARK 465 GLU A 708
REMARK 465 LEU A 709
REMARK 465 ALA A 710
REMARK 465 THR A 711
REMARK 465 SER A 712
REMARK 465 GLN A 713
REMARK 465 LEU A 714
REMARK 465 GLU A 715
REMARK 465 HIS A 716
REMARK 465 HIS A 717
REMARK 465 HIS A 718
REMARK 465 HIS A 719
REMARK 465 HIS A 720
REMARK 465 HIS A 721
REMARK 465 GLY B 1
REMARK 465 VAL B 2
REMARK 465 THR B 3
REMARK 465 VAL B 4
REMARK 465 ILE B 5
REMARK 465 PRO B 6
REMARK 465 ARG B 7
REMARK 465 LEU B 8
REMARK 465 LEU B 9
REMARK 465 GLY B 10
REMARK 465 LEU B 11
REMARK 465 LYS B 12
REMARK 465 ASP B 13
REMARK 465 GLU B 14
REMARK 465 LYS B 15
REMARK 465 PRO B 105
REMARK 465 GLY B 106
REMARK 465 ILE B 107
REMARK 465 LYS B 108
REMARK 465 GLU B 522
REMARK 465 ASP B 523
REMARK 465 GLY B 524
REMARK 465 GLN B 525
REMARK 465 GLU B 708
REMARK 465 LEU B 709
REMARK 465 ALA B 710
REMARK 465 THR B 711
REMARK 465 SER B 712
REMARK 465 GLN B 713
REMARK 465 LEU B 714
REMARK 465 GLU B 715
REMARK 465 HIS B 716
REMARK 465 HIS B 717
REMARK 465 HIS B 718
REMARK 465 HIS B 719
REMARK 465 HIS B 720
REMARK 465 HIS B 721
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 6104 O HOH A 7226 1.10
REMARK 500 O HOH B 5648 O HOH B 7292 1.43
REMARK 500 O HOH A 5581 O HOH A 6542 1.44
REMARK 500 O HOH A 5338 O HOH A 6267 1.50
REMARK 500 O HOH A 5509 O HOH A 7333 1.53
REMARK 500 CZ ARG A 576 O HOH A 7214 1.61
REMARK 500 NH1 ARG B 576 O HOH B 7215 1.72
REMARK 500 O HOH A 6307 O HOH A 7264 1.73
REMARK 500 CB ALA B 707 O HOH B 7180 1.74
REMARK 500 O HOH A 6408 O HOH A 7288 1.76
REMARK 500 CD2 LEU B 203 O HOH B 7224 1.78
REMARK 500 O HOH A 5733 O HOH A 6869 1.78
REMARK 500 O HOH A 5885 O HOH A 7219 1.78
REMARK 500 O HOH A 5757 O HOH A 7234 1.80
REMARK 500 CG2 VAL A 273 O HOH A 7335 1.83
REMARK 500 O HOH B 5397 O HOH B 7235 1.84
REMARK 500 OE1 GLU A 250 O HOH A 6445 1.85
REMARK 500 O HOH B 5680 O HOH B 7235 1.85
REMARK 500 O HOH B 5995 O HOH B 7007 1.87
REMARK 500 O HOH B 5481 O HOH B 7248 1.88
REMARK 500 NE ARG A 576 O HOH A 7214 1.89
REMARK 500 O HOH A 5833 O HOH A 7221 1.89
REMARK 500 O HOH B 6537 O HOH B 6658 1.90
REMARK 500 CG GLU A 690 O HOH A 7212 1.95
REMARK 500 CD ARG B 475 O HOH B 5680 1.97
REMARK 500 O HOH B 5697 O HOH B 7171 1.99
REMARK 500 O LYS A 703 O HOH A 7160 1.99
REMARK 500 O ALA A 280 O HOH A 7314 1.99
REMARK 500 CD ARG A 475 O HOH A 7220 2.01
REMARK 500 O HOH B 6360 O HOH B 6855 2.01
REMARK 500 O HOH A 6346 O HOH A 7333 2.02
REMARK 500 O HOH A 5848 O HOH A 7265 2.02
REMARK 500 O HOH A 6131 O HOH A 7300 2.02
REMARK 500 CG GLU A 250 O HOH A 7206 2.02
REMARK 500 O HOH A 5965 O HOH A 7256 2.03
REMARK 500 CD GLN B 368 O HOH B 7218 2.04
REMARK 500 O PRO A 705 O HOH A 7176 2.05
REMARK 500 O HOH B 7012 O HOH B 7199 2.05
REMARK 500 O HOH A 5289 O HOH A 7153 2.06
REMARK 500 CB ASN A 352 O HOH A 7156 2.06
REMARK 500 O HOH B 6934 O HOH B 7001 2.07
REMARK 500 CG ARG B 58 O HOH B 6553 2.07
REMARK 500 O HOH A 5518 O HOH A 5692 2.07
REMARK 500 O HOH A 7213 O HOH A 7254 2.08
REMARK 500 O HOH B 5691 O HOH B 7177 2.08
REMARK 500 O HOH B 6241 O HOH B 7190 2.08
REMARK 500 O HOH B 6808 O HOH B 7179 2.09
REMARK 500 O HOH B 6083 O HOH B 7182 2.09
REMARK 500 O HOH A 6117 O HOH A 7157 2.09
REMARK 500 OE2 GLU A 559 O HOH A 7204 2.09
REMARK 500
REMARK 500 THIS ENTRY HAS 87 CLOSE CONTACTS
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 O HOH A 6708 O HOH B 5918 3756 1.53
REMARK 500 O SER B 642 O HOH A 7291 2664 1.63
REMARK 500 O HOH A 5893 O HOH B 5532 3756 1.66
REMARK 500 O HOH A 5408 O HOH B 6743 2664 1.70
REMARK 500 C SER B 642 O HOH A 7291 2664 1.98
REMARK 500 O HOH A 5935 O HOH A 7149 3756 2.14
REMARK 500
REMARK 500 REMARK: NULL
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 ARG A 32 CG ARG A 32 CD -0.214
REMARK 500 ARG A 77 CZ ARG A 77 NH1 -0.100
REMARK 500 ILE A 147 CA ILE A 147 CB 0.234
REMARK 500 TYR A 154 CZ TYR A 154 CE2 -0.081
REMARK 500 PRO A 245 N PRO A 245 CA 0.155
REMARK 500 PRO A 245 CA PRO A 245 C 0.141
REMARK 500 ALA A 246 C ALA A 246 O 0.152
REMARK 500 GLU A 250 CG GLU A 250 CD -0.141
REMARK 500 GLU A 282 CD GLU A 282 OE2 0.078
REMARK 500 SER A 323 CA SER A 323 CB 0.124
REMARK 500 SER A 323 CB SER A 323 OG -0.137
REMARK 500 GLU A 345 CG GLU A 345 CD -0.116
REMARK 500 SER A 422 CA SER A 422 CB 0.150
REMARK 500 GLN A 430 CD GLN A 430 OE1 0.133
REMARK 500 ARG A 544 CG ARG A 544 CD 0.172
REMARK 500 ARG A 544 CD ARG A 544 NE 0.157
REMARK 500 ARG A 544 NE ARG A 544 CZ -0.111
REMARK 500 ARG A 544 CZ ARG A 544 NH2 -0.158
REMARK 500 GLU A 559 CD GLU A 559 OE2 -0.074
REMARK 500 MET A 570 CG MET A 570 SD -0.645
REMARK 500 ARG A 576 CZ ARG A 576 NH2 0.183
REMARK 500 LYS A 579 CD LYS A 579 CE 0.152
REMARK 500 GLU A 597 CD GLU A 597 OE2 -0.071
REMARK 500 ARG A 599 NE ARG A 599 CZ 0.083
REMARK 500 THR A 609 CB THR A 609 OG1 0.133
REMARK 500 THR A 609 CB THR A 609 CG2 -0.237
REMARK 500 SER A 642 CB SER A 642 OG 0.103
REMARK 500 ARG B 32 CG ARG B 32 CD -0.195
REMARK 500 ARG B 58 CZ ARG B 58 NH2 0.080
REMARK 500 ILE B 147 CA ILE B 147 CB 0.306
REMARK 500 LYS B 204 CD LYS B 204 CE 0.155
REMARK 500 GLU B 282 CG GLU B 282 CD 0.098
REMARK 500 GLU B 282 CD GLU B 282 OE2 0.069
REMARK 500 ASP B 296 CB ASP B 296 CG 0.183
REMARK 500 GLU B 297 CG GLU B 297 CD 0.106
REMARK 500 GLU B 297 CD GLU B 297 OE2 0.237
REMARK 500 SER B 323 CB SER B 323 OG -0.079
REMARK 500 ARG B 544 CG ARG B 544 CD 0.235
REMARK 500 ARG B 544 CD ARG B 544 NE 0.187
REMARK 500 ARG B 544 NE ARG B 544 CZ -0.107
REMARK 500 ARG B 544 CZ ARG B 544 NH2 -0.196
REMARK 500 ARG B 546 CZ ARG B 546 NH1 -0.086
REMARK 500 ARG B 576 CZ ARG B 576 NH2 0.157
REMARK 500 THR B 609 CB THR B 609 OG1 0.142
REMARK 500 THR B 609 CB THR B 609 CG2 -0.301
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 32 NE - CZ - NH1 ANGL. DEV. = 5.1 DEGREES
REMARK 500 ARG A 77 CD - NE - CZ ANGL. DEV. = 9.5 DEGREES
REMARK 500 PRO A 245 C - N - CA ANGL. DEV. = -17.1 DEGREES
REMARK 500 PRO A 245 O - C - N ANGL. DEV. = -11.4 DEGREES
REMARK 500 ASP A 247 CB - CG - OD1 ANGL. DEV. = -6.4 DEGREES
REMARK 500 ASP A 247 CB - CG - OD2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 LEU A 293 CB - CG - CD1 ANGL. DEV. = 13.4 DEGREES
REMARK 500 ASP A 294 CB - CG - OD1 ANGL. DEV. = 6.6 DEGREES
REMARK 500 ARG A 370 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG A 370 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 455 CB - CG - OD1 ANGL. DEV. = -7.1 DEGREES
REMARK 500 ARG A 475 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 ARG A 544 CG - CD - NE ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG A 544 NE - CZ - NH1 ANGL. DEV. = -9.4 DEGREES
REMARK 500 ARG A 544 NE - CZ - NH2 ANGL. DEV. = 11.6 DEGREES
REMARK 500 ARG A 546 NE - CZ - NH1 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 546 NE - CZ - NH2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 GLU A 559 OE1 - CD - OE2 ANGL. DEV. = -10.8 DEGREES
REMARK 500 ASP A 564 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG A 568 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 MET A 570 CG - SD - CE ANGL. DEV. = 25.7 DEGREES
REMARK 500 ARG A 573 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 576 CD - NE - CZ ANGL. DEV. = 14.1 DEGREES
REMARK 500 ARG A 576 NE - CZ - NH1 ANGL. DEV. = -8.0 DEGREES
REMARK 500 ARG A 576 NE - CZ - NH2 ANGL. DEV. = 9.7 DEGREES
REMARK 500 TYR A 592 CB - CG - CD2 ANGL. DEV. = 7.9 DEGREES
REMARK 500 TYR A 592 CB - CG - CD1 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG A 599 NE - CZ - NH1 ANGL. DEV. = 6.8 DEGREES
REMARK 500 ARG A 599 NE - CZ - NH2 ANGL. DEV. = -8.5 DEGREES
REMARK 500 ARG A 633 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 692 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG A 692 NE - CZ - NH2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG B 77 CD - NE - CZ ANGL. DEV. = 17.5 DEGREES
REMARK 500 ARG B 77 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG B 77 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP B 89 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP B 89 CB - CG - OD2 ANGL. DEV. = -6.1 DEGREES
REMARK 500 ASP B 296 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 GLU B 297 CG - CD - OE1 ANGL. DEV. = -17.7 DEGREES
REMARK 500 GLU B 297 CG - CD - OE2 ANGL. DEV. = 13.3 DEGREES
REMARK 500 ARG B 329 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ARG B 370 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG B 370 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ARG B 386 NE - CZ - NH1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 386 NE - CZ - NH2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG B 475 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ARG B 544 CG - CD - NE ANGL. DEV. = 17.4 DEGREES
REMARK 500 ARG B 544 NE - CZ - NH1 ANGL. DEV. = -7.6 DEGREES
REMARK 500 ARG B 544 NE - CZ - NH2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 ARG B 546 NE - CZ - NH1 ANGL. DEV. = -5.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 60 ANGLE DEVIATIONS.
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 SER A 36 49.49 -144.40
REMARK 500 MET A 142 -17.10 -151.33
REMARK 500 ALA A 409 56.43 -106.02
REMARK 500 ALA A 511 -67.32 72.19
REMARK 500 GLU A 539 -131.13 53.92
REMARK 500 LEU A 657 50.37 -144.32
REMARK 500 SER B 36 48.54 -143.23
REMARK 500 MET B 142 -15.82 -152.45
REMARK 500 ASP B 247 -10.22 73.28
REMARK 500 ASP B 294 -179.14 -64.60
REMARK 500 ALA B 409 54.65 -105.46
REMARK 500 ALA B 511 -65.32 70.00
REMARK 500 GLU B 539 -132.30 53.58
REMARK 500 ASP B 644 63.32 -102.52
REMARK 500 LEU B 657 50.52 -144.25
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO A 244 PRO A 245 141.77
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A 335 0.07 SIDE CHAIN
REMARK 500 GLN A 430 0.09 SIDE CHAIN
REMARK 500 TYR A 654 0.09 SIDE CHAIN
REMARK 500 ARG B 77 0.08 SIDE CHAIN
REMARK 500 TYR B 335 0.07 SIDE CHAIN
REMARK 500 TYR B 654 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 ALA A 241 -10.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 3002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHE A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHE B 1904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3AYI RELATED DB: PDB
REMARK 900 RELATED ID: 3AYL RELATED DB: PDB
DBREF 3AYJ A 1 713 UNP Q5W9R9 Q5W9R9_9PSED 2 714
DBREF 3AYJ B 1 713 UNP Q5W9R9 Q5W9R9_9PSED 2 714
SEQADV 3AYJ LEU A 714 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ GLU A 715 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ HIS A 716 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ HIS A 717 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ HIS A 718 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ HIS A 719 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ HIS A 720 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ HIS A 721 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ LEU B 714 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ GLU B 715 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ HIS B 716 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ HIS B 717 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ HIS B 718 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ HIS B 719 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ HIS B 720 UNP Q5W9R9 EXPRESSION TAG
SEQADV 3AYJ HIS B 721 UNP Q5W9R9 EXPRESSION TAG
SEQRES 1 A 721 GLY VAL THR VAL ILE PRO ARG LEU LEU GLY LEU LYS ASP
SEQRES 2 A 721 GLU LYS LYS ILE ALA THR THR VAL GLY GLU ALA ARG LEU
SEQRES 3 A 721 SER GLY ILE ASN TYR ARG HIS PRO ASP SER ALA LEU VAL
SEQRES 4 A 721 SER TYR PRO VAL ALA ALA ALA ALA PRO LEU GLY ARG LEU
SEQRES 5 A 721 PRO ALA GLY ASN TYR ARG ILE ALA ILE VAL GLY GLY GLY
SEQRES 6 A 721 ALA GLY GLY ILE ALA ALA LEU TYR GLU LEU GLY ARG LEU
SEQRES 7 A 721 ALA ALA THR LEU PRO ALA GLY SER GLY ILE ASP VAL GLN
SEQRES 8 A 721 ILE TYR GLU ALA ASP PRO ASP SER PHE LEU HIS ASP ARG
SEQRES 9 A 721 PRO GLY ILE LYS ALA ILE LYS VAL ARG GLY LEU LYS ALA
SEQRES 10 A 721 GLY ARG VAL SER ALA ALA LEU VAL HIS ASN GLY ASP PRO
SEQRES 11 A 721 ALA SER GLY ASP THR ILE TYR GLU VAL GLY ALA MET ARG
SEQRES 12 A 721 PHE PRO GLU ILE ALA GLY LEU THR TRP HIS TYR ALA SER
SEQRES 13 A 721 ALA ALA PHE GLY ASP ALA ALA PRO ILE LYS VAL PHE PRO
SEQRES 14 A 721 ASN PRO GLY LYS VAL PRO THR GLU PHE VAL PHE GLY ASN
SEQRES 15 A 721 ARG VAL ASP ARG TYR VAL GLY SER ASP PRO LYS ASP TRP
SEQRES 16 A 721 GLU ASP PRO ASP SER PRO THR LEU LYS VAL LEU GLY VAL
SEQRES 17 A 721 VAL ALA GLY GLY LEU VAL GLY ASN PRO GLN GLY GLU ASN
SEQRES 18 A 721 VAL ALA MET TYR PRO ILE ALA ASN VAL ASP PRO ALA LYS
SEQRES 19 A 721 ILE ALA ALA ILE LEU ASN ALA ALA THR PRO PRO ALA ASP
SEQRES 20 A 721 ALA LEU GLU ARG ILE GLN THR LYS TYR TRP PRO GLU PHE
SEQRES 21 A 721 ILE ALA GLN TYR ASP GLY LEU THR LEU GLY ALA ALA VAL
SEQRES 22 A 721 ARG GLU ILE VAL THR VAL ALA PHE GLU LYS GLY THR LEU
SEQRES 23 A 721 PRO PRO VAL ASP GLY VAL LEU ASP VAL ASP GLU SER ILE
SEQRES 24 A 721 SER TYR TYR VAL GLU LEU PHE GLY ARG PHE GLY PHE GLY
SEQRES 25 A 721 THR GLY GLY PHE LYS PRO LEU TYR ASN ILE SER LEU VAL
SEQRES 26 A 721 GLU MET MET ARG LEU ILE LEU TRP ASP TYR SER ASN GLU
SEQRES 27 A 721 TYR THR LEU PRO VAL THR GLU ASN VAL GLU PHE ILE ARG
SEQRES 28 A 721 ASN LEU PHE LEU LYS ALA GLN ASN VAL GLY ALA GLY LYS
SEQRES 29 A 721 LEU VAL VAL GLN VAL ARG GLN GLU ARG VAL ALA ASN ALA
SEQRES 30 A 721 CYS HIS SER GLY THR ALA SER ALA ARG ALA GLN LEU LEU
SEQRES 31 A 721 SER TYR ASP SER HIS ASN ALA VAL HIS SER GLU ALA TYR
SEQRES 32 A 721 ASP PHE VAL ILE LEU ALA VAL PRO HIS ASP GLN LEU THR
SEQRES 33 A 721 PRO ILE VAL SER ARG SER GLY PHE GLU HIS ALA ALA SER
SEQRES 34 A 721 GLN ASN LEU GLY ASP ALA GLY LEU GLY LEU GLU THR HIS
SEQRES 35 A 721 THR TYR ASN GLN VAL TYR PRO PRO LEU LEU LEU SER ASP
SEQRES 36 A 721 SER SER PRO ALA ALA ASN ALA ARG ILE VAL THR ALA ILE
SEQRES 37 A 721 GLY GLN LEU HIS MET ALA ARG SER SER LYS VAL PHE ALA
SEQRES 38 A 721 THR VAL LYS THR ALA ALA LEU ASP GLN PRO TRP VAL PRO
SEQRES 39 A 721 GLN TRP ARG GLY GLU PRO ILE LYS ALA VAL VAL SER ASP
SEQRES 40 A 721 SER GLY LEU ALA ALA SER TYR VAL VAL PRO SER PRO ILE
SEQRES 41 A 721 VAL GLU ASP GLY GLN ALA PRO GLU TYR SER SER LEU LEU
SEQRES 42 A 721 ALA SER TYR THR TRP GLU ASP ASP SER THR ARG LEU ARG
SEQRES 43 A 721 HIS ASP PHE GLY LEU TYR PRO GLN ASN PRO ALA THR GLU
SEQRES 44 A 721 THR GLY THR ALA ASP GLY MET TYR ARG THR MET VAL ASN
SEQRES 45 A 721 ARG ALA TYR ARG TYR VAL LYS TYR ALA GLY ALA SER ASN
SEQRES 46 A 721 ALA GLN PRO TRP TRP PHE TYR GLN LEU LEU ALA GLU ALA
SEQRES 47 A 721 ARG THR ALA ASP ARG PHE VAL PHE ASP TRP THR THR ASN
SEQRES 48 A 721 LYS THR ALA GLY GLY PHE LYS LEU ASP MET THR GLY ASP
SEQRES 49 A 721 HIS HIS GLN SER ASN LEU CYS PHE ARG TYR HIS THR HIS
SEQRES 50 A 721 ALA LEU ALA ALA SER LEU ASP ASN ARG PHE PHE ILE ALA
SEQRES 51 A 721 SER ASP SER TYR SER HIS LEU GLY GLY TRP LEU GLU GLY
SEQRES 52 A 721 ALA PHE MET SER ALA LEU ASN ALA VAL ALA GLY LEU ILE
SEQRES 53 A 721 VAL ARG ALA ASN ARG GLY ASP VAL SER ALA LEU SER THR
SEQRES 54 A 721 GLU ALA ARG PRO LEU VAL ILE GLY LEU ARG PRO VAL VAL
SEQRES 55 A 721 LYS VAL PRO ALA ALA GLU LEU ALA THR SER GLN LEU GLU
SEQRES 56 A 721 HIS HIS HIS HIS HIS HIS
SEQRES 1 B 721 GLY VAL THR VAL ILE PRO ARG LEU LEU GLY LEU LYS ASP
SEQRES 2 B 721 GLU LYS LYS ILE ALA THR THR VAL GLY GLU ALA ARG LEU
SEQRES 3 B 721 SER GLY ILE ASN TYR ARG HIS PRO ASP SER ALA LEU VAL
SEQRES 4 B 721 SER TYR PRO VAL ALA ALA ALA ALA PRO LEU GLY ARG LEU
SEQRES 5 B 721 PRO ALA GLY ASN TYR ARG ILE ALA ILE VAL GLY GLY GLY
SEQRES 6 B 721 ALA GLY GLY ILE ALA ALA LEU TYR GLU LEU GLY ARG LEU
SEQRES 7 B 721 ALA ALA THR LEU PRO ALA GLY SER GLY ILE ASP VAL GLN
SEQRES 8 B 721 ILE TYR GLU ALA ASP PRO ASP SER PHE LEU HIS ASP ARG
SEQRES 9 B 721 PRO GLY ILE LYS ALA ILE LYS VAL ARG GLY LEU LYS ALA
SEQRES 10 B 721 GLY ARG VAL SER ALA ALA LEU VAL HIS ASN GLY ASP PRO
SEQRES 11 B 721 ALA SER GLY ASP THR ILE TYR GLU VAL GLY ALA MET ARG
SEQRES 12 B 721 PHE PRO GLU ILE ALA GLY LEU THR TRP HIS TYR ALA SER
SEQRES 13 B 721 ALA ALA PHE GLY ASP ALA ALA PRO ILE LYS VAL PHE PRO
SEQRES 14 B 721 ASN PRO GLY LYS VAL PRO THR GLU PHE VAL PHE GLY ASN
SEQRES 15 B 721 ARG VAL ASP ARG TYR VAL GLY SER ASP PRO LYS ASP TRP
SEQRES 16 B 721 GLU ASP PRO ASP SER PRO THR LEU LYS VAL LEU GLY VAL
SEQRES 17 B 721 VAL ALA GLY GLY LEU VAL GLY ASN PRO GLN GLY GLU ASN
SEQRES 18 B 721 VAL ALA MET TYR PRO ILE ALA ASN VAL ASP PRO ALA LYS
SEQRES 19 B 721 ILE ALA ALA ILE LEU ASN ALA ALA THR PRO PRO ALA ASP
SEQRES 20 B 721 ALA LEU GLU ARG ILE GLN THR LYS TYR TRP PRO GLU PHE
SEQRES 21 B 721 ILE ALA GLN TYR ASP GLY LEU THR LEU GLY ALA ALA VAL
SEQRES 22 B 721 ARG GLU ILE VAL THR VAL ALA PHE GLU LYS GLY THR LEU
SEQRES 23 B 721 PRO PRO VAL ASP GLY VAL LEU ASP VAL ASP GLU SER ILE
SEQRES 24 B 721 SER TYR TYR VAL GLU LEU PHE GLY ARG PHE GLY PHE GLY
SEQRES 25 B 721 THR GLY GLY PHE LYS PRO LEU TYR ASN ILE SER LEU VAL
SEQRES 26 B 721 GLU MET MET ARG LEU ILE LEU TRP ASP TYR SER ASN GLU
SEQRES 27 B 721 TYR THR LEU PRO VAL THR GLU ASN VAL GLU PHE ILE ARG
SEQRES 28 B 721 ASN LEU PHE LEU LYS ALA GLN ASN VAL GLY ALA GLY LYS
SEQRES 29 B 721 LEU VAL VAL GLN VAL ARG GLN GLU ARG VAL ALA ASN ALA
SEQRES 30 B 721 CYS HIS SER GLY THR ALA SER ALA ARG ALA GLN LEU LEU
SEQRES 31 B 721 SER TYR ASP SER HIS ASN ALA VAL HIS SER GLU ALA TYR
SEQRES 32 B 721 ASP PHE VAL ILE LEU ALA VAL PRO HIS ASP GLN LEU THR
SEQRES 33 B 721 PRO ILE VAL SER ARG SER GLY PHE GLU HIS ALA ALA SER
SEQRES 34 B 721 GLN ASN LEU GLY ASP ALA GLY LEU GLY LEU GLU THR HIS
SEQRES 35 B 721 THR TYR ASN GLN VAL TYR PRO PRO LEU LEU LEU SER ASP
SEQRES 36 B 721 SER SER PRO ALA ALA ASN ALA ARG ILE VAL THR ALA ILE
SEQRES 37 B 721 GLY GLN LEU HIS MET ALA ARG SER SER LYS VAL PHE ALA
SEQRES 38 B 721 THR VAL LYS THR ALA ALA LEU ASP GLN PRO TRP VAL PRO
SEQRES 39 B 721 GLN TRP ARG GLY GLU PRO ILE LYS ALA VAL VAL SER ASP
SEQRES 40 B 721 SER GLY LEU ALA ALA SER TYR VAL VAL PRO SER PRO ILE
SEQRES 41 B 721 VAL GLU ASP GLY GLN ALA PRO GLU TYR SER SER LEU LEU
SEQRES 42 B 721 ALA SER TYR THR TRP GLU ASP ASP SER THR ARG LEU ARG
SEQRES 43 B 721 HIS ASP PHE GLY LEU TYR PRO GLN ASN PRO ALA THR GLU
SEQRES 44 B 721 THR GLY THR ALA ASP GLY MET TYR ARG THR MET VAL ASN
SEQRES 45 B 721 ARG ALA TYR ARG TYR VAL LYS TYR ALA GLY ALA SER ASN
SEQRES 46 B 721 ALA GLN PRO TRP TRP PHE TYR GLN LEU LEU ALA GLU ALA
SEQRES 47 B 721 ARG THR ALA ASP ARG PHE VAL PHE ASP TRP THR THR ASN
SEQRES 48 B 721 LYS THR ALA GLY GLY PHE LYS LEU ASP MET THR GLY ASP
SEQRES 49 B 721 HIS HIS GLN SER ASN LEU CYS PHE ARG TYR HIS THR HIS
SEQRES 50 B 721 ALA LEU ALA ALA SER LEU ASP ASN ARG PHE PHE ILE ALA
SEQRES 51 B 721 SER ASP SER TYR SER HIS LEU GLY GLY TRP LEU GLU GLY
SEQRES 52 B 721 ALA PHE MET SER ALA LEU ASN ALA VAL ALA GLY LEU ILE
SEQRES 53 B 721 VAL ARG ALA ASN ARG GLY ASP VAL SER ALA LEU SER THR
SEQRES 54 B 721 GLU ALA ARG PRO LEU VAL ILE GLY LEU ARG PRO VAL VAL
SEQRES 55 B 721 LYS VAL PRO ALA ALA GLU LEU ALA THR SER GLN LEU GLU
SEQRES 56 B 721 HIS HIS HIS HIS HIS HIS
HET SO4 A3001 5
HET SO4 A3002 5
HET FAD A 801 53
HET PHE A 904 12
HET GOL A 902 6
HET FAD B 801 53
HET PHE B1904 12
HET GOL B1902 6
HETNAM SO4 SULFATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM PHE PHENYLALANINE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 5 FAD 2(C27 H33 N9 O15 P2)
FORMUL 6 PHE 2(C9 H11 N O2)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 11 HOH *2337(H2 O)
HELIX 1 1 THR A 20 GLY A 28 1 9
HELIX 2 2 HIS A 33 ALA A 37 5 5
HELIX 3 3 SER A 40 ALA A 45 1 6
HELIX 4 4 GLY A 65 ALA A 80 1 16
HELIX 5 5 SER A 99 ASP A 103 5 5
HELIX 6 6 ASP A 129 GLY A 133 5 5
HELIX 7 7 ALA A 148 GLY A 160 1 13
HELIX 8 8 ASP A 191 TRP A 195 5 5
HELIX 9 9 SER A 200 VAL A 214 1 15
HELIX 10 10 ASP A 231 ASN A 240 1 10
HELIX 11 11 PRO A 245 LYS A 255 1 11
HELIX 12 12 LYS A 255 ASP A 265 1 11
HELIX 13 13 THR A 268 LYS A 283 1 16
HELIX 14 14 PRO A 288 VAL A 292 5 5
HELIX 15 15 ASP A 294 GLY A 310 1 17
HELIX 16 16 PHE A 316 TYR A 320 5 5
HELIX 17 17 SER A 323 TRP A 333 1 11
HELIX 18 18 ASN A 346 GLY A 361 1 16
HELIX 19 19 PRO A 411 SER A 420 1 10
HELIX 20 20 ASP A 434 GLY A 438 5 5
HELIX 21 21 SER A 457 GLN A 470 1 14
HELIX 22 22 ALA A 486 GLN A 490 5 5
HELIX 23 23 GLU A 539 HIS A 547 1 9
HELIX 24 24 ALA A 563 ALA A 574 1 12
HELIX 25 25 TRP A 589 GLU A 597 1 9
HELIX 26 26 THR A 609 ASN A 611 5 3
HELIX 27 27 ASP A 624 TYR A 634 1 11
HELIX 28 28 HIS A 635 ALA A 640 5 6
HELIX 29 29 SER A 651 SER A 655 5 5
HELIX 30 30 TRP A 660 ASN A 680 1 21
HELIX 31 31 ASP A 683 LEU A 687 5 5
HELIX 32 32 ARG A 692 GLY A 697 1 6
HELIX 33 33 THR B 20 GLY B 28 1 9
HELIX 34 34 HIS B 33 ALA B 37 5 5
HELIX 35 35 SER B 40 ALA B 45 1 6
HELIX 36 36 GLY B 65 ALA B 80 1 16
HELIX 37 37 SER B 99 ASP B 103 5 5
HELIX 38 38 ALA B 148 GLY B 160 1 13
HELIX 39 39 ASP B 191 TRP B 195 5 5
HELIX 40 40 SER B 200 VAL B 214 1 15
HELIX 41 41 ASP B 231 ASN B 240 1 10
HELIX 42 42 ASP B 247 LYS B 255 1 9
HELIX 43 43 LYS B 255 ASP B 265 1 11
HELIX 44 44 THR B 268 LYS B 283 1 16
HELIX 45 45 ASP B 294 GLY B 310 1 17
HELIX 46 46 PHE B 316 TYR B 320 5 5
HELIX 47 47 SER B 323 TRP B 333 1 11
HELIX 48 48 ASN B 346 GLY B 361 1 16
HELIX 49 49 PRO B 411 SER B 420 1 10
HELIX 50 50 ASP B 434 GLY B 438 5 5
HELIX 51 51 SER B 457 GLN B 470 1 14
HELIX 52 52 ALA B 486 GLN B 490 5 5
HELIX 53 53 GLU B 539 HIS B 547 1 9
HELIX 54 54 ALA B 563 ALA B 574 1 12
HELIX 55 55 TRP B 589 ALA B 598 1 10
HELIX 56 56 ASP B 624 TYR B 634 1 11
HELIX 57 57 HIS B 635 ALA B 640 5 6
HELIX 58 58 SER B 651 SER B 655 5 5
HELIX 59 59 TRP B 660 ASN B 680 1 21
HELIX 60 60 ASP B 683 LEU B 687 5 5
HELIX 61 61 ARG B 692 GLY B 697 1 6
SHEET 1 A 5 LEU A 365 ARG A 370 0
SHEET 2 A 5 GLY A 87 TYR A 93 1 N ILE A 92 O ARG A 370
SHEET 3 A 5 ASN A 56 VAL A 62 1 N ILE A 59 O ASP A 89
SHEET 4 A 5 PHE A 405 LEU A 408 1 O ILE A 407 N VAL A 62
SHEET 5 A 5 PHE A 647 ILE A 649 1 O PHE A 648 N LEU A 408
SHEET 1 B 3 ILE A 110 LYS A 111 0
SHEET 2 B 3 VAL A 120 VAL A 125 -1 O LEU A 124 N LYS A 111
SHEET 3 B 3 LYS A 116 ALA A 117 -1 N ALA A 117 O VAL A 120
SHEET 1 C 3 ILE A 110 LYS A 111 0
SHEET 2 C 3 VAL A 120 VAL A 125 -1 O LEU A 124 N LYS A 111
SHEET 3 C 3 THR A 135 GLU A 138 -1 O TYR A 137 N ALA A 123
SHEET 1 D 2 PHE A 144 PRO A 145 0
SHEET 2 D 2 GLU A 338 TYR A 339 -1 O TYR A 339 N PHE A 144
SHEET 1 E 8 ARG A 183 TYR A 187 0
SHEET 2 E 8 THR A 176 PHE A 180 -1 N PHE A 180 O ARG A 183
SHEET 3 E 8 ALA A 503 SER A 506 1 O VAL A 505 N GLU A 177
SHEET 4 E 8 ALA A 511 PRO A 517 -1 O SER A 513 N VAL A 504
SHEET 5 E 8 TYR A 529 TRP A 538 -1 O SER A 531 N VAL A 516
SHEET 6 E 8 SER A 476 LYS A 484 -1 N ALA A 481 O LEU A 532
SHEET 7 E 8 PHE A 604 ASP A 607 -1 O PHE A 604 N PHE A 480
SHEET 8 E 8 GLN A 554 ASN A 555 -1 N ASN A 555 O VAL A 605
SHEET 1 F 3 GLU A 372 HIS A 379 0
SHEET 2 F 3 ALA A 387 ASP A 393 -1 O LEU A 390 N ALA A 375
SHEET 3 F 3 VAL A 398 TYR A 403 -1 O HIS A 399 N SER A 391
SHEET 1 G 2 ALA A 427 LEU A 432 0
SHEET 2 G 2 HIS A 442 VAL A 447 -1 O TYR A 444 N GLN A 430
SHEET 1 H 2 MET A 473 ALA A 474 0
SHEET 2 H 2 PHE A 617 LYS A 618 -1 O PHE A 617 N ALA A 474
SHEET 1 I 2 GLN A 495 TRP A 496 0
SHEET 2 I 2 GLU A 499 PRO A 500 -1 O GLU A 499 N TRP A 496
SHEET 1 J 2 TYR A 577 VAL A 578 0
SHEET 2 J 2 GLN A 587 PRO A 588 -1 O GLN A 587 N VAL A 578
SHEET 1 K 5 LEU B 365 ARG B 370 0
SHEET 2 K 5 GLY B 87 TYR B 93 1 N VAL B 90 O VAL B 366
SHEET 3 K 5 ASN B 56 VAL B 62 1 N ILE B 59 O ASP B 89
SHEET 4 K 5 PHE B 405 LEU B 408 1 O ILE B 407 N ALA B 60
SHEET 5 K 5 PHE B 647 ILE B 649 1 O PHE B 648 N LEU B 408
SHEET 1 L 3 ILE B 110 LYS B 111 0
SHEET 2 L 3 VAL B 120 VAL B 125 -1 O LEU B 124 N LYS B 111
SHEET 3 L 3 LYS B 116 ALA B 117 -1 N ALA B 117 O VAL B 120
SHEET 1 M 3 ILE B 110 LYS B 111 0
SHEET 2 M 3 VAL B 120 VAL B 125 -1 O LEU B 124 N LYS B 111
SHEET 3 M 3 THR B 135 GLU B 138 -1 O TYR B 137 N ALA B 123
SHEET 1 N 2 PHE B 144 PRO B 145 0
SHEET 2 N 2 GLU B 338 TYR B 339 -1 O TYR B 339 N PHE B 144
SHEET 1 O 8 ARG B 183 TYR B 187 0
SHEET 2 O 8 THR B 176 PHE B 180 -1 N PHE B 178 O ASP B 185
SHEET 3 O 8 ALA B 503 SER B 506 1 O VAL B 505 N GLU B 177
SHEET 4 O 8 ALA B 511 PRO B 517 -1 O SER B 513 N VAL B 504
SHEET 5 O 8 TYR B 529 TRP B 538 -1 O SER B 531 N VAL B 516
SHEET 6 O 8 SER B 476 LYS B 484 -1 N ALA B 481 O LEU B 532
SHEET 7 O 8 PHE B 604 ASP B 607 -1 O PHE B 604 N PHE B 480
SHEET 8 O 8 GLN B 554 ASN B 555 -1 N ASN B 555 O VAL B 605
SHEET 1 P 3 ARG B 373 HIS B 379 0
SHEET 2 P 3 ALA B 387 TYR B 392 -1 O LEU B 390 N ALA B 375
SHEET 3 P 3 VAL B 398 TYR B 403 -1 O HIS B 399 N SER B 391
SHEET 1 Q 2 ALA B 427 LEU B 432 0
SHEET 2 Q 2 HIS B 442 VAL B 447 -1 O TYR B 444 N GLN B 430
SHEET 1 R 2 MET B 473 ALA B 474 0
SHEET 2 R 2 PHE B 617 LYS B 618 -1 O PHE B 617 N ALA B 474
SHEET 1 S 2 GLN B 495 TRP B 496 0
SHEET 2 S 2 GLU B 499 PRO B 500 -1 O GLU B 499 N TRP B 496
SHEET 1 T 2 TYR B 577 VAL B 578 0
SHEET 2 T 2 GLN B 587 PRO B 588 -1 O GLN B 587 N VAL B 578
CISPEP 1 TYR A 552 PRO A 553 0 2.61
CISPEP 2 ASN A 555 PRO A 556 0 2.90
CISPEP 3 VAL A 704 PRO A 705 0 -5.53
CISPEP 4 TYR B 552 PRO B 553 0 4.30
CISPEP 5 ASN B 555 PRO B 556 0 3.24
SITE 1 AC1 8 ARG A 475 THR A 543 ARG A 546 ARG B 475
SITE 2 AC1 8 THR B 543 ARG B 546 THR B 609 HOH B7205
SITE 1 AC2 9 ARG A 599 THR A 600 HOH A5266 HOH A7275
SITE 2 AC2 9 ASN B 56 HOH B5352 HOH B5735 HOH B5927
SITE 3 AC2 9 HOH B6144
SITE 1 AC3 41 GLY A 63 GLY A 65 ALA A 66 GLY A 67
SITE 2 AC3 41 TYR A 93 GLU A 94 ALA A 95 ASP A 96
SITE 3 AC3 41 GLY A 118 ARG A 119 VAL A 120 GLY A 140
SITE 4 AC3 41 ALA A 141 MET A 142 ARG A 143 PHE A 144
SITE 5 AC3 41 GLU A 372 ARG A 373 VAL A 374 ALA A 409
SITE 6 AC3 41 VAL A 410 PRO A 411 GLN A 414 ILE A 418
SITE 7 AC3 41 SER A 476 TYR A 536 TRP A 608 GLY A 616
SITE 8 AC3 41 SER A 651 ASP A 652 GLY A 659 TRP A 660
SITE 9 AC3 41 LEU A 661 GOL A 902 PHE A 904 HOH A5001
SITE 10 AC3 41 HOH A5025 HOH A5034 HOH A5037 HOH A5091
SITE 11 AC3 41 HOH A5149
SITE 1 AC4 9 ARG A 143 LEU A 319 TYR A 536 TRP A 538
SITE 2 AC4 9 PHE A 617 GLY A 659 TRP A 660 FAD A 801
SITE 3 AC4 9 HOH A5170
SITE 1 AC5 8 GLN A 414 LYS A 612 FAD A 801 HOH A5120
SITE 2 AC5 8 HOH A5319 HOH A5402 HOH A5580 HOH A5959
SITE 1 AC6 41 GLY B 63 GLY B 65 ALA B 66 GLY B 67
SITE 2 AC6 41 TYR B 93 GLU B 94 ALA B 95 ASP B 96
SITE 3 AC6 41 GLY B 118 ARG B 119 VAL B 120 GLY B 140
SITE 4 AC6 41 ALA B 141 MET B 142 ARG B 143 PHE B 144
SITE 5 AC6 41 GLU B 372 ARG B 373 VAL B 374 ALA B 409
SITE 6 AC6 41 VAL B 410 PRO B 411 GLN B 414 ILE B 418
SITE 7 AC6 41 SER B 476 TYR B 536 TRP B 608 GLY B 616
SITE 8 AC6 41 SER B 651 ASP B 652 GLY B 659 TRP B 660
SITE 9 AC6 41 LEU B 661 GOL B1902 PHE B1904 HOH B5008
SITE 10 AC6 41 HOH B5031 HOH B5065 HOH B5068 HOH B5099
SITE 11 AC6 41 HOH B5151
SITE 1 AC7 9 ARG B 143 LEU B 319 TYR B 536 TRP B 538
SITE 2 AC7 9 PHE B 617 GLY B 659 TRP B 660 FAD B 801
SITE 3 AC7 9 HOH B5132
SITE 1 AC8 7 GLN B 414 LYS B 612 FAD B 801 HOH B5088
SITE 2 AC8 7 HOH B5295 HOH B5317 HOH B5705
CRYST1 100.985 112.941 136.458 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009902 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008854 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007328 0.00000
(ATOM LINES ARE NOT SHOWN.)
END