HEADER OXIDOREDUCTASE 28-JAN-11 3QJ4
TITLE CRYSTAL STRUCTURE OF HUMAN RENALASE (ISOFORM 1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RENALASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MONOAMINE OXIDASE-C, MAO-C;
COMPND 5 EC: 1.4.-.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: RNLS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET SUMO
KEYWDS FAD/NAD(P)-BINDING ROSSMANN FOLD SUPERFAMILY, FLAVIN CONTAINING AMINE
KEYWDS 2 OXIDOREDUCTASE, MONOAMINE OXIDASE, NAD, EXTRACELLULAR,
KEYWDS 3 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.MILANI,F.CIRIELLO,S.BARONI,V.PANDINI,A.ALIVERTI,G.CANEVARI,
AUTHOR 2 M.BOLOGNESI
REVDAT 3 01-NOV-23 3QJ4 1 REMARK
REVDAT 2 19-JUN-13 3QJ4 1 JRNL
REVDAT 1 13-JUL-11 3QJ4 0
JRNL AUTH M.MILANI,F.CIRIELLO,S.BARONI,V.PANDINI,G.CANEVARI,
JRNL AUTH 2 M.BOLOGNESI,A.ALIVERTI
JRNL TITL FAD-BINDING SITE AND NADP REACTIVITY IN HUMAN RENALASE: A
JRNL TITL 2 NEW ENZYME INVOLVED IN BLOOD PRESSURE REGULATION
JRNL REF J.MOL.BIOL. V. 411 463 2011
JRNL REFN ISSN 0022-2836
JRNL PMID 21699903
JRNL DOI 10.1016/J.JMB.2011.06.010
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 24995
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.140
REMARK 3 FREE R VALUE TEST SET COUNT : 1284
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 : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.60
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2876
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2250
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2739
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE : 0.2657
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.76
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 137
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 : 5181
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 121
REMARK 3 SOLVENT ATOMS : 128
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.16
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 10.32970
REMARK 3 B22 (A**2) : -17.81080
REMARK 3 B33 (A**2) : 7.48110
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -3.18990
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.369
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.922
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.886
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5444 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7411 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1866 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 155 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 812 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5444 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : 18 ; 0.000 ; HARMONIC
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 708 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5632 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.14
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.53
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.59
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: A 1 - A 341, A 401
REMARK 3 ORIGIN FOR THE GROUP (A): 14.5045 -6.4689 20.8850
REMARK 3 T TENSOR
REMARK 3 T11: 0.0867 T22: 0.0413
REMARK 3 T33: 0.1412 T12: 0.0236
REMARK 3 T13: 0.0003 T23: 0.0381
REMARK 3 L TENSOR
REMARK 3 L11: 2.8253 L22: 0.8266
REMARK 3 L33: 3.2044 L12: -0.2547
REMARK 3 L13: -0.6286 L23: 0.6898
REMARK 3 S TENSOR
REMARK 3 S11: -0.0777 S12: -0.0395 S13: -0.0212
REMARK 3 S21: -0.0661 S22: 0.0726 S23: 0.0077
REMARK 3 S31: -0.1000 S32: 0.2661 S33: 0.0050
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: B 2 - B 341, B 401
REMARK 3 ORIGIN FOR THE GROUP (A): 29.5662 36.9051 26.7451
REMARK 3 T TENSOR
REMARK 3 T11: 0.0696 T22: 0.2633
REMARK 3 T33: 0.0863 T12: 0.0071
REMARK 3 T13: 0.0057 T23: 0.0940
REMARK 3 L TENSOR
REMARK 3 L11: 3.0485 L22: 0.8660
REMARK 3 L33: 2.7339 L12: -0.3076
REMARK 3 L13: -0.3147 L23: 0.5092
REMARK 3 S TENSOR
REMARK 3 S11: -0.0627 S12: -0.4608 S13: -0.0713
REMARK 3 S21: -0.0913 S22: 0.1420 S23: -0.0430
REMARK 3 S31: -0.1071 S32: 0.0674 S33: -0.0793
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3QJ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1000063709.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87260
REMARK 200 MONOCHROMATOR : HORIZONTALLY SIDE DIFFRACTING
REMARK 200 SILICON 111 CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29646
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 48.390
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.7
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.64
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 3KKJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 8000, 0.2M AMMONIUM SULFATE,
REMARK 280 PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
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 43.29650
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 SER A 25
REMARK 465 LYS A 99
REMARK 465 GLU A 100
REMARK 465 LYS A 205
REMARK 465 ILE A 206
REMARK 465 GLU A 237
REMARK 465 ILE A 342
REMARK 465 MET B 1
REMARK 465 LYS B 99
REMARK 465 ASP B 140
REMARK 465 SER B 150
REMARK 465 GLU B 201
REMARK 465 SER B 236
REMARK 465 GLU B 237
REMARK 465 CYS B 300
REMARK 465 ILE B 342
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 THR A 148 127.84 -173.49
REMARK 500 THR A 294 -81.27 -88.15
REMARK 500 ALA A 297 -68.36 -141.60
REMARK 500 CYS A 300 -8.35 95.94
REMARK 500 THR A 320 -104.64 -126.22
REMARK 500 HIS B 73 30.33 -95.87
REMARK 500 ALA B 298 -127.09 55.22
REMARK 500 HIS B 307 145.44 -175.95
REMARK 500 THR B 320 -100.22 -125.89
REMARK 500 LYS B 339 -60.66 -21.62
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 343
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 344
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 343
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 NATURAL VARIANT, SEE UNP DATABASE RNLS_HUMAN
DBREF 3QJ4 A 1 342 UNP Q5VYX0 RNLS_HUMAN 1 342
DBREF 3QJ4 B 1 342 UNP Q5VYX0 RNLS_HUMAN 1 342
SEQADV 3QJ4 ASP A 37 UNP Q5VYX0 GLU 37 SEE REMARK 999
SEQADV 3QJ4 ASP B 37 UNP Q5VYX0 GLU 37 SEE REMARK 999
SEQRES 1 A 342 MET ALA GLN VAL LEU ILE VAL GLY ALA GLY MET THR GLY
SEQRES 2 A 342 SER LEU CYS ALA ALA LEU LEU ARG ARG GLN THR SER GLY
SEQRES 3 A 342 PRO LEU TYR LEU ALA VAL TRP ASP LYS ALA ASP ASP SER
SEQRES 4 A 342 GLY GLY ARG MET THR THR ALA CYS SER PRO HIS ASN PRO
SEQRES 5 A 342 GLN CYS THR ALA ASP LEU GLY ALA GLN TYR ILE THR CYS
SEQRES 6 A 342 THR PRO HIS TYR ALA LYS LYS HIS GLN ARG PHE TYR ASP
SEQRES 7 A 342 GLU LEU LEU ALA TYR GLY VAL LEU ARG PRO LEU SER SER
SEQRES 8 A 342 PRO ILE GLU GLY MET VAL MET LYS GLU GLY ASP CYS ASN
SEQRES 9 A 342 PHE VAL ALA PRO GLN GLY ILE SER SER ILE ILE LYS HIS
SEQRES 10 A 342 TYR LEU LYS GLU SER GLY ALA GLU VAL TYR PHE ARG HIS
SEQRES 11 A 342 ARG VAL THR GLN ILE ASN LEU ARG ASP ASP LYS TRP GLU
SEQRES 12 A 342 VAL SER LYS GLN THR GLY SER PRO GLU GLN PHE ASP LEU
SEQRES 13 A 342 ILE VAL LEU THR MET PRO VAL PRO GLU ILE LEU GLN LEU
SEQRES 14 A 342 GLN GLY ASP ILE THR THR LEU ILE SER GLU CYS GLN ARG
SEQRES 15 A 342 GLN GLN LEU GLU ALA VAL SER TYR SER SER ARG TYR ALA
SEQRES 16 A 342 LEU GLY LEU PHE TYR GLU ALA GLY THR LYS ILE ASP VAL
SEQRES 17 A 342 PRO TRP ALA GLY GLN TYR ILE THR SER ASN PRO CYS ILE
SEQRES 18 A 342 ARG PHE VAL SER ILE ASP ASN LYS LYS ARG ASN ILE GLU
SEQRES 19 A 342 SER SER GLU ILE GLY PRO SER LEU VAL ILE HIS THR THR
SEQRES 20 A 342 VAL PRO PHE GLY VAL THR TYR LEU GLU HIS SER ILE GLU
SEQRES 21 A 342 ASP VAL GLN GLU LEU VAL PHE GLN GLN LEU GLU ASN ILE
SEQRES 22 A 342 LEU PRO GLY LEU PRO GLN PRO ILE ALA THR LYS CYS GLN
SEQRES 23 A 342 LYS TRP ARG HIS SER GLN VAL THR ASN ALA ALA ALA ASN
SEQRES 24 A 342 CYS PRO GLY GLN MET THR LEU HIS HIS LYS PRO PHE LEU
SEQRES 25 A 342 ALA CYS GLY GLY ASP GLY PHE THR GLN SER ASN PHE ASP
SEQRES 26 A 342 GLY CYS ILE THR SER ALA LEU CYS VAL LEU GLU ALA LEU
SEQRES 27 A 342 LYS ASN TYR ILE
SEQRES 1 B 342 MET ALA GLN VAL LEU ILE VAL GLY ALA GLY MET THR GLY
SEQRES 2 B 342 SER LEU CYS ALA ALA LEU LEU ARG ARG GLN THR SER GLY
SEQRES 3 B 342 PRO LEU TYR LEU ALA VAL TRP ASP LYS ALA ASP ASP SER
SEQRES 4 B 342 GLY GLY ARG MET THR THR ALA CYS SER PRO HIS ASN PRO
SEQRES 5 B 342 GLN CYS THR ALA ASP LEU GLY ALA GLN TYR ILE THR CYS
SEQRES 6 B 342 THR PRO HIS TYR ALA LYS LYS HIS GLN ARG PHE TYR ASP
SEQRES 7 B 342 GLU LEU LEU ALA TYR GLY VAL LEU ARG PRO LEU SER SER
SEQRES 8 B 342 PRO ILE GLU GLY MET VAL MET LYS GLU GLY ASP CYS ASN
SEQRES 9 B 342 PHE VAL ALA PRO GLN GLY ILE SER SER ILE ILE LYS HIS
SEQRES 10 B 342 TYR LEU LYS GLU SER GLY ALA GLU VAL TYR PHE ARG HIS
SEQRES 11 B 342 ARG VAL THR GLN ILE ASN LEU ARG ASP ASP LYS TRP GLU
SEQRES 12 B 342 VAL SER LYS GLN THR GLY SER PRO GLU GLN PHE ASP LEU
SEQRES 13 B 342 ILE VAL LEU THR MET PRO VAL PRO GLU ILE LEU GLN LEU
SEQRES 14 B 342 GLN GLY ASP ILE THR THR LEU ILE SER GLU CYS GLN ARG
SEQRES 15 B 342 GLN GLN LEU GLU ALA VAL SER TYR SER SER ARG TYR ALA
SEQRES 16 B 342 LEU GLY LEU PHE TYR GLU ALA GLY THR LYS ILE ASP VAL
SEQRES 17 B 342 PRO TRP ALA GLY GLN TYR ILE THR SER ASN PRO CYS ILE
SEQRES 18 B 342 ARG PHE VAL SER ILE ASP ASN LYS LYS ARG ASN ILE GLU
SEQRES 19 B 342 SER SER GLU ILE GLY PRO SER LEU VAL ILE HIS THR THR
SEQRES 20 B 342 VAL PRO PHE GLY VAL THR TYR LEU GLU HIS SER ILE GLU
SEQRES 21 B 342 ASP VAL GLN GLU LEU VAL PHE GLN GLN LEU GLU ASN ILE
SEQRES 22 B 342 LEU PRO GLY LEU PRO GLN PRO ILE ALA THR LYS CYS GLN
SEQRES 23 B 342 LYS TRP ARG HIS SER GLN VAL THR ASN ALA ALA ALA ASN
SEQRES 24 B 342 CYS PRO GLY GLN MET THR LEU HIS HIS LYS PRO PHE LEU
SEQRES 25 B 342 ALA CYS GLY GLY ASP GLY PHE THR GLN SER ASN PHE ASP
SEQRES 26 B 342 GLY CYS ILE THR SER ALA LEU CYS VAL LEU GLU ALA LEU
SEQRES 27 B 342 LYS ASN TYR ILE
HET FAD A 401 53
HET SO4 A 343 5
HET SO4 A 344 5
HET FAD B 401 53
HET SO4 B 343 5
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM SO4 SULFATE ION
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 SO4 3(O4 S 2-)
FORMUL 8 HOH *128(H2 O)
HELIX 1 1 GLY A 10 ARG A 22 1 13
HELIX 2 2 GLY A 40 MET A 43 5 4
HELIX 3 3 HIS A 68 HIS A 73 1 6
HELIX 4 4 HIS A 73 TYR A 83 1 11
HELIX 5 5 SER A 112 GLY A 123 1 12
HELIX 6 6 PRO A 162 LEU A 167 1 6
HELIX 7 7 ASP A 172 ILE A 177 1 6
HELIX 8 8 SER A 178 ALA A 187 1 10
HELIX 9 9 ASP A 227 ARG A 231 1 5
HELIX 10 10 THR A 247 TYR A 254 1 8
HELIX 11 11 SER A 258 LEU A 274 1 17
HELIX 12 12 GLY A 316 THR A 320 5 5
HELIX 13 13 ASN A 323 LYS A 339 1 17
HELIX 14 14 GLY B 10 THR B 24 1 15
HELIX 15 15 GLY B 40 MET B 43 5 4
HELIX 16 16 HIS B 68 HIS B 73 1 6
HELIX 17 17 HIS B 73 TYR B 83 1 11
HELIX 18 18 SER B 112 SER B 122 1 11
HELIX 19 19 PRO B 162 LEU B 167 1 6
HELIX 20 20 ASP B 172 ILE B 177 1 6
HELIX 21 21 SER B 178 ALA B 187 1 10
HELIX 22 22 ASP B 227 ARG B 231 1 5
HELIX 23 23 THR B 247 TYR B 254 1 8
HELIX 24 24 SER B 258 LEU B 274 1 17
HELIX 25 25 GLY B 316 THR B 320 5 5
HELIX 26 26 ASN B 323 LYS B 339 1 17
SHEET 1 A 6 GLU A 125 TYR A 127 0
SHEET 2 A 6 LEU A 28 TRP A 33 1 N VAL A 32 O TYR A 127
SHEET 3 A 6 ALA A 2 VAL A 7 1 N ALA A 2 O TYR A 29
SHEET 4 A 6 LEU A 156 LEU A 159 1 O VAL A 158 N VAL A 7
SHEET 5 A 6 PHE A 311 CYS A 314 1 O ALA A 313 N LEU A 159
SHEET 6 A 6 MET A 304 HIS A 307 -1 N LEU A 306 O LEU A 312
SHEET 1 B 2 THR A 45 CYS A 47 0
SHEET 2 B 2 THR A 55 ASP A 57 -1 O ALA A 56 N ALA A 46
SHEET 1 C 3 ILE A 63 CYS A 65 0
SHEET 2 C 3 CYS A 103 VAL A 106 -1 O CYS A 103 N CYS A 65
SHEET 3 C 3 ARG A 87 PRO A 88 -1 N ARG A 87 O VAL A 106
SHEET 1 D 6 ILE A 93 GLU A 94 0
SHEET 2 D 6 GLY A 212 TYR A 214 1 O TYR A 214 N GLU A 94
SHEET 3 D 6 ILE A 221 ILE A 226 -1 O VAL A 224 N GLN A 213
SHEET 4 D 6 SER A 241 THR A 246 -1 O HIS A 245 N PHE A 223
SHEET 5 D 6 ARG A 193 PHE A 199 -1 N LEU A 198 O LEU A 242
SHEET 6 D 6 ALA A 282 TRP A 288 -1 O ALA A 282 N PHE A 199
SHEET 1 E 3 VAL A 132 LEU A 137 0
SHEET 2 E 3 TRP A 142 LYS A 146 -1 O GLU A 143 N ASN A 136
SHEET 3 E 3 GLU A 152 PHE A 154 -1 O GLU A 152 N VAL A 144
SHEET 1 F 6 ALA B 124 TYR B 127 0
SHEET 2 F 6 TYR B 29 TRP B 33 1 N VAL B 32 O TYR B 127
SHEET 3 F 6 GLN B 3 VAL B 7 1 N VAL B 4 O TYR B 29
SHEET 4 F 6 LEU B 156 LEU B 159 1 O LEU B 156 N LEU B 5
SHEET 5 F 6 PHE B 311 CYS B 314 1 O ALA B 313 N LEU B 159
SHEET 6 F 6 MET B 304 HIS B 307 -1 N LEU B 306 O LEU B 312
SHEET 1 G 2 THR B 45 CYS B 47 0
SHEET 2 G 2 THR B 55 ASP B 57 -1 O ALA B 56 N ALA B 46
SHEET 1 H 3 ILE B 63 CYS B 65 0
SHEET 2 H 3 CYS B 103 VAL B 106 -1 O CYS B 103 N CYS B 65
SHEET 3 H 3 ARG B 87 PRO B 88 -1 N ARG B 87 O VAL B 106
SHEET 1 I 6 ILE B 93 GLU B 94 0
SHEET 2 I 6 GLY B 212 TYR B 214 1 O TYR B 214 N GLU B 94
SHEET 3 I 6 ILE B 221 ILE B 226 -1 O VAL B 224 N GLN B 213
SHEET 4 I 6 SER B 241 THR B 246 -1 O HIS B 245 N PHE B 223
SHEET 5 I 6 ARG B 193 PHE B 199 -1 N LEU B 198 O LEU B 242
SHEET 6 I 6 ALA B 282 TRP B 288 -1 O ALA B 282 N PHE B 199
SHEET 1 J 3 VAL B 132 LEU B 137 0
SHEET 2 J 3 TRP B 142 LYS B 146 -1 O GLU B 143 N ASN B 136
SHEET 3 J 3 GLU B 152 PHE B 154 -1 O GLU B 152 N VAL B 144
SHEET 1 K 2 SER B 189 TYR B 190 0
SHEET 2 K 2 VAL B 293 ASN B 295 -1 O THR B 294 N SER B 189
CISPEP 1 GLY A 26 PRO A 27 0 0.63
CISPEP 2 ALA A 70 LYS A 71 0 12.39
CISPEP 3 THR A 148 GLY A 149 0 0.63
CISPEP 4 ALA A 297 ALA A 298 0 -3.26
CISPEP 5 LYS A 309 PRO A 310 0 3.55
CISPEP 6 LYS B 309 PRO B 310 0 0.49
SITE 1 AC1 30 VAL A 7 GLY A 8 MET A 11 THR A 12
SITE 2 AC1 30 ASP A 34 LYS A 35 GLY A 41 ARG A 42
SITE 3 AC1 30 GLY A 59 ALA A 60 GLN A 61 TYR A 62
SITE 4 AC1 30 HIS A 130 ARG A 131 VAL A 132 MET A 161
SITE 5 AC1 30 HIS A 245 TRP A 288 SER A 291 GLN A 292
SITE 6 AC1 30 ASP A 317 SER A 322 ASN A 323 PHE A 324
SITE 7 AC1 30 CYS A 327 HOH A 348 HOH A 392 HOH A 394
SITE 8 AC1 30 HOH A 404 HOH A 411
SITE 1 AC2 2 LYS A 287 ARG A 289
SITE 1 AC3 4 ARG A 193 ARG A 222 THR A 247 VAL A 248
SITE 1 AC4 30 VAL B 7 GLY B 8 MET B 11 THR B 12
SITE 2 AC4 30 ASP B 34 LYS B 35 GLY B 41 ARG B 42
SITE 3 AC4 30 GLY B 59 ALA B 60 GLN B 61 TYR B 62
SITE 4 AC4 30 HIS B 130 ARG B 131 VAL B 132 MET B 161
SITE 5 AC4 30 HIS B 245 TRP B 288 SER B 291 ASP B 317
SITE 6 AC4 30 SER B 322 ASN B 323 PHE B 324 CYS B 327
SITE 7 AC4 30 HOH B 352 HOH B 386 HOH B 388 HOH B 389
SITE 8 AC4 30 HOH B 390 HOH B 391
SITE 1 AC5 5 ARG B 193 ARG B 222 THR B 247 VAL B 248
SITE 2 AC5 5 HOH B 402
CRYST1 53.837 86.593 93.180 90.00 95.30 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 0.018575 0.000000 0.001723 0.00000
SCALE2 0.000000 0.011548 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010778 0.00000
(ATOM LINES ARE NOT SHOWN.)
END