HEADER LYASE 21-JAN-09 3FY4
TITLE (6-4) PHOTOLYASE CRYSTAL STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-4 PHOTOLYASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: MOUSE-EAR CRESS,THALE-CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: 6-4 PHOTOLYASE, UVR3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM 109;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKK223
KEYWDS (6-4) PHOTOLYASE, DNA REPAIR, CLOCK CRYPTOCHROME, LYASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.HITOMI,A.S.ARVAI,J.A.TAINER,E.D.GETZOFF
REVDAT 3 21-FEB-24 3FY4 1 REMARK
REVDAT 2 19-MAY-09 3FY4 1 JRNL
REVDAT 1 28-APR-09 3FY4 0
JRNL AUTH K.HITOMI,L.DITACCHIO,A.S.ARVAI,J.YAMAMOTO,S.T.KIM,T.TODO,
JRNL AUTH 2 J.A.TAINER,S.IWAI,S.PANDA,E.D.GETZOFF
JRNL TITL FUNCTIONAL MOTIFS IN THE (6-4) PHOTOLYASE CRYSTAL STRUCTURE
JRNL TITL 2 MAKE A COMPARATIVE FRAMEWORK FOR DNA REPAIR PHOTOLYASES AND
JRNL TITL 3 CLOCK CRYPTOCHROMES.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 6962 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19359474
JRNL DOI 10.1073/PNAS.0809180106
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.2
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) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 74928.000
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 59584
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) : 0.202
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3016
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.004
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) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 88.40
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 8564
REMARK 3 BIN R VALUE (WORKING SET) : 0.3040
REMARK 3 BIN FREE R VALUE : 0.3670
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 477
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.017
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12553
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 260
REMARK 3 SOLVENT ATOMS : 678
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 35.80
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 39.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.97000
REMARK 3 B22 (A**2) : -0.22000
REMARK 3 B33 (A**2) : 3.19000
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) : 0.30
REMARK 3 ESD FROM SIGMAA (A) : 0.36
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) : 0.37
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.47
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.300
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.10
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.850
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) : 1.240 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.120 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.790 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.750 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 56.13
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 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : FAD.PAR
REMARK 3 PARAMETER FILE 5 : XXX.PAR
REMARK 3 PARAMETER FILE 6 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : ION.TOP
REMARK 3 TOPOLOGY FILE 4 : FAD.TOP
REMARK 3 TOPOLOGY FILE 5 : XXX.TOP
REMARK 3 TOPOLOGY FILE 6 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED
REMARK 4
REMARK 4 3FY4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-FEB-09.
REMARK 100 THE DEPOSITION ID IS D_1000051183.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-NOV-02
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0688
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59584
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 60.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
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) : 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: NULL
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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 56.22350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 71.55900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 69.51650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 71.55900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 56.22350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 69.51650
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, 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 THR A 3
REMARK 465 GLU A 526
REMARK 465 SER A 527
REMARK 465 LYS A 528
REMARK 465 ILE A 529
REMARK 465 ARG A 530
REMARK 465 ASN A 531
REMARK 465 GLN A 532
REMARK 465 ARG A 533
REMARK 465 PRO A 534
REMARK 465 LYS A 535
REMARK 465 LEU A 536
REMARK 465 LYS A 537
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 THR B 3
REMARK 465 PHE B 51
REMARK 465 HIS B 148
REMARK 465 SER B 527
REMARK 465 LYS B 528
REMARK 465 ILE B 529
REMARK 465 ARG B 530
REMARK 465 ASN B 531
REMARK 465 GLN B 532
REMARK 465 ARG B 533
REMARK 465 PRO B 534
REMARK 465 LYS B 535
REMARK 465 LEU B 536
REMARK 465 LYS B 537
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 THR C 3
REMARK 465 GLY C 4
REMARK 465 GLU C 525
REMARK 465 GLU C 526
REMARK 465 SER C 527
REMARK 465 LYS C 528
REMARK 465 ILE C 529
REMARK 465 ARG C 530
REMARK 465 ASN C 531
REMARK 465 GLN C 532
REMARK 465 ARG C 533
REMARK 465 PRO C 534
REMARK 465 LYS C 535
REMARK 465 LEU C 536
REMARK 465 LYS C 537
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 513 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 517 CD NE CZ NH1 NH2
REMARK 470 GLN A 520 CD OE1 NE2
REMARK 470 LYS A 521 CG CD CE NZ
REMARK 470 GLU A 523 CG CD OE1 OE2
REMARK 470 HIS A 524 CG ND1 CD2 CE1 NE2
REMARK 470 ARG B 513 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 517 CD NE CZ NH1 NH2
REMARK 470 GLN B 520 CD OE1 NE2
REMARK 470 LYS B 521 CG CD CE NZ
REMARK 470 GLU B 523 CG CD OE1 OE2
REMARK 470 HIS B 524 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 526 CG CD OE1 OE2
REMARK 470 ARG C 513 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 517 CD NE CZ NH1 NH2
REMARK 470 GLN C 520 CD OE1 NE2
REMARK 470 LYS C 521 CG CD CE NZ
REMARK 470 GLU C 523 CG CD OE1 OE2
REMARK 470 HIS C 524 CG ND1 CD2 CE1 NE2
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 B 3433 O HOH B 3620 1.83
REMARK 500 O HOH A 3062 O HOH A 3375 1.89
REMARK 500 O HOH A 3400 O HOH A 3612 1.90
REMARK 500 O HOH A 3171 O HOH A 3237 1.93
REMARK 500 O HOH C 3170 O HOH C 3177 1.93
REMARK 500 O HOH A 3225 O HOH A 3374 1.95
REMARK 500 O HOH B 3208 O HOH B 3331 1.96
REMARK 500 O HOH C 3521 O HOH C 3636 1.96
REMARK 500 O HOH C 3349 O HOH C 3370 1.97
REMARK 500 O HOH B 3441 O HOH B 3659 1.98
REMARK 500 O HOH A 3168 O HOH C 3119 2.02
REMARK 500 O HOH C 3286 O HOH C 3298 2.02
REMARK 500 O HOH C 3338 O HOH C 3382 2.03
REMARK 500 O HOH A 3423 O HOH A 3616 2.04
REMARK 500 O HOH A 3281 O HOH A 3558 2.05
REMARK 500 O HOH A 3023 O HOH A 3102 2.06
REMARK 500 O HOH A 3361 O HOH A 3390 2.07
REMARK 500 O HOH A 3494 O HOH A 3526 2.08
REMARK 500 O HOH A 3644 O HOH A 3651 2.09
REMARK 500 O HOH B 3166 O HOH B 3500 2.09
REMARK 500 OG1 THR A 113 O HOH A 3245 2.10
REMARK 500 O HOH A 3287 O HOH A 3363 2.12
REMARK 500 O HOH A 3400 O HOH A 3511 2.12
REMARK 500 OG1 THR A 113 O HOH A 3180 2.16
REMARK 500 O HOH A 3355 O HOH A 3381 2.16
REMARK 500 O HOH A 3247 O HOH A 3593 2.16
REMARK 500 O HOH B 3289 O HOH B 3596 2.19
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 12 -67.06 -134.27
REMARK 500 LEU A 15 66.09 -63.55
REMARK 500 ASP A 19 58.85 34.83
REMARK 500 PRO A 53 133.85 -37.46
REMARK 500 SER A 82 -154.31 -101.77
REMARK 500 ASN A 153 14.41 -68.35
REMARK 500 CYS A 173 -8.98 -58.74
REMARK 500 ALA A 174 -74.17 -51.18
REMARK 500 ASP A 190 118.28 -31.89
REMARK 500 VAL A 285 -90.95 -103.44
REMARK 500 LYS A 286 -51.30 153.40
REMARK 500 ASP A 332 83.13 -172.76
REMARK 500 THR A 375 -109.13 -100.41
REMARK 500 ASP A 378 -59.96 -138.03
REMARK 500 PHE A 414 -47.30 73.33
REMARK 500 GLU A 455 63.89 -154.62
REMARK 500 LYS A 473 -63.85 -123.25
REMARK 500 ASP A 504 67.17 39.47
REMARK 500 GLU A 510 -71.63 -69.95
REMARK 500 HIS A 524 -26.85 -145.97
REMARK 500 ARG B 12 -64.86 -135.51
REMARK 500 LYS B 13 -163.85 -116.19
REMARK 500 SER B 82 -156.21 -132.63
REMARK 500 SER B 172 54.23 -62.28
REMARK 500 CYS B 173 -2.51 -155.93
REMARK 500 SER B 176 148.88 -31.47
REMARK 500 PRO B 187 -178.31 -66.80
REMARK 500 ILE B 196 119.59 -31.98
REMARK 500 PRO B 255 140.10 -39.05
REMARK 500 LYS B 286 -89.50 -64.72
REMARK 500 ASP B 316 33.85 -95.82
REMARK 500 ASP B 332 91.10 -168.98
REMARK 500 THR B 375 -101.24 -102.14
REMARK 500 ASP B 378 -56.75 -141.65
REMARK 500 PHE B 414 -65.89 77.93
REMARK 500 LYS B 450 -62.81 -26.46
REMARK 500 GLN B 451 -37.47 -30.16
REMARK 500 GLU B 455 63.18 -166.08
REMARK 500 CYS B 469 84.52 -161.78
REMARK 500 LYS B 473 -76.01 -131.88
REMARK 500 MET B 503 21.27 -65.43
REMARK 500 LYS B 506 27.90 -77.79
REMARK 500 ASP B 508 -168.31 -103.86
REMARK 500 GLU B 525 -79.59 -109.77
REMARK 500 ARG C 12 -60.64 -143.64
REMARK 500 ASP C 19 53.79 36.75
REMARK 500 ASN C 20 79.73 -117.67
REMARK 500 PRO C 53 129.62 -37.36
REMARK 500 SER C 82 -162.94 -126.92
REMARK 500 SER C 140 12.96 -145.21
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
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 IMD A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 920
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 930
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD C 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD C 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES C 920
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 930
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 900
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 905
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD B 906
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 920
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 930
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 900
DBREF 3FY4 A 1 537 UNP O48652 O48652_ARATH 1 537
DBREF 3FY4 B 1 537 UNP O48652 O48652_ARATH 1 537
DBREF 3FY4 C 1 537 UNP O48652 O48652_ARATH 1 537
SEQRES 1 A 537 MET ALA THR GLY SER GLY SER LEU ILE TRP PHE ARG LYS
SEQRES 2 A 537 GLY LEU ARG VAL HIS ASP ASN PRO ALA LEU GLU TYR ALA
SEQRES 3 A 537 SER LYS GLY SER GLU PHE MET TYR PRO VAL PHE VAL ILE
SEQRES 4 A 537 ASP PRO HIS TYR MET GLU SER ASP PRO SER ALA PHE SER
SEQRES 5 A 537 PRO GLY SER SER ARG ALA GLY VAL ASN ARG ILE ARG PHE
SEQRES 6 A 537 LEU LEU GLU SER LEU LYS ASP LEU ASP SER SER LEU LYS
SEQRES 7 A 537 LYS LEU GLY SER ARG LEU LEU VAL PHE LYS GLY GLU PRO
SEQRES 8 A 537 GLY GLU VAL LEU VAL ARG CYS LEU GLN GLU TRP LYS VAL
SEQRES 9 A 537 LYS ARG LEU CYS PHE GLU TYR ASP THR ASP PRO TYR TYR
SEQRES 10 A 537 GLN ALA LEU ASP VAL LYS VAL LYS ASP TYR ALA SER SER
SEQRES 11 A 537 THR GLY VAL GLU VAL PHE SER PRO VAL SER HIS THR LEU
SEQRES 12 A 537 PHE ASN PRO ALA HIS ILE ILE GLU LYS ASN GLY GLY LYS
SEQRES 13 A 537 PRO PRO LEU SER TYR GLN SER PHE LEU LYS VAL ALA GLY
SEQRES 14 A 537 GLU PRO SER CYS ALA LYS SER GLU LEU VAL MET SER TYR
SEQRES 15 A 537 SER SER LEU PRO PRO ILE GLY ASP ILE GLY ASN LEU GLY
SEQRES 16 A 537 ILE SER GLU VAL PRO SER LEU GLU GLU LEU GLY TYR LYS
SEQRES 17 A 537 ASP ASP GLU GLN ALA ASP TRP THR PRO PHE ARG GLY GLY
SEQRES 18 A 537 GLU SER GLU ALA LEU LYS ARG LEU THR LYS SER ILE SER
SEQRES 19 A 537 ASP LYS ALA TRP VAL ALA ASN PHE GLU LYS PRO LYS GLY
SEQRES 20 A 537 ASP PRO SER ALA PHE LEU LYS PRO ALA THR THR VAL MET
SEQRES 21 A 537 SER PRO TYR LEU LYS PHE GLY CYS LEU SER SER ARG TYR
SEQRES 22 A 537 PHE TYR GLN CYS LEU GLN ASN ILE TYR LYS ASP VAL LYS
SEQRES 23 A 537 LYS HIS THR SER PRO PRO VAL SER LEU LEU GLY GLN LEU
SEQRES 24 A 537 LEU TRP ARG GLU PHE PHE TYR THR THR ALA PHE GLY THR
SEQRES 25 A 537 PRO ASN PHE ASP LYS MET LYS GLY ASN ARG ILE CYS LYS
SEQRES 26 A 537 GLN ILE PRO TRP ASN GLU ASP HIS ALA MET LEU ALA ALA
SEQRES 27 A 537 TRP ARG ASP GLY LYS THR GLY TYR PRO TRP ILE ASP ALA
SEQRES 28 A 537 ILE MET VAL GLN LEU LEU LYS TRP GLY TRP MET HIS HIS
SEQRES 29 A 537 LEU ALA ARG HIS CYS VAL ALA CYS PHE LEU THR ARG GLY
SEQRES 30 A 537 ASP LEU PHE ILE HIS TRP GLU GLN GLY ARG ASP VAL PHE
SEQRES 31 A 537 GLU ARG LEU LEU ILE ASP SER ASP TRP ALA ILE ASN ASN
SEQRES 32 A 537 GLY ASN TRP MET TRP LEU SER CYS SER SER PHE PHE TYR
SEQRES 33 A 537 GLN PHE ASN ARG ILE TYR SER PRO ILE SER PHE GLY LYS
SEQRES 34 A 537 LYS TYR ASP PRO ASP GLY LYS TYR ILE ARG HIS PHE LEU
SEQRES 35 A 537 PRO VAL LEU LYS ASP MET PRO LYS GLN TYR ILE TYR GLU
SEQRES 36 A 537 PRO TRP THR ALA PRO LEU SER VAL GLN THR LYS ALA ASN
SEQRES 37 A 537 CYS ILE VAL GLY LYS ASP TYR PRO LYS PRO MET VAL LEU
SEQRES 38 A 537 HIS ASP SER ALA SER LYS GLU CYS LYS ARG LYS MET GLY
SEQRES 39 A 537 GLU ALA TYR ALA LEU ASN LYS LYS MET ASP GLY LYS VAL
SEQRES 40 A 537 ASP GLU GLU ASN LEU ARG ASP LEU ARG ARG LYS LEU GLN
SEQRES 41 A 537 LYS ASP GLU HIS GLU GLU SER LYS ILE ARG ASN GLN ARG
SEQRES 42 A 537 PRO LYS LEU LYS
SEQRES 1 B 537 MET ALA THR GLY SER GLY SER LEU ILE TRP PHE ARG LYS
SEQRES 2 B 537 GLY LEU ARG VAL HIS ASP ASN PRO ALA LEU GLU TYR ALA
SEQRES 3 B 537 SER LYS GLY SER GLU PHE MET TYR PRO VAL PHE VAL ILE
SEQRES 4 B 537 ASP PRO HIS TYR MET GLU SER ASP PRO SER ALA PHE SER
SEQRES 5 B 537 PRO GLY SER SER ARG ALA GLY VAL ASN ARG ILE ARG PHE
SEQRES 6 B 537 LEU LEU GLU SER LEU LYS ASP LEU ASP SER SER LEU LYS
SEQRES 7 B 537 LYS LEU GLY SER ARG LEU LEU VAL PHE LYS GLY GLU PRO
SEQRES 8 B 537 GLY GLU VAL LEU VAL ARG CYS LEU GLN GLU TRP LYS VAL
SEQRES 9 B 537 LYS ARG LEU CYS PHE GLU TYR ASP THR ASP PRO TYR TYR
SEQRES 10 B 537 GLN ALA LEU ASP VAL LYS VAL LYS ASP TYR ALA SER SER
SEQRES 11 B 537 THR GLY VAL GLU VAL PHE SER PRO VAL SER HIS THR LEU
SEQRES 12 B 537 PHE ASN PRO ALA HIS ILE ILE GLU LYS ASN GLY GLY LYS
SEQRES 13 B 537 PRO PRO LEU SER TYR GLN SER PHE LEU LYS VAL ALA GLY
SEQRES 14 B 537 GLU PRO SER CYS ALA LYS SER GLU LEU VAL MET SER TYR
SEQRES 15 B 537 SER SER LEU PRO PRO ILE GLY ASP ILE GLY ASN LEU GLY
SEQRES 16 B 537 ILE SER GLU VAL PRO SER LEU GLU GLU LEU GLY TYR LYS
SEQRES 17 B 537 ASP ASP GLU GLN ALA ASP TRP THR PRO PHE ARG GLY GLY
SEQRES 18 B 537 GLU SER GLU ALA LEU LYS ARG LEU THR LYS SER ILE SER
SEQRES 19 B 537 ASP LYS ALA TRP VAL ALA ASN PHE GLU LYS PRO LYS GLY
SEQRES 20 B 537 ASP PRO SER ALA PHE LEU LYS PRO ALA THR THR VAL MET
SEQRES 21 B 537 SER PRO TYR LEU LYS PHE GLY CYS LEU SER SER ARG TYR
SEQRES 22 B 537 PHE TYR GLN CYS LEU GLN ASN ILE TYR LYS ASP VAL LYS
SEQRES 23 B 537 LYS HIS THR SER PRO PRO VAL SER LEU LEU GLY GLN LEU
SEQRES 24 B 537 LEU TRP ARG GLU PHE PHE TYR THR THR ALA PHE GLY THR
SEQRES 25 B 537 PRO ASN PHE ASP LYS MET LYS GLY ASN ARG ILE CYS LYS
SEQRES 26 B 537 GLN ILE PRO TRP ASN GLU ASP HIS ALA MET LEU ALA ALA
SEQRES 27 B 537 TRP ARG ASP GLY LYS THR GLY TYR PRO TRP ILE ASP ALA
SEQRES 28 B 537 ILE MET VAL GLN LEU LEU LYS TRP GLY TRP MET HIS HIS
SEQRES 29 B 537 LEU ALA ARG HIS CYS VAL ALA CYS PHE LEU THR ARG GLY
SEQRES 30 B 537 ASP LEU PHE ILE HIS TRP GLU GLN GLY ARG ASP VAL PHE
SEQRES 31 B 537 GLU ARG LEU LEU ILE ASP SER ASP TRP ALA ILE ASN ASN
SEQRES 32 B 537 GLY ASN TRP MET TRP LEU SER CYS SER SER PHE PHE TYR
SEQRES 33 B 537 GLN PHE ASN ARG ILE TYR SER PRO ILE SER PHE GLY LYS
SEQRES 34 B 537 LYS TYR ASP PRO ASP GLY LYS TYR ILE ARG HIS PHE LEU
SEQRES 35 B 537 PRO VAL LEU LYS ASP MET PRO LYS GLN TYR ILE TYR GLU
SEQRES 36 B 537 PRO TRP THR ALA PRO LEU SER VAL GLN THR LYS ALA ASN
SEQRES 37 B 537 CYS ILE VAL GLY LYS ASP TYR PRO LYS PRO MET VAL LEU
SEQRES 38 B 537 HIS ASP SER ALA SER LYS GLU CYS LYS ARG LYS MET GLY
SEQRES 39 B 537 GLU ALA TYR ALA LEU ASN LYS LYS MET ASP GLY LYS VAL
SEQRES 40 B 537 ASP GLU GLU ASN LEU ARG ASP LEU ARG ARG LYS LEU GLN
SEQRES 41 B 537 LYS ASP GLU HIS GLU GLU SER LYS ILE ARG ASN GLN ARG
SEQRES 42 B 537 PRO LYS LEU LYS
SEQRES 1 C 537 MET ALA THR GLY SER GLY SER LEU ILE TRP PHE ARG LYS
SEQRES 2 C 537 GLY LEU ARG VAL HIS ASP ASN PRO ALA LEU GLU TYR ALA
SEQRES 3 C 537 SER LYS GLY SER GLU PHE MET TYR PRO VAL PHE VAL ILE
SEQRES 4 C 537 ASP PRO HIS TYR MET GLU SER ASP PRO SER ALA PHE SER
SEQRES 5 C 537 PRO GLY SER SER ARG ALA GLY VAL ASN ARG ILE ARG PHE
SEQRES 6 C 537 LEU LEU GLU SER LEU LYS ASP LEU ASP SER SER LEU LYS
SEQRES 7 C 537 LYS LEU GLY SER ARG LEU LEU VAL PHE LYS GLY GLU PRO
SEQRES 8 C 537 GLY GLU VAL LEU VAL ARG CYS LEU GLN GLU TRP LYS VAL
SEQRES 9 C 537 LYS ARG LEU CYS PHE GLU TYR ASP THR ASP PRO TYR TYR
SEQRES 10 C 537 GLN ALA LEU ASP VAL LYS VAL LYS ASP TYR ALA SER SER
SEQRES 11 C 537 THR GLY VAL GLU VAL PHE SER PRO VAL SER HIS THR LEU
SEQRES 12 C 537 PHE ASN PRO ALA HIS ILE ILE GLU LYS ASN GLY GLY LYS
SEQRES 13 C 537 PRO PRO LEU SER TYR GLN SER PHE LEU LYS VAL ALA GLY
SEQRES 14 C 537 GLU PRO SER CYS ALA LYS SER GLU LEU VAL MET SER TYR
SEQRES 15 C 537 SER SER LEU PRO PRO ILE GLY ASP ILE GLY ASN LEU GLY
SEQRES 16 C 537 ILE SER GLU VAL PRO SER LEU GLU GLU LEU GLY TYR LYS
SEQRES 17 C 537 ASP ASP GLU GLN ALA ASP TRP THR PRO PHE ARG GLY GLY
SEQRES 18 C 537 GLU SER GLU ALA LEU LYS ARG LEU THR LYS SER ILE SER
SEQRES 19 C 537 ASP LYS ALA TRP VAL ALA ASN PHE GLU LYS PRO LYS GLY
SEQRES 20 C 537 ASP PRO SER ALA PHE LEU LYS PRO ALA THR THR VAL MET
SEQRES 21 C 537 SER PRO TYR LEU LYS PHE GLY CYS LEU SER SER ARG TYR
SEQRES 22 C 537 PHE TYR GLN CYS LEU GLN ASN ILE TYR LYS ASP VAL LYS
SEQRES 23 C 537 LYS HIS THR SER PRO PRO VAL SER LEU LEU GLY GLN LEU
SEQRES 24 C 537 LEU TRP ARG GLU PHE PHE TYR THR THR ALA PHE GLY THR
SEQRES 25 C 537 PRO ASN PHE ASP LYS MET LYS GLY ASN ARG ILE CYS LYS
SEQRES 26 C 537 GLN ILE PRO TRP ASN GLU ASP HIS ALA MET LEU ALA ALA
SEQRES 27 C 537 TRP ARG ASP GLY LYS THR GLY TYR PRO TRP ILE ASP ALA
SEQRES 28 C 537 ILE MET VAL GLN LEU LEU LYS TRP GLY TRP MET HIS HIS
SEQRES 29 C 537 LEU ALA ARG HIS CYS VAL ALA CYS PHE LEU THR ARG GLY
SEQRES 30 C 537 ASP LEU PHE ILE HIS TRP GLU GLN GLY ARG ASP VAL PHE
SEQRES 31 C 537 GLU ARG LEU LEU ILE ASP SER ASP TRP ALA ILE ASN ASN
SEQRES 32 C 537 GLY ASN TRP MET TRP LEU SER CYS SER SER PHE PHE TYR
SEQRES 33 C 537 GLN PHE ASN ARG ILE TYR SER PRO ILE SER PHE GLY LYS
SEQRES 34 C 537 LYS TYR ASP PRO ASP GLY LYS TYR ILE ARG HIS PHE LEU
SEQRES 35 C 537 PRO VAL LEU LYS ASP MET PRO LYS GLN TYR ILE TYR GLU
SEQRES 36 C 537 PRO TRP THR ALA PRO LEU SER VAL GLN THR LYS ALA ASN
SEQRES 37 C 537 CYS ILE VAL GLY LYS ASP TYR PRO LYS PRO MET VAL LEU
SEQRES 38 C 537 HIS ASP SER ALA SER LYS GLU CYS LYS ARG LYS MET GLY
SEQRES 39 C 537 GLU ALA TYR ALA LEU ASN LYS LYS MET ASP GLY LYS VAL
SEQRES 40 C 537 ASP GLU GLU ASN LEU ARG ASP LEU ARG ARG LYS LEU GLN
SEQRES 41 C 537 LYS ASP GLU HIS GLU GLU SER LYS ILE ARG ASN GLN ARG
SEQRES 42 C 537 PRO LYS LEU LYS
HET IMD A 901 5
HET IMD A 902 5
HET IMD A 905 5
HET MES A 920 12
HET PO4 A 930 5
HET FAD A 900 53
HET IMD B 901 5
HET IMD B 903 5
HET IMD B 904 5
HET IMD B 905 5
HET IMD B 906 5
HET MES B 920 12
HET PO4 B 930 5
HET FAD B 900 53
HET IMD C 901 5
HET IMD C 902 5
HET MES C 920 12
HET PO4 C 930 5
HET FAD C 900 53
HETNAM IMD IMIDAZOLE
HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID
HETNAM PO4 PHOSPHATE ION
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 4 IMD 10(C3 H5 N2 1+)
FORMUL 7 MES 3(C6 H13 N O4 S)
FORMUL 8 PO4 3(O4 P 3-)
FORMUL 9 FAD 3(C27 H33 N9 O15 P2)
FORMUL 23 HOH *678(H2 O)
HELIX 1 1 ASN A 20 LYS A 28 1 9
HELIX 2 2 ASP A 40 GLU A 45 1 6
HELIX 3 3 GLY A 59 LEU A 80 1 22
HELIX 4 4 GLU A 90 GLN A 100 1 11
HELIX 5 5 ASP A 114 THR A 131 1 18
HELIX 6 6 ASN A 145 ASN A 153 1 9
HELIX 7 7 SER A 160 GLY A 169 1 10
HELIX 8 8 LYS A 208 GLN A 212 5 5
HELIX 9 9 GLY A 221 ILE A 233 1 13
HELIX 10 10 ASP A 235 ASN A 241 1 7
HELIX 11 11 GLU A 243 GLY A 247 5 5
HELIX 12 12 MET A 260 PHE A 266 1 7
HELIX 13 13 SER A 270 ASP A 284 1 15
HELIX 14 14 SER A 294 GLY A 311 1 18
HELIX 15 15 ASP A 332 ASP A 341 1 10
HELIX 16 16 TYR A 346 GLY A 360 1 15
HELIX 17 17 HIS A 363 THR A 375 1 13
HELIX 18 18 HIS A 382 LEU A 394 1 13
HELIX 19 19 ASP A 398 SER A 410 1 13
HELIX 20 20 PHE A 427 TYR A 431 5 5
HELIX 21 21 GLY A 435 LEU A 442 1 8
HELIX 22 22 PRO A 443 LYS A 446 5 4
HELIX 23 23 GLU A 455 ALA A 459 5 5
HELIX 24 24 PRO A 460 ASN A 468 1 9
HELIX 25 25 LEU A 481 MET A 503 1 23
HELIX 26 26 ASP A 508 GLU A 523 1 16
HELIX 27 27 ASN B 20 LYS B 28 1 9
HELIX 28 28 ASP B 40 GLU B 45 1 6
HELIX 29 29 GLY B 59 LEU B 80 1 22
HELIX 30 30 GLU B 90 TRP B 102 1 13
HELIX 31 31 ASP B 114 THR B 131 1 18
HELIX 32 32 PRO B 146 ALA B 147 5 2
HELIX 33 33 ILE B 149 GLU B 151 5 3
HELIX 34 34 SER B 160 GLY B 169 1 10
HELIX 35 35 ASP B 209 ALA B 213 5 5
HELIX 36 36 GLY B 221 ILE B 233 1 13
HELIX 37 37 ASP B 235 ASN B 241 1 7
HELIX 38 38 GLU B 243 GLY B 247 5 5
HELIX 39 39 MET B 260 PHE B 266 1 7
HELIX 40 40 SER B 270 ASP B 284 1 15
HELIX 41 41 SER B 294 GLY B 311 1 18
HELIX 42 42 ASP B 332 ASP B 341 1 10
HELIX 43 43 TYR B 346 GLY B 360 1 15
HELIX 44 44 HIS B 363 THR B 375 1 13
HELIX 45 45 HIS B 382 LEU B 394 1 13
HELIX 46 46 ASP B 398 SER B 410 1 13
HELIX 47 47 SER B 426 ASP B 432 1 7
HELIX 48 48 GLY B 435 LEU B 442 1 8
HELIX 49 49 PRO B 443 LYS B 446 5 4
HELIX 50 50 PRO B 449 TYR B 454 1 6
HELIX 51 51 GLU B 455 ALA B 459 5 5
HELIX 52 52 PRO B 460 ASN B 468 1 9
HELIX 53 53 LEU B 481 MET B 503 1 23
HELIX 54 54 ASP B 508 HIS B 524 1 17
HELIX 55 55 ASN C 20 LYS C 28 1 9
HELIX 56 56 ASP C 40 GLU C 45 1 6
HELIX 57 57 GLY C 59 LEU C 80 1 22
HELIX 58 58 GLU C 90 LYS C 103 1 14
HELIX 59 59 ASP C 114 THR C 131 1 18
HELIX 60 60 ASN C 145 LYS C 152 1 8
HELIX 61 61 SER C 160 GLY C 169 1 10
HELIX 62 62 LYS C 208 GLN C 212 5 5
HELIX 63 63 GLY C 221 ILE C 233 1 13
HELIX 64 64 ASP C 235 PHE C 242 1 8
HELIX 65 65 GLU C 243 GLY C 247 5 5
HELIX 66 66 MET C 260 PHE C 266 1 7
HELIX 67 67 SER C 270 ASP C 284 1 15
HELIX 68 68 SER C 294 GLY C 311 1 18
HELIX 69 69 ASP C 332 ASP C 341 1 10
HELIX 70 70 TYR C 346 TRP C 359 1 14
HELIX 71 71 HIS C 363 THR C 375 1 13
HELIX 72 72 HIS C 382 LEU C 394 1 13
HELIX 73 73 ASP C 398 SER C 410 1 13
HELIX 74 74 PHE C 427 TYR C 431 5 5
HELIX 75 75 GLY C 435 LEU C 442 1 8
HELIX 76 76 PRO C 443 LYS C 446 5 4
HELIX 77 77 PRO C 449 TYR C 454 1 6
HELIX 78 78 GLU C 455 ALA C 459 5 5
HELIX 79 79 PRO C 460 ASN C 468 1 9
HELIX 80 80 LEU C 481 MET C 503 1 23
HELIX 81 81 ASP C 508 HIS C 524 1 17
SHEET 1 A 5 LEU A 85 LYS A 88 0
SHEET 2 A 5 MET A 33 ILE A 39 1 N ILE A 39 O PHE A 87
SHEET 3 A 5 GLY A 6 PHE A 11 1 N PHE A 11 O VAL A 36
SHEET 4 A 5 VAL A 104 PHE A 109 1 O CYS A 108 N TRP A 10
SHEET 5 A 5 GLU A 134 PHE A 136 1 O GLU A 134 N LYS A 105
SHEET 1 B 5 LEU B 85 LYS B 88 0
SHEET 2 B 5 MET B 33 ILE B 39 1 N ILE B 39 O PHE B 87
SHEET 3 B 5 GLY B 6 PHE B 11 1 N PHE B 11 O VAL B 36
SHEET 4 B 5 VAL B 104 CYS B 108 1 O CYS B 108 N TRP B 10
SHEET 5 B 5 GLU B 134 PHE B 136 1 O GLU B 134 N LEU B 107
SHEET 1 C 5 LEU C 85 LYS C 88 0
SHEET 2 C 5 MET C 33 ILE C 39 1 N PRO C 35 O LEU C 85
SHEET 3 C 5 SER C 7 PHE C 11 1 N PHE C 11 O VAL C 36
SHEET 4 C 5 ARG C 106 PHE C 109 1 O CYS C 108 N TRP C 10
SHEET 5 C 5 GLU C 134 PHE C 136 1 O GLU C 134 N LEU C 107
CISPEP 1 PRO A 291 PRO A 292 0 0.17
CISPEP 2 PRO B 291 PRO B 292 0 0.18
CISPEP 3 PRO C 291 PRO C 292 0 0.13
SITE 1 AC1 4 TRP A 408 PHE A 415 TYR A 422 LYS B 208
SITE 1 AC2 4 ASN A 330 ASP A 378 LEU A 379 LYS A 492
SITE 1 AC3 3 PHE A 252 PRO A 255 TRP A 359
SITE 1 AC4 9 LYS A 244 PRO A 245 PRO A 292 VAL A 293
SITE 2 AC4 9 GLN A 298 TRP A 301 HIS A 364 HIS A 368
SITE 3 AC4 9 ASN A 405
SITE 1 AC5 2 PHE A 242 GLU A 243
SITE 1 AC6 27 LYS A 244 THR A 257 THR A 258 VAL A 259
SITE 2 AC6 27 MET A 260 SER A 261 LEU A 264 GLN A 298
SITE 3 AC6 27 TRP A 301 ARG A 302 PHE A 305 TRP A 361
SITE 4 AC6 27 HIS A 364 ARG A 367 HIS A 368 PHE A 390
SITE 5 AC6 27 LEU A 394 ASP A 396 SER A 397 ASP A 398
SITE 6 AC6 27 ILE A 401 ASN A 402 ASN A 405 TRP A 406
SITE 7 AC6 27 LEU A 409 HOH A3199 HOH A3354
SITE 1 AC7 5 TRP C 408 PHE C 415 ARG C 420 TYR C 422
SITE 2 AC7 5 HOH C3357
SITE 1 AC8 4 ASN C 330 ASP C 378 ALA C 485 LYS C 492
SITE 1 AC9 10 LYS C 244 PRO C 245 PRO C 292 TRP C 301
SITE 2 AC9 10 HIS C 364 HIS C 368 ASN C 405 TRP C 408
SITE 3 AC9 10 FAD C 900 HOH C3135
SITE 1 BC1 5 TRP C 238 PHE C 242 GLU C 243 LYS C 246
SITE 2 BC1 5 HOH C3286
SITE 1 BC2 29 LYS C 244 THR C 257 THR C 258 VAL C 259
SITE 2 BC2 29 MET C 260 SER C 261 LEU C 264 GLN C 298
SITE 3 BC2 29 TRP C 301 ARG C 302 PHE C 305 TRP C 361
SITE 4 BC2 29 HIS C 364 ARG C 367 HIS C 368 PHE C 390
SITE 5 BC2 29 LEU C 394 ASP C 396 SER C 397 ASP C 398
SITE 6 BC2 29 ILE C 401 ASN C 402 ASN C 405 TRP C 406
SITE 7 BC2 29 LEU C 409 MES C 920 HOH C3013 HOH C3047
SITE 8 BC2 29 HOH C3136
SITE 1 BC3 5 TRP B 408 PHE B 415 ARG B 420 TYR B 422
SITE 2 BC3 5 LYS C 208
SITE 1 BC4 2 LYS B 325 TYR B 416
SITE 1 BC5 3 PHE B 252 PRO B 255 TRP B 359
SITE 1 BC6 5 LEU B 229 THR B 230 ILE B 233 TYR B 273
SITE 2 BC6 5 CYS B 277
SITE 1 BC7 8 LYS B 244 PRO B 245 PRO B 292 GLN B 298
SITE 2 BC7 8 TRP B 301 HIS B 364 HIS B 368 ASN B 405
SITE 1 BC8 2 TRP B 238 GLU B 243
SITE 1 BC9 28 LYS B 244 THR B 257 THR B 258 VAL B 259
SITE 2 BC9 28 MET B 260 SER B 261 LEU B 264 GLN B 298
SITE 3 BC9 28 TRP B 301 ARG B 302 PHE B 305 TRP B 361
SITE 4 BC9 28 MET B 362 HIS B 364 ARG B 367 HIS B 368
SITE 5 BC9 28 PHE B 390 LEU B 394 ASP B 396 SER B 397
SITE 6 BC9 28 ASP B 398 ILE B 401 ASN B 402 ASN B 405
SITE 7 BC9 28 TRP B 406 LEU B 409 HOH B3138 HOH B3153
CRYST1 112.447 139.033 143.118 90.00 90.00 90.00 P 21 21 21 12
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 0.008893 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007193 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006987 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
