HEADER OXIDOREDUCTASE 19-AUG-07 2R0G
TITLE CHROMOPYRROLIC ACID-SOAKED REBC WITH BOUND 7-CARBOXY-K252C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REBC;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: PUTATIVE MONOOXYGENASE, PUTATIVE FAD-MONOOXYGENASE;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: LECHEVALIERIA AEROCOLONIGENES;
SOURCE 3 ORGANISM_TAXID: 68170;
SOURCE 4 STRAIN: ATCC 39243;
SOURCE 5 GENE: RBMD, REBC;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS FLAVIN ADENINE DINUCLEOTIDE, CHROMOPYRROLIC ACID, 7-CARBOXY-K252C,
KEYWDS 2 MONOOXYGENASE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.S.RYAN,C.L.DRENNAN
REVDAT 3 30-AUG-23 2R0G 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2R0G 1 VERSN
REVDAT 1 25-SEP-07 2R0G 0
JRNL AUTH K.S.RYAN,A.R.HOWARD-JONES,M.J.HAMILL,S.J.ELLIOTT,C.T.WALSH,
JRNL AUTH 2 C.L.DRENNAN
JRNL TITL CRYSTALLOGRAPHIC TRAPPING IN THE REBECCAMYCIN BIOSYNTHETIC
JRNL TITL 2 ENZYME REBC
JRNL REF PROC.NATL.ACAD.SCI.USA V. 104 15311 2007
JRNL REFN ISSN 0027-8424
JRNL PMID 17873060
JRNL DOI 10.1073/PNAS.0707190104
REMARK 2
REMARK 2 RESOLUTION. 2.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 91.7
REMARK 3 NUMBER OF REFLECTIONS : 45763
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.255
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 2283
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7965
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 160
REMARK 3 SOLVENT ATOMS : 353
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.32
REMARK 3 ESD FROM SIGMAA (A) : 0.33
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) : 0.41
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.41
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.304
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2R0G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-07.
REMARK 100 THE DEPOSITION ID IS D_1000044271.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 141.4
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46328
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.370
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.8
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 28.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 61.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.27400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2R0C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 MICROLITERS OF REBC (9 MG/ML IN
REMARK 280 150 MM NACL, 10% GLYCEROL, 25 MM HEPES PH 7.5) WAS INCUBATED
REMARK 280 WITH 0.35 MICROLITERS OF GUANIDINE-HCL FOR 30 SECONDS, FOLLOWED
REMARK 280 BY ADDITION OF 1.5 MICROLITERS OF PRECIPITANT SOLUTION (19% PEG-
REMARK 280 8000, 0.1 M HEPES PH 7.4), WITHOUT MIXING, AT ROOM TEMPERATURE
REMARK 280 AND SEALED OVER A PRECIPITANT WELL SOLUTION. IMMEDIATELY AFTER
REMARK 280 SET UP, CRYSTAL TRAYS WERE PLACED ON A GEL SHAKER AND THEN,
REMARK 280 AFTER 12 HOURS, TRANSFERRED TO A STORAGE SPACE IN VIBRATION-
REMARK 280 ISOLATION. A CRYSTAL WAS THEN SOAKED IN 19% PEG-8000, 0.1 M
REMARK 280 HEPES PH 7.4, AND 5 MM CHROMOPYRROLIC ACID FOR 1 WEEK. THE
REMARK 280 CRYSTAL WAS THEN SOAKED FOR 5 SECONDS IN A CRYOGENIC SOLUTION
REMARK 280 CONTAINING 19% PEG-8000, 0.1 M HEPES PH 7.4, 20% GLYCEROL, AND 5
REMARK 280 MM CHROMOPYRROLIC ACID AND THEN FLASH-FROZEN IN LIQUID NITROGEN,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 39.21850
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASN A 2
REMARK 465 ASP A 246
REMARK 465 ALA A 247
REMARK 465 SER A 248
REMARK 465 LYS A 249
REMARK 465 SER A 250
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ASN B 2
REMARK 465 ASP B 246
REMARK 465 ALA B 247
REMARK 465 SER B 248
REMARK 465 LYS B 249
REMARK 465 SER B 250
REMARK 465 GLU B 418
REMARK 465 THR B 419
REMARK 465 GLU B 420
REMARK 465 VAL B 421
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 161 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 245 CG OD1 OD2
REMARK 470 THR A 251 OG1 CG2
REMARK 470 GLU A 418 CG CD OE1 OE2
REMARK 470 THR A 419 OG1 CG2
REMARK 470 GLU A 420 CG CD OE1 OE2
REMARK 470 VAL A 421 CG1 CG2
REMARK 470 LEU B 370 CG CD1 CD2
REMARK 470 ARG B 379 CG CD NE CZ NH1 NH2
REMARK 470 ILE B 380 CG1 CG2 CD1
REMARK 470 GLU B 386 CG CD OE1 OE2
REMARK 470 ARG B 390 CG CD NE CZ NH1 NH2
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 PRO A 203 C - N - CA ANGL. DEV. = 10.2 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 46 -63.76 -98.74
REMARK 500 ARG A 131 1.07 -66.73
REMARK 500 ARG A 144 -164.47 -103.29
REMARK 500 CYS A 171 54.98 -118.92
REMARK 500 SER A 176 106.62 -33.45
REMARK 500 ALA A 186 75.82 -117.00
REMARK 500 LEU A 225 68.21 -114.16
REMARK 500 ARG A 235 31.58 -152.15
REMARK 500 ALA A 263 46.84 -81.31
REMARK 500 ALA A 288 109.92 -163.67
REMARK 500 PRO A 368 -75.77 -38.46
REMARK 500 PRO A 375 -16.29 -47.16
REMARK 500 ASP A 398 78.12 -156.05
REMARK 500 ALA A 399 58.95 -114.11
REMARK 500 GLU A 418 115.28 -25.08
REMARK 500 VAL A 421 95.80 -160.39
REMARK 500 ARG A 453 -93.39 -98.24
REMARK 500 ALA A 487 102.80 -16.83
REMARK 500 GLU A 495 -43.77 72.49
REMARK 500 GLN B 29 53.64 38.72
REMARK 500 ARG B 46 -66.61 -101.67
REMARK 500 SER B 176 106.00 -33.40
REMARK 500 GLU B 211 9.65 -68.72
REMARK 500 MET B 220 55.37 -142.68
REMARK 500 LEU B 225 66.92 -101.49
REMARK 500 MET B 252 -137.80 -98.13
REMARK 500 SER B 254 -78.14 -36.94
REMARK 500 PHE B 264 144.76 -38.74
REMARK 500 ALA B 288 102.25 -164.99
REMARK 500 SER B 304 92.19 -64.98
REMARK 500 ASP B 398 80.28 -155.30
REMARK 500 ALA B 399 66.35 -117.25
REMARK 500 ARG B 409 72.99 -116.39
REMARK 500 THR B 423 -151.87 -72.71
REMARK 500 ARG B 453 -99.80 -104.15
REMARK 500 GLU B 495 -1.93 57.84
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 FAD A 1354
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7CK A 1355
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1356
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 7CK B 1357
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2R0C RELATED DB: PDB
REMARK 900 STRUCTURE OF THE SUBSTRATE-FREE FORM OF THE REBECCAMYCIN
REMARK 900 BIOSYNTHETIC ENZYME REBC
REMARK 900 RELATED ID: 2R0P RELATED DB: PDB
REMARK 900 K252C-SOAKED REBC
DBREF 2R0G A 1 529 UNP Q8KI25 Q8KI25_NOCAE 1 529
DBREF 2R0G B 1 529 UNP Q8KI25 Q8KI25_NOCAE 1 529
SEQADV 2R0G MET A -19 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G GLY A -18 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G SER A -17 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G SER A -16 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS A -15 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS A -14 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS A -13 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS A -12 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS A -11 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS A -10 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G SER A -9 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G SER A -8 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G GLY A -7 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G LEU A -6 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G VAL A -5 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G PRO A -4 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G ARG A -3 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G GLY A -2 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G SER A -1 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS A 0 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G MET B -19 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G GLY B -18 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G SER B -17 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G SER B -16 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS B -15 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS B -14 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS B -13 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS B -12 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS B -11 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS B -10 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G SER B -9 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G SER B -8 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G GLY B -7 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G LEU B -6 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G VAL B -5 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G PRO B -4 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G ARG B -3 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G GLY B -2 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G SER B -1 UNP Q8KI25 EXPRESSION TAG
SEQADV 2R0G HIS B 0 UNP Q8KI25 EXPRESSION TAG
SEQRES 1 A 549 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 549 LEU VAL PRO ARG GLY SER HIS MET ASN ALA PRO ILE GLU
SEQRES 3 A 549 THR ASP VAL LEU ILE LEU GLY GLY GLY PRO VAL GLY MET
SEQRES 4 A 549 ALA LEU ALA LEU ASP LEU ALA HIS ARG GLN VAL GLY HIS
SEQRES 5 A 549 LEU VAL VAL GLU GLN THR ASP GLY THR ILE THR HIS PRO
SEQRES 6 A 549 ARG VAL GLY THR ILE GLY PRO ARG SER MET GLU LEU PHE
SEQRES 7 A 549 ARG ARG TRP GLY VAL ALA LYS GLN ILE ARG THR ALA GLY
SEQRES 8 A 549 TRP PRO GLY ASP HIS PRO LEU ASP ALA ALA TRP VAL THR
SEQRES 9 A 549 ARG VAL GLY GLY HIS GLU VAL TYR ARG ILE PRO LEU GLY
SEQRES 10 A 549 THR ALA ASP THR ARG ALA THR PRO GLU HIS THR PRO GLU
SEQRES 11 A 549 PRO ASP ALA ILE CYS PRO GLN HIS TRP LEU ALA PRO LEU
SEQRES 12 A 549 LEU ALA GLU ALA VAL GLY GLU ARG LEU ARG THR ARG SER
SEQRES 13 A 549 ARG LEU ASP SER PHE GLU GLN ARG ASP ASP HIS VAL ARG
SEQRES 14 A 549 ALA THR ILE THR ASP LEU ARG THR GLY ALA THR ARG ALA
SEQRES 15 A 549 VAL HIS ALA ARG TYR LEU VAL ALA CYS ASP GLY ALA SER
SEQRES 16 A 549 SER PRO THR ARG LYS ALA LEU GLY ILE ASP ALA PRO PRO
SEQRES 17 A 549 ARG HIS ARG THR GLN VAL PHE ARG ASN ILE LEU PHE ARG
SEQRES 18 A 549 ALA PRO GLU LEU ARG SER LEU LEU GLY GLU ARG ALA ALA
SEQRES 19 A 549 LEU PHE PHE PHE LEU MET LEU SER SER SER LEU ARG PHE
SEQRES 20 A 549 PRO LEU ARG ALA LEU ASP GLY ARG GLY LEU TYR ARG LEU
SEQRES 21 A 549 THR VAL GLY VAL ASP ASP ALA SER LYS SER THR MET ASP
SEQRES 22 A 549 SER PHE GLU LEU VAL ARG ARG ALA VAL ALA PHE ASP THR
SEQRES 23 A 549 GLU ILE GLU VAL LEU SER ASP SER GLU TRP HIS LEU THR
SEQRES 24 A 549 HIS ARG VAL ALA ASP SER PHE SER ALA GLY ARG VAL PHE
SEQRES 25 A 549 LEU THR GLY ASP ALA ALA HIS THR LEU SER PRO SER GLY
SEQRES 26 A 549 GLY PHE GLY MET ASN THR GLY ILE GLY SER ALA ALA ASP
SEQRES 27 A 549 LEU GLY TRP LYS LEU ALA ALA THR LEU ARG GLY TRP ALA
SEQRES 28 A 549 GLY PRO GLY LEU LEU ALA THR TYR GLU GLU GLU ARG ARG
SEQRES 29 A 549 PRO VAL ALA ILE THR SER LEU GLU GLU ALA ASN VAL ASN
SEQRES 30 A 549 LEU ARG ARG THR MET ASP ARG GLU LEU PRO PRO GLY LEU
SEQRES 31 A 549 HIS ASP ASP GLY PRO ARG GLY GLU ARG ILE ARG ALA ALA
SEQRES 32 A 549 VAL ALA GLU LYS LEU GLU ARG SER GLY ALA ARG ARG GLU
SEQRES 33 A 549 PHE ASP ALA PRO GLY ILE HIS PHE GLY HIS THR TYR ARG
SEQRES 34 A 549 SER SER ILE VAL CYS GLY GLU PRO GLU THR GLU VAL ALA
SEQRES 35 A 549 THR GLY GLY TRP ARG PRO SER ALA ARG PRO GLY ALA ARG
SEQRES 36 A 549 ALA PRO HIS ALA TRP LEU THR PRO THR THR SER THR LEU
SEQRES 37 A 549 ASP LEU PHE GLY ARG GLY PHE VAL LEU LEU SER PHE GLY
SEQRES 38 A 549 THR THR ASP GLY VAL GLU ALA VAL THR ARG ALA PHE ALA
SEQRES 39 A 549 ASP ARG HIS VAL PRO LEU GLU THR VAL THR CYS HIS ALA
SEQRES 40 A 549 PRO GLU ILE HIS ALA LEU TYR GLU ARG ALA HIS VAL LEU
SEQRES 41 A 549 VAL ARG PRO ASP GLY HIS VAL ALA TRP ARG GLY ASP HIS
SEQRES 42 A 549 LEU PRO ALA GLU LEU GLY GLY LEU VAL ASP LYS VAL ARG
SEQRES 43 A 549 GLY ALA ALA
SEQRES 1 B 549 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 549 LEU VAL PRO ARG GLY SER HIS MET ASN ALA PRO ILE GLU
SEQRES 3 B 549 THR ASP VAL LEU ILE LEU GLY GLY GLY PRO VAL GLY MET
SEQRES 4 B 549 ALA LEU ALA LEU ASP LEU ALA HIS ARG GLN VAL GLY HIS
SEQRES 5 B 549 LEU VAL VAL GLU GLN THR ASP GLY THR ILE THR HIS PRO
SEQRES 6 B 549 ARG VAL GLY THR ILE GLY PRO ARG SER MET GLU LEU PHE
SEQRES 7 B 549 ARG ARG TRP GLY VAL ALA LYS GLN ILE ARG THR ALA GLY
SEQRES 8 B 549 TRP PRO GLY ASP HIS PRO LEU ASP ALA ALA TRP VAL THR
SEQRES 9 B 549 ARG VAL GLY GLY HIS GLU VAL TYR ARG ILE PRO LEU GLY
SEQRES 10 B 549 THR ALA ASP THR ARG ALA THR PRO GLU HIS THR PRO GLU
SEQRES 11 B 549 PRO ASP ALA ILE CYS PRO GLN HIS TRP LEU ALA PRO LEU
SEQRES 12 B 549 LEU ALA GLU ALA VAL GLY GLU ARG LEU ARG THR ARG SER
SEQRES 13 B 549 ARG LEU ASP SER PHE GLU GLN ARG ASP ASP HIS VAL ARG
SEQRES 14 B 549 ALA THR ILE THR ASP LEU ARG THR GLY ALA THR ARG ALA
SEQRES 15 B 549 VAL HIS ALA ARG TYR LEU VAL ALA CYS ASP GLY ALA SER
SEQRES 16 B 549 SER PRO THR ARG LYS ALA LEU GLY ILE ASP ALA PRO PRO
SEQRES 17 B 549 ARG HIS ARG THR GLN VAL PHE ARG ASN ILE LEU PHE ARG
SEQRES 18 B 549 ALA PRO GLU LEU ARG SER LEU LEU GLY GLU ARG ALA ALA
SEQRES 19 B 549 LEU PHE PHE PHE LEU MET LEU SER SER SER LEU ARG PHE
SEQRES 20 B 549 PRO LEU ARG ALA LEU ASP GLY ARG GLY LEU TYR ARG LEU
SEQRES 21 B 549 THR VAL GLY VAL ASP ASP ALA SER LYS SER THR MET ASP
SEQRES 22 B 549 SER PHE GLU LEU VAL ARG ARG ALA VAL ALA PHE ASP THR
SEQRES 23 B 549 GLU ILE GLU VAL LEU SER ASP SER GLU TRP HIS LEU THR
SEQRES 24 B 549 HIS ARG VAL ALA ASP SER PHE SER ALA GLY ARG VAL PHE
SEQRES 25 B 549 LEU THR GLY ASP ALA ALA HIS THR LEU SER PRO SER GLY
SEQRES 26 B 549 GLY PHE GLY MET ASN THR GLY ILE GLY SER ALA ALA ASP
SEQRES 27 B 549 LEU GLY TRP LYS LEU ALA ALA THR LEU ARG GLY TRP ALA
SEQRES 28 B 549 GLY PRO GLY LEU LEU ALA THR TYR GLU GLU GLU ARG ARG
SEQRES 29 B 549 PRO VAL ALA ILE THR SER LEU GLU GLU ALA ASN VAL ASN
SEQRES 30 B 549 LEU ARG ARG THR MET ASP ARG GLU LEU PRO PRO GLY LEU
SEQRES 31 B 549 HIS ASP ASP GLY PRO ARG GLY GLU ARG ILE ARG ALA ALA
SEQRES 32 B 549 VAL ALA GLU LYS LEU GLU ARG SER GLY ALA ARG ARG GLU
SEQRES 33 B 549 PHE ASP ALA PRO GLY ILE HIS PHE GLY HIS THR TYR ARG
SEQRES 34 B 549 SER SER ILE VAL CYS GLY GLU PRO GLU THR GLU VAL ALA
SEQRES 35 B 549 THR GLY GLY TRP ARG PRO SER ALA ARG PRO GLY ALA ARG
SEQRES 36 B 549 ALA PRO HIS ALA TRP LEU THR PRO THR THR SER THR LEU
SEQRES 37 B 549 ASP LEU PHE GLY ARG GLY PHE VAL LEU LEU SER PHE GLY
SEQRES 38 B 549 THR THR ASP GLY VAL GLU ALA VAL THR ARG ALA PHE ALA
SEQRES 39 B 549 ASP ARG HIS VAL PRO LEU GLU THR VAL THR CYS HIS ALA
SEQRES 40 B 549 PRO GLU ILE HIS ALA LEU TYR GLU ARG ALA HIS VAL LEU
SEQRES 41 B 549 VAL ARG PRO ASP GLY HIS VAL ALA TRP ARG GLY ASP HIS
SEQRES 42 B 549 LEU PRO ALA GLU LEU GLY GLY LEU VAL ASP LYS VAL ARG
SEQRES 43 B 549 GLY ALA ALA
HET FAD A1354 53
HET 7CK A1355 27
HET FAD B1356 53
HET 7CK B1357 27
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM 7CK 7-CARBOXY-5-HYDROXY-12,13-DIHYDRO-6H-INDOLO[2,3-
HETNAM 2 7CK A]PYRROLO[3,4-C]CARBAZOLE
HETSYN 7CK 7-HYDROXY-12,13-DIHYDRO-6H-INDOLO[2,3-A]PYRROLO[3,4-
HETSYN 2 7CK C]CARBAZOLE-5-CARBOXYLIC ACID
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 7CK 2(C21 H13 N3 O3)
FORMUL 7 HOH *353(H2 O)
HELIX 1 1 GLY A 15 HIS A 27 1 13
HELIX 2 2 GLY A 51 TRP A 61 1 11
HELIX 3 3 VAL A 63 THR A 69 1 7
HELIX 4 4 PRO A 116 GLY A 129 1 14
HELIX 5 5 SER A 176 LEU A 182 1 7
HELIX 6 6 GLU A 204 GLY A 210 1 7
HELIX 7 7 GLU A 211 ALA A 213 5 3
HELIX 8 8 ASP A 253 VAL A 262 1 10
HELIX 9 9 GLY A 295 ALA A 298 5 4
HELIX 10 10 PHE A 307 GLY A 329 1 23
HELIX 11 11 ALA A 337 ASP A 363 1 27
HELIX 12 12 GLY A 374 SER A 391 1 18
HELIX 13 13 GLY A 392 PHE A 397 5 6
HELIX 14 14 ALA A 399 GLY A 405 1 7
HELIX 15 15 LEU A 448 PHE A 451 5 4
HELIX 16 16 GLY A 465 ASP A 475 1 11
HELIX 17 17 ALA A 487 GLU A 495 1 9
HELIX 18 18 GLU A 517 ARG A 526 1 10
HELIX 19 19 GLY B 15 HIS B 27 1 13
HELIX 20 20 GLY B 51 TRP B 61 1 11
HELIX 21 21 VAL B 63 THR B 69 1 7
HELIX 22 22 PRO B 116 GLY B 129 1 14
HELIX 23 23 SER B 176 LEU B 182 1 7
HELIX 24 24 GLU B 204 GLY B 210 1 7
HELIX 25 25 GLU B 211 ALA B 213 5 3
HELIX 26 26 ASP B 253 VAL B 262 1 10
HELIX 27 27 GLY B 295 ALA B 298 5 4
HELIX 28 28 PHE B 307 GLY B 329 1 23
HELIX 29 29 ALA B 337 ARG B 364 1 28
HELIX 30 30 GLY B 374 GLY B 392 1 19
HELIX 31 31 ALA B 393 ASP B 398 5 6
HELIX 32 32 ALA B 399 GLY B 405 1 7
HELIX 33 33 LEU B 448 PHE B 451 5 4
HELIX 34 34 GLY B 465 ARG B 476 1 12
HELIX 35 35 ALA B 487 GLU B 495 1 9
HELIX 36 36 GLU B 517 ARG B 526 1 10
SHEET 1 A 6 LEU A 132 THR A 134 0
SHEET 2 A 6 HIS A 32 GLU A 36 1 N VAL A 34 O ARG A 133
SHEET 3 A 6 ILE A 5 LEU A 12 1 N ILE A 11 O LEU A 33
SHEET 4 A 6 THR A 160 ALA A 170 1 O VAL A 169 N LEU A 12
SHEET 5 A 6 VAL A 148 ASP A 154 -1 N VAL A 148 O ALA A 165
SHEET 6 A 6 SER A 136 GLN A 143 -1 N ARG A 137 O THR A 153
SHEET 1 B 6 LEU A 132 THR A 134 0
SHEET 2 B 6 HIS A 32 GLU A 36 1 N VAL A 34 O ARG A 133
SHEET 3 B 6 ILE A 5 LEU A 12 1 N ILE A 11 O LEU A 33
SHEET 4 B 6 THR A 160 ALA A 170 1 O VAL A 169 N LEU A 12
SHEET 5 B 6 VAL A 291 LEU A 293 1 O PHE A 292 N ALA A 170
SHEET 6 B 6 SER A 287 ALA A 288 -1 N ALA A 288 O VAL A 291
SHEET 1 C 2 THR A 49 ILE A 50 0
SHEET 2 C 2 ALA A 113 ILE A 114 -1 O ALA A 113 N ILE A 50
SHEET 1 D 7 GLU A 90 ILE A 94 0
SHEET 2 D 7 ALA A 80 VAL A 83 -1 N TRP A 82 O TYR A 92
SHEET 3 D 7 PHE A 216 LEU A 219 1 O PHE A 218 N ALA A 81
SHEET 4 D 7 PRO A 228 ALA A 231 -1 O LEU A 229 N PHE A 217
SHEET 5 D 7 LEU A 237 GLY A 243 -1 O ARG A 239 N ARG A 230
SHEET 6 D 7 GLN A 193 ARG A 201 -1 N ARG A 196 O VAL A 242
SHEET 7 D 7 GLU A 269 LEU A 278 -1 O LEU A 271 N LEU A 199
SHEET 1 E 2 TRP A 440 THR A 442 0
SHEET 2 E 2 THR A 445 SER A 446 -1 O THR A 445 N LEU A 441
SHEET 1 F 4 LEU A 480 THR A 484 0
SHEET 2 F 4 PHE A 455 SER A 459 1 N LEU A 457 O GLU A 481
SHEET 3 F 4 HIS A 498 VAL A 501 -1 O VAL A 501 N VAL A 456
SHEET 4 F 4 VAL A 507 GLY A 511 -1 O ALA A 508 N LEU A 500
SHEET 1 G 6 LEU B 132 ARG B 133 0
SHEET 2 G 6 HIS B 32 VAL B 35 1 N VAL B 34 O ARG B 133
SHEET 3 G 6 ILE B 5 LEU B 12 1 N ILE B 11 O LEU B 33
SHEET 4 G 6 THR B 160 ALA B 170 1 O TYR B 167 N LEU B 10
SHEET 5 G 6 VAL B 148 ASP B 154 -1 N ILE B 152 O ARG B 161
SHEET 6 G 6 SER B 136 GLN B 143 -1 N GLU B 142 O ARG B 149
SHEET 1 H 6 LEU B 132 ARG B 133 0
SHEET 2 H 6 HIS B 32 VAL B 35 1 N VAL B 34 O ARG B 133
SHEET 3 H 6 ILE B 5 LEU B 12 1 N ILE B 11 O LEU B 33
SHEET 4 H 6 THR B 160 ALA B 170 1 O TYR B 167 N LEU B 10
SHEET 5 H 6 VAL B 291 LEU B 293 1 O PHE B 292 N ALA B 170
SHEET 6 H 6 SER B 287 ALA B 288 -1 N ALA B 288 O VAL B 291
SHEET 1 I 2 THR B 49 ILE B 50 0
SHEET 2 I 2 ALA B 113 ILE B 114 -1 O ALA B 113 N ILE B 50
SHEET 1 J 7 GLU B 90 ILE B 94 0
SHEET 2 J 7 ALA B 80 VAL B 83 -1 N TRP B 82 O TYR B 92
SHEET 3 J 7 PHE B 216 LEU B 219 1 O PHE B 218 N VAL B 83
SHEET 4 J 7 PRO B 228 ALA B 231 -1 O LEU B 229 N PHE B 217
SHEET 5 J 7 LEU B 237 VAL B 244 -1 O ARG B 239 N ARG B 230
SHEET 6 J 7 GLN B 193 ARG B 201 -1 N ARG B 196 O VAL B 242
SHEET 7 J 7 GLU B 269 LEU B 278 -1 O SER B 274 N ASN B 197
SHEET 1 K 2 TRP B 440 THR B 442 0
SHEET 2 K 2 THR B 445 SER B 446 -1 O THR B 445 N LEU B 441
SHEET 1 L 4 LEU B 480 THR B 484 0
SHEET 2 L 4 PHE B 455 SER B 459 1 N LEU B 457 O GLU B 481
SHEET 3 L 4 HIS B 498 VAL B 501 -1 O VAL B 501 N VAL B 456
SHEET 4 L 4 VAL B 507 GLY B 511 -1 O TRP B 509 N LEU B 500
SITE 1 AC1 34 LEU A 12 GLY A 13 PRO A 16 VAL A 17
SITE 2 AC1 34 VAL A 35 GLU A 36 GLN A 37 THR A 38
SITE 3 AC1 34 ARG A 46 VAL A 47 GLY A 48 THR A 49
SITE 4 AC1 34 SER A 136 ARG A 137 LEU A 138 CYS A 171
SITE 5 AC1 34 ASP A 172 GLY A 173 ASN A 197 TRP A 276
SITE 6 AC1 34 GLY A 295 ASP A 296 GLY A 306 GLY A 308
SITE 7 AC1 34 MET A 309 ASN A 310 HOH A1050 HOH A1051
SITE 8 AC1 34 HOH A1059 HOH A1149 HOH A1224 HOH A1271
SITE 9 AC1 34 HOH A1291 7CK A1355
SITE 1 AC2 13 THR A 49 PHE A 216 PHE A 227 ARG A 230
SITE 2 AC2 13 ARG A 239 PRO A 303 SER A 304 GLY A 305
SITE 3 AC2 13 LEU A 358 GLU A 396 PHE A 397 HOH A1224
SITE 4 AC2 13 FAD A1354
SITE 1 AC3 31 LEU B 12 GLY B 13 PRO B 16 VAL B 17
SITE 2 AC3 31 VAL B 35 GLU B 36 GLN B 37 ARG B 46
SITE 3 AC3 31 VAL B 47 GLY B 48 THR B 49 SER B 136
SITE 4 AC3 31 ARG B 137 LEU B 138 CYS B 171 ASN B 197
SITE 5 AC3 31 TRP B 276 GLY B 295 ASP B 296 GLY B 308
SITE 6 AC3 31 MET B 309 ASN B 310 HOH B1018 HOH B1092
SITE 7 AC3 31 HOH B1100 HOH B1195 HOH B1219 HOH B1243
SITE 8 AC3 31 HOH B1314 HOH B1315 7CK B1357
SITE 1 AC4 12 PHE B 216 PHE B 227 ARG B 230 ARG B 239
SITE 2 AC4 12 THR B 241 PRO B 303 SER B 304 GLY B 305
SITE 3 AC4 12 GLU B 396 PHE B 397 HOH B1195 FAD B1356
CRYST1 64.892 78.437 123.625 90.00 99.61 90.00 P 1 21 1 4
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 0.015410 0.000000 0.002609 0.00000
SCALE2 0.000000 0.012749 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008204 0.00000
(ATOM LINES ARE NOT SHOWN.)
END