HEADER OXIDOREDUCTASE 23-JAN-14 4CNJ
TITLE L-AMINOACETONE OXIDASE FROM STREPTOCOCCUS OLIGOFERMENTANS BELONGS TO A
TITLE 2 NEW 3-DOMAIN FAMILY OF BACTERIAL FLAVOPROTEINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: L-AMINO ACID OXIDASE;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 SYNONYM: L-AMINOACETONE OXIDASE;
COMPND 5 EC: 1.1.3.2;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS OLIGOFERMENTANS;
SOURCE 3 ORGANISM_TAXID: 195041;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET24B
KEYWDS OXIDOREDUCTASE, FLAVOPROTEINS
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MOLLA,M.NARDINI,P.MOTTA,P.D'ARRIGO,M.BOLOGNESI,L.POLLEGIONI
REVDAT 3 20-DEC-23 4CNJ 1 REMARK
REVDAT 2 17-DEC-14 4CNJ 1 JRNL
REVDAT 1 15-OCT-14 4CNJ 0
JRNL AUTH G.MOLLA,M.NARDINI,P.MOTTA,P.D'ARRIGO,W.PANZERI,L.POLLEGIONI
JRNL TITL AMINOACETONE OXIDASE FROM STREPTOCOCCUS OLIGOFERMENTAS
JRNL TITL 2 BELONGS TO A NEW THREE-DOMAIN FAMILY OF BACTERIAL
JRNL TITL 3 FLAVOPROTEINS.
JRNL REF BIOCHEM.J. V. 464 387 2014
JRNL REFN ISSN 0264-6021
JRNL PMID 25269103
JRNL DOI 10.1042/BJ20140972
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0032
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 60955
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) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.188
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3252
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.70
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.77
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4489
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.68
REMARK 3 BIN R VALUE (WORKING SET) : 0.3230
REMARK 3 BIN FREE R VALUE SET COUNT : 231
REMARK 3 BIN FREE R VALUE : 0.3860
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12024
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 212
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.08
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.60000
REMARK 3 B22 (A**2) : 0.73000
REMARK 3 B33 (A**2) : -1.33000
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): 0.553
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.297
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.235
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.878
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12619 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 17088 ; 1.342 ; 1.994
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1574 ; 6.082 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 498 ;38.089 ;24.819
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2205 ;18.325 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;22.464 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1964 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9165 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 6266 ; 3.073 ; 5.702
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7829 ; 4.850 ; 8.545
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 6353 ; 3.857 ; 6.047
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 4CNJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JAN-14.
REMARK 100 THE DEPOSITION ID IS D_1290059534.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
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 : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 68683
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 64.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.53000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
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 2GQF
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 63.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0 M (NH4)2SO4, 0.1 M NA-CACODYLATE
REMARK 280 OR MES (PH 6.5), AND 0.2 M NACL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X,-Y,-Z
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.17300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 112.09950
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.17300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 112.09950
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 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 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 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 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 THR B 130 CB - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 ASN C 51 N - CA - C ANGL. DEV. = -16.8 DEGREES
REMARK 500 CYS D 50 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 TYR A 25 34.22 -90.82
REMARK 500 CYS A 50 107.29 80.24
REMARK 500 ASN A 57 -163.54 -76.87
REMARK 500 ASP A 141 -97.87 56.98
REMARK 500 TYR A 167 54.09 39.08
REMARK 500 THR A 188 -179.14 -61.92
REMARK 500 PHE A 201 146.71 -175.42
REMARK 500 PRO A 202 68.38 -68.12
REMARK 500 ASP A 213 79.59 62.05
REMARK 500 TYR A 218 113.07 -169.81
REMARK 500 HIS A 225 -165.16 -170.78
REMARK 500 ARG A 273 -1.75 -56.34
REMARK 500 GLU A 318 42.89 -151.33
REMARK 500 ASP A 365 58.08 -69.73
REMARK 500 ASN B 2 31.93 -83.85
REMARK 500 CYS B 50 89.31 72.46
REMARK 500 GLU B 98 -151.40 -90.53
REMARK 500 ASP B 108 7.60 55.92
REMARK 500 ARG B 111 -9.98 -56.46
REMARK 500 ASN B 131 -8.44 78.05
REMARK 500 ASP B 141 -120.17 61.11
REMARK 500 THR B 161 59.02 -142.46
REMARK 500 TYR B 167 59.44 73.35
REMARK 500 SER B 169 -5.61 -59.73
REMARK 500 PHE B 201 149.80 -170.72
REMARK 500 PRO B 202 72.79 -69.69
REMARK 500 ASP B 213 60.65 33.47
REMARK 500 TYR B 218 118.42 -161.82
REMARK 500 PRO B 298 159.52 -46.43
REMARK 500 GLU B 318 70.17 -151.51
REMARK 500 CYS C 50 76.81 54.36
REMARK 500 ASN C 51 107.66 -51.19
REMARK 500 THR C 53 -179.73 176.70
REMARK 500 ASP C 80 -165.64 -117.81
REMARK 500 GLU C 98 -132.00 -94.75
REMARK 500 ASP C 141 -117.08 50.29
REMARK 500 PHE C 183 31.47 -87.59
REMARK 500 PHE C 201 147.65 -170.95
REMARK 500 PRO C 202 77.12 -68.08
REMARK 500 PRO C 298 156.01 -48.28
REMARK 500 GLU C 318 48.28 -153.03
REMARK 500 CYS D 50 63.96 68.55
REMARK 500 ASN D 51 105.30 -54.21
REMARK 500 GLU D 98 -138.16 -118.43
REMARK 500 ASP D 141 -128.46 64.21
REMARK 500 PRO D 202 72.13 -67.60
REMARK 500 HIS D 225 -156.14 -151.90
REMARK 500 LYS D 247 -18.00 -143.57
REMARK 500 GLU D 318 47.66 -149.28
REMARK 500 ASP D 365 75.41 -68.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: DSSP
REMARK 700 THE SHEETS PRESENTED AS "AE" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "BE" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "CF" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
REMARK 700 THE SHEETS PRESENTED AS "DF" IN EACH CHAIN ON SHEET RECORDS
REMARK 700 BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY
REMARK 700 A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
REMARK 700 ARE IDENTICAL.
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 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4CNK RELATED DB: PDB
REMARK 900 L-AMINOACETONE OXIDASE FROM STREPTOCOCCUS OLIGOFERMENTANS BELONGS
REMARK 900 TO A NEW 3-DOMAIN FAMILY OF BACTERIAL FLAVOPROTEINS
DBREF 4CNJ A 1 391 UNP B1PUC6 B1PUC6_9STRE 1 391
DBREF 4CNJ B 1 391 UNP B1PUC6 B1PUC6_9STRE 1 391
DBREF 4CNJ C 1 391 UNP B1PUC6 B1PUC6_9STRE 1 391
DBREF 4CNJ D 1 391 UNP B1PUC6 B1PUC6_9STRE 1 391
SEQRES 1 A 391 MET ASN HIS PHE ASP THR ILE ILE ILE GLY GLY GLY PRO
SEQRES 2 A 391 ALA GLY MET MET ALA THR ILE SER SER SER PHE TYR GLY
SEQRES 3 A 391 GLN LYS THR LEU LEU LEU GLU LYS ASN LYS ARG LEU GLY
SEQRES 4 A 391 LYS LYS LEU ALA GLY THR GLY GLY GLY ARG CYS ASN VAL
SEQRES 5 A 391 THR ASN ASN GLY ASN LEU ASP ASP LEU MET ALA GLY ILE
SEQRES 6 A 391 PRO GLY ASN GLY ARG PHE LEU TYR SER VAL PHE SER GLN
SEQRES 7 A 391 PHE ASP ASN HIS ASP ILE ILE ASN PHE PHE THR GLU ASN
SEQRES 8 A 391 GLY VAL LYS LEU LYS VAL GLU ASP HIS GLY ARG VAL PHE
SEQRES 9 A 391 PRO VAL THR ASP LYS SER ARG THR ILE ILE GLU ALA LEU
SEQRES 10 A 391 GLU LYS LYS ILE ALA GLU LEU GLY GLY THR VAL ILE THR
SEQRES 11 A 391 ASN THR GLU ILE VAL SER VAL LYS LYS THR ASP GLU LEU
SEQRES 12 A 391 PHE THR VAL ARG SER SER ASP GLN ALA TRP THR CYS GLN
SEQRES 13 A 391 LYS LEU ILE VAL THR THR GLY GLY LYS SER TYR PRO SER
SEQRES 14 A 391 THR GLY SER THR GLY PHE GLY HIS ASP ILE ALA ARG HIS
SEQRES 15 A 391 PHE LYS HIS THR VAL THR ASP LEU GLU ALA ALA GLU SER
SEQRES 16 A 391 PRO LEU LEU THR ASP PHE PRO HIS LYS ALA LEU GLN GLY
SEQRES 17 A 391 ILE SER LEU ASP ASP VAL THR LEU SER TYR GLY LYS HIS
SEQRES 18 A 391 ILE ILE THR HIS ASP LEU LEU PHE THR HIS PHE GLY LEU
SEQRES 19 A 391 SER GLY PRO ALA ALA LEU ARG LEU SER SER PHE VAL LYS
SEQRES 20 A 391 GLY GLY GLU THR ILE TYR LEU ASP VAL LEU PRO GLN MET
SEQRES 21 A 391 SER GLN GLN ASP LEU ALA ASP PHE LEU GLU GLU HIS ARG
SEQRES 22 A 391 GLU LYS SER LEU LYS ASN CYS LEU LYS ILE LEU LEU PRO
SEQRES 23 A 391 GLU ARG ILE ALA ASP PHE PHE THR GLN PRO PHE PRO GLU
SEQRES 24 A 391 LYS VAL LYS GLN LEU ASN LEU SER GLU LYS GLU ALA LEU
SEQRES 25 A 391 ILE LYS GLN ILE LYS GLU LEU PRO ILE SER VAL THR GLY
SEQRES 26 A 391 LYS MET SER LEU ALA LYS SER PHE VAL THR LYS GLY GLY
SEQRES 27 A 391 VAL SER LEU LYS GLU ILE ASN PRO LYS THR LEU GLU SER
SEQRES 28 A 391 LYS LEU VAL PRO GLY LEU HIS PHE ALA GLY GLU VAL LEU
SEQRES 29 A 391 ASP ILE ASN ALA HIS THR GLY GLY PHE ASN ILE THR SER
SEQRES 30 A 391 ALA LEU CYS THR GLY TRP VAL ALA GLY SER LEU HIS TYR
SEQRES 31 A 391 ASP
SEQRES 1 B 391 MET ASN HIS PHE ASP THR ILE ILE ILE GLY GLY GLY PRO
SEQRES 2 B 391 ALA GLY MET MET ALA THR ILE SER SER SER PHE TYR GLY
SEQRES 3 B 391 GLN LYS THR LEU LEU LEU GLU LYS ASN LYS ARG LEU GLY
SEQRES 4 B 391 LYS LYS LEU ALA GLY THR GLY GLY GLY ARG CYS ASN VAL
SEQRES 5 B 391 THR ASN ASN GLY ASN LEU ASP ASP LEU MET ALA GLY ILE
SEQRES 6 B 391 PRO GLY ASN GLY ARG PHE LEU TYR SER VAL PHE SER GLN
SEQRES 7 B 391 PHE ASP ASN HIS ASP ILE ILE ASN PHE PHE THR GLU ASN
SEQRES 8 B 391 GLY VAL LYS LEU LYS VAL GLU ASP HIS GLY ARG VAL PHE
SEQRES 9 B 391 PRO VAL THR ASP LYS SER ARG THR ILE ILE GLU ALA LEU
SEQRES 10 B 391 GLU LYS LYS ILE ALA GLU LEU GLY GLY THR VAL ILE THR
SEQRES 11 B 391 ASN THR GLU ILE VAL SER VAL LYS LYS THR ASP GLU LEU
SEQRES 12 B 391 PHE THR VAL ARG SER SER ASP GLN ALA TRP THR CYS GLN
SEQRES 13 B 391 LYS LEU ILE VAL THR THR GLY GLY LYS SER TYR PRO SER
SEQRES 14 B 391 THR GLY SER THR GLY PHE GLY HIS ASP ILE ALA ARG HIS
SEQRES 15 B 391 PHE LYS HIS THR VAL THR ASP LEU GLU ALA ALA GLU SER
SEQRES 16 B 391 PRO LEU LEU THR ASP PHE PRO HIS LYS ALA LEU GLN GLY
SEQRES 17 B 391 ILE SER LEU ASP ASP VAL THR LEU SER TYR GLY LYS HIS
SEQRES 18 B 391 ILE ILE THR HIS ASP LEU LEU PHE THR HIS PHE GLY LEU
SEQRES 19 B 391 SER GLY PRO ALA ALA LEU ARG LEU SER SER PHE VAL LYS
SEQRES 20 B 391 GLY GLY GLU THR ILE TYR LEU ASP VAL LEU PRO GLN MET
SEQRES 21 B 391 SER GLN GLN ASP LEU ALA ASP PHE LEU GLU GLU HIS ARG
SEQRES 22 B 391 GLU LYS SER LEU LYS ASN CYS LEU LYS ILE LEU LEU PRO
SEQRES 23 B 391 GLU ARG ILE ALA ASP PHE PHE THR GLN PRO PHE PRO GLU
SEQRES 24 B 391 LYS VAL LYS GLN LEU ASN LEU SER GLU LYS GLU ALA LEU
SEQRES 25 B 391 ILE LYS GLN ILE LYS GLU LEU PRO ILE SER VAL THR GLY
SEQRES 26 B 391 LYS MET SER LEU ALA LYS SER PHE VAL THR LYS GLY GLY
SEQRES 27 B 391 VAL SER LEU LYS GLU ILE ASN PRO LYS THR LEU GLU SER
SEQRES 28 B 391 LYS LEU VAL PRO GLY LEU HIS PHE ALA GLY GLU VAL LEU
SEQRES 29 B 391 ASP ILE ASN ALA HIS THR GLY GLY PHE ASN ILE THR SER
SEQRES 30 B 391 ALA LEU CYS THR GLY TRP VAL ALA GLY SER LEU HIS TYR
SEQRES 31 B 391 ASP
SEQRES 1 C 391 MET ASN HIS PHE ASP THR ILE ILE ILE GLY GLY GLY PRO
SEQRES 2 C 391 ALA GLY MET MET ALA THR ILE SER SER SER PHE TYR GLY
SEQRES 3 C 391 GLN LYS THR LEU LEU LEU GLU LYS ASN LYS ARG LEU GLY
SEQRES 4 C 391 LYS LYS LEU ALA GLY THR GLY GLY GLY ARG CYS ASN VAL
SEQRES 5 C 391 THR ASN ASN GLY ASN LEU ASP ASP LEU MET ALA GLY ILE
SEQRES 6 C 391 PRO GLY ASN GLY ARG PHE LEU TYR SER VAL PHE SER GLN
SEQRES 7 C 391 PHE ASP ASN HIS ASP ILE ILE ASN PHE PHE THR GLU ASN
SEQRES 8 C 391 GLY VAL LYS LEU LYS VAL GLU ASP HIS GLY ARG VAL PHE
SEQRES 9 C 391 PRO VAL THR ASP LYS SER ARG THR ILE ILE GLU ALA LEU
SEQRES 10 C 391 GLU LYS LYS ILE ALA GLU LEU GLY GLY THR VAL ILE THR
SEQRES 11 C 391 ASN THR GLU ILE VAL SER VAL LYS LYS THR ASP GLU LEU
SEQRES 12 C 391 PHE THR VAL ARG SER SER ASP GLN ALA TRP THR CYS GLN
SEQRES 13 C 391 LYS LEU ILE VAL THR THR GLY GLY LYS SER TYR PRO SER
SEQRES 14 C 391 THR GLY SER THR GLY PHE GLY HIS ASP ILE ALA ARG HIS
SEQRES 15 C 391 PHE LYS HIS THR VAL THR ASP LEU GLU ALA ALA GLU SER
SEQRES 16 C 391 PRO LEU LEU THR ASP PHE PRO HIS LYS ALA LEU GLN GLY
SEQRES 17 C 391 ILE SER LEU ASP ASP VAL THR LEU SER TYR GLY LYS HIS
SEQRES 18 C 391 ILE ILE THR HIS ASP LEU LEU PHE THR HIS PHE GLY LEU
SEQRES 19 C 391 SER GLY PRO ALA ALA LEU ARG LEU SER SER PHE VAL LYS
SEQRES 20 C 391 GLY GLY GLU THR ILE TYR LEU ASP VAL LEU PRO GLN MET
SEQRES 21 C 391 SER GLN GLN ASP LEU ALA ASP PHE LEU GLU GLU HIS ARG
SEQRES 22 C 391 GLU LYS SER LEU LYS ASN CYS LEU LYS ILE LEU LEU PRO
SEQRES 23 C 391 GLU ARG ILE ALA ASP PHE PHE THR GLN PRO PHE PRO GLU
SEQRES 24 C 391 LYS VAL LYS GLN LEU ASN LEU SER GLU LYS GLU ALA LEU
SEQRES 25 C 391 ILE LYS GLN ILE LYS GLU LEU PRO ILE SER VAL THR GLY
SEQRES 26 C 391 LYS MET SER LEU ALA LYS SER PHE VAL THR LYS GLY GLY
SEQRES 27 C 391 VAL SER LEU LYS GLU ILE ASN PRO LYS THR LEU GLU SER
SEQRES 28 C 391 LYS LEU VAL PRO GLY LEU HIS PHE ALA GLY GLU VAL LEU
SEQRES 29 C 391 ASP ILE ASN ALA HIS THR GLY GLY PHE ASN ILE THR SER
SEQRES 30 C 391 ALA LEU CYS THR GLY TRP VAL ALA GLY SER LEU HIS TYR
SEQRES 31 C 391 ASP
SEQRES 1 D 391 MET ASN HIS PHE ASP THR ILE ILE ILE GLY GLY GLY PRO
SEQRES 2 D 391 ALA GLY MET MET ALA THR ILE SER SER SER PHE TYR GLY
SEQRES 3 D 391 GLN LYS THR LEU LEU LEU GLU LYS ASN LYS ARG LEU GLY
SEQRES 4 D 391 LYS LYS LEU ALA GLY THR GLY GLY GLY ARG CYS ASN VAL
SEQRES 5 D 391 THR ASN ASN GLY ASN LEU ASP ASP LEU MET ALA GLY ILE
SEQRES 6 D 391 PRO GLY ASN GLY ARG PHE LEU TYR SER VAL PHE SER GLN
SEQRES 7 D 391 PHE ASP ASN HIS ASP ILE ILE ASN PHE PHE THR GLU ASN
SEQRES 8 D 391 GLY VAL LYS LEU LYS VAL GLU ASP HIS GLY ARG VAL PHE
SEQRES 9 D 391 PRO VAL THR ASP LYS SER ARG THR ILE ILE GLU ALA LEU
SEQRES 10 D 391 GLU LYS LYS ILE ALA GLU LEU GLY GLY THR VAL ILE THR
SEQRES 11 D 391 ASN THR GLU ILE VAL SER VAL LYS LYS THR ASP GLU LEU
SEQRES 12 D 391 PHE THR VAL ARG SER SER ASP GLN ALA TRP THR CYS GLN
SEQRES 13 D 391 LYS LEU ILE VAL THR THR GLY GLY LYS SER TYR PRO SER
SEQRES 14 D 391 THR GLY SER THR GLY PHE GLY HIS ASP ILE ALA ARG HIS
SEQRES 15 D 391 PHE LYS HIS THR VAL THR ASP LEU GLU ALA ALA GLU SER
SEQRES 16 D 391 PRO LEU LEU THR ASP PHE PRO HIS LYS ALA LEU GLN GLY
SEQRES 17 D 391 ILE SER LEU ASP ASP VAL THR LEU SER TYR GLY LYS HIS
SEQRES 18 D 391 ILE ILE THR HIS ASP LEU LEU PHE THR HIS PHE GLY LEU
SEQRES 19 D 391 SER GLY PRO ALA ALA LEU ARG LEU SER SER PHE VAL LYS
SEQRES 20 D 391 GLY GLY GLU THR ILE TYR LEU ASP VAL LEU PRO GLN MET
SEQRES 21 D 391 SER GLN GLN ASP LEU ALA ASP PHE LEU GLU GLU HIS ARG
SEQRES 22 D 391 GLU LYS SER LEU LYS ASN CYS LEU LYS ILE LEU LEU PRO
SEQRES 23 D 391 GLU ARG ILE ALA ASP PHE PHE THR GLN PRO PHE PRO GLU
SEQRES 24 D 391 LYS VAL LYS GLN LEU ASN LEU SER GLU LYS GLU ALA LEU
SEQRES 25 D 391 ILE LYS GLN ILE LYS GLU LEU PRO ILE SER VAL THR GLY
SEQRES 26 D 391 LYS MET SER LEU ALA LYS SER PHE VAL THR LYS GLY GLY
SEQRES 27 D 391 VAL SER LEU LYS GLU ILE ASN PRO LYS THR LEU GLU SER
SEQRES 28 D 391 LYS LEU VAL PRO GLY LEU HIS PHE ALA GLY GLU VAL LEU
SEQRES 29 D 391 ASP ILE ASN ALA HIS THR GLY GLY PHE ASN ILE THR SER
SEQRES 30 D 391 ALA LEU CYS THR GLY TRP VAL ALA GLY SER LEU HIS TYR
SEQRES 31 D 391 ASP
HET FAD A 400 53
HET FAD B 400 53
HET FAD C 400 53
HET FAD D 400 53
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 5 FAD 4(C27 H33 N9 O15 P2)
HELIX 1 1 GLY A 12 TYR A 25 1 14
HELIX 2 2 LYS A 41 THR A 45 5 5
HELIX 3 3 THR A 45 ARG A 49 5 5
HELIX 4 4 ASN A 57 ALA A 63 1 7
HELIX 5 5 ASN A 68 PHE A 71 5 4
HELIX 6 6 LEU A 72 PHE A 79 1 8
HELIX 7 7 ASP A 80 ASN A 91 1 12
HELIX 8 8 LYS A 109 LEU A 124 1 16
HELIX 9 9 TYR A 167 GLY A 171 5 5
HELIX 10 10 GLY A 174 PHE A 183 1 10
HELIX 11 11 PRO A 202 LEU A 206 5 5
HELIX 12 12 GLY A 236 SER A 243 1 8
HELIX 13 13 SER A 261 HIS A 272 1 12
HELIX 14 14 SER A 276 LEU A 285 1 10
HELIX 15 15 PRO A 286 GLN A 295 1 10
HELIX 16 16 VAL A 301 LEU A 304 5 4
HELIX 17 17 ASN A 305 GLU A 318 1 14
HELIX 18 18 SER A 328 SER A 332 5 5
HELIX 19 19 SER A 340 GLU A 343 5 4
HELIX 20 20 GLY A 372 SER A 387 1 16
HELIX 21 21 GLY B 12 TYR B 25 1 14
HELIX 22 22 GLY B 39 GLY B 44 1 6
HELIX 23 23 ASN B 57 ILE B 65 1 9
HELIX 24 24 ASN B 68 PHE B 71 5 4
HELIX 25 25 LEU B 72 PHE B 79 1 8
HELIX 26 26 ASP B 80 GLU B 90 1 11
HELIX 27 27 SER B 110 LEU B 124 1 15
HELIX 28 28 TYR B 167 GLY B 171 5 5
HELIX 29 29 GLY B 174 PHE B 183 1 10
HELIX 30 30 PRO B 202 GLN B 207 1 6
HELIX 31 31 GLY B 236 SER B 243 1 8
HELIX 32 32 SER B 244 VAL B 246 5 3
HELIX 33 33 SER B 261 HIS B 272 1 12
HELIX 34 34 SER B 276 LYS B 282 1 7
HELIX 35 35 PRO B 286 GLN B 295 1 10
HELIX 36 36 VAL B 301 LEU B 304 5 4
HELIX 37 37 ASN B 305 GLU B 318 1 14
HELIX 38 38 GLY B 372 SER B 387 1 16
HELIX 39 39 GLY C 12 TYR C 25 1 14
HELIX 40 40 LYS C 41 THR C 45 5 5
HELIX 41 41 THR C 45 ARG C 49 5 5
HELIX 42 42 ASN C 57 GLY C 64 1 8
HELIX 43 43 ASN C 68 PHE C 71 5 4
HELIX 44 44 LEU C 72 PHE C 79 1 8
HELIX 45 45 ASP C 80 ASN C 91 1 12
HELIX 46 46 LYS C 109 LEU C 124 1 16
HELIX 47 47 TYR C 167 GLY C 171 5 5
HELIX 48 48 GLY C 174 PHE C 183 1 10
HELIX 49 49 PRO C 202 GLN C 207 1 6
HELIX 50 50 GLY C 236 SER C 243 1 8
HELIX 51 51 SER C 244 VAL C 246 5 3
HELIX 52 52 SER C 261 HIS C 272 1 12
HELIX 53 53 SER C 276 ILE C 283 1 8
HELIX 54 54 PRO C 286 GLN C 295 1 10
HELIX 55 55 VAL C 301 LEU C 304 5 4
HELIX 56 56 ASN C 305 GLU C 318 1 14
HELIX 57 57 SER C 328 SER C 332 5 5
HELIX 58 58 SER C 340 GLU C 343 5 4
HELIX 59 59 GLY C 372 SER C 387 1 16
HELIX 60 60 GLY D 12 TYR D 25 1 14
HELIX 61 61 LYS D 41 THR D 45 5 5
HELIX 62 62 ASN D 57 GLY D 64 1 8
HELIX 63 63 ASN D 68 PHE D 71 5 4
HELIX 64 64 LEU D 72 PHE D 79 1 8
HELIX 65 65 ASP D 80 GLU D 90 1 11
HELIX 66 66 LYS D 109 GLY D 125 1 17
HELIX 67 67 TYR D 167 GLY D 171 5 5
HELIX 68 68 GLY D 174 PHE D 183 1 10
HELIX 69 69 PRO D 202 LEU D 206 5 5
HELIX 70 70 GLY D 236 SER D 243 1 8
HELIX 71 71 SER D 244 VAL D 246 5 3
HELIX 72 72 SER D 261 HIS D 272 1 12
HELIX 73 73 SER D 276 ILE D 283 1 8
HELIX 74 74 PRO D 286 GLN D 295 1 10
HELIX 75 75 ASN D 305 GLU D 318 1 14
HELIX 76 76 SER D 328 SER D 332 5 5
HELIX 77 77 SER D 340 GLU D 343 5 4
HELIX 78 78 GLY D 361 VAL D 363 5 3
HELIX 79 79 GLY D 372 SER D 387 1 16
SHEET 1 AA 5 THR A 127 ILE A 129 0
SHEET 2 AA 5 THR A 29 LEU A 32 1 O THR A 29 N THR A 127
SHEET 3 AA 5 THR A 6 ILE A 9 1 O THR A 6 N LEU A 30
SHEET 4 AA 5 LYS A 157 VAL A 160 1 O LYS A 157 N ILE A 7
SHEET 5 AA 5 LEU A 357 PHE A 359 1 O HIS A 358 N VAL A 160
SHEET 1 AB 3 THR A 53 ASN A 54 0
SHEET 2 AB 3 ARG A 102 PRO A 105 -1 O VAL A 103 N THR A 53
SHEET 3 AB 3 LEU A 95 VAL A 97 -1 O LYS A 96 N PHE A 104
SHEET 1 AC 3 SER A 136 THR A 140 0
SHEET 2 AC 3 LEU A 143 ARG A 147 -1 O LEU A 143 N THR A 140
SHEET 3 AC 3 ALA A 152 CYS A 155 -1 O TRP A 153 N VAL A 146
SHEET 1 AD 2 GLU A 191 ALA A 193 0
SHEET 2 AD 2 VAL A 334 LYS A 336 -1 O VAL A 334 N ALA A 193
SHEET 1 AE 7 LEU A 197 ASP A 200 0
SHEET 2 AE 7 GLY A 233 SER A 235 -1 O LEU A 234 N LEU A 197
SHEET 3 AE 7 HIS A 221 THR A 230 -1 O LEU A 228 N SER A 235
SHEET 4 AE 7 SER A 210 TYR A 218 -1 O LEU A 211 N LEU A 227
SHEET 5 AE 7 GLU A 250 ASP A 255 -1 O TYR A 253 N SER A 217
SHEET 6 AE 7 LEU A 319 LYS A 326 -1 O LEU A 319 N LEU A 254
SHEET 7 AE 7 LEU A 197 ASP A 200 -1 O LEU A 198 N THR A 324
SHEET 1 BA 5 THR B 127 ILE B 129 0
SHEET 2 BA 5 THR B 29 LEU B 32 1 O THR B 29 N THR B 127
SHEET 3 BA 5 THR B 6 ILE B 9 1 O THR B 6 N LEU B 30
SHEET 4 BA 5 LYS B 157 VAL B 160 1 O LYS B 157 N ILE B 7
SHEET 5 BA 5 LEU B 357 PHE B 359 1 O HIS B 358 N VAL B 160
SHEET 1 BB 3 THR B 53 ASN B 54 0
SHEET 2 BB 3 ARG B 102 PRO B 105 -1 N VAL B 103 O THR B 53
SHEET 3 BB 3 LEU B 95 VAL B 97 -1 O LYS B 96 N PHE B 104
SHEET 1 BC 3 SER B 136 THR B 140 0
SHEET 2 BC 3 LEU B 143 ARG B 147 -1 O LEU B 143 N THR B 140
SHEET 3 BC 3 TRP B 153 CYS B 155 -1 O TRP B 153 N VAL B 146
SHEET 1 BD 2 GLU B 191 ALA B 193 0
SHEET 2 BD 2 VAL B 334 LYS B 336 -1 O VAL B 334 N ALA B 193
SHEET 1 BE 7 LEU B 197 ASP B 200 0
SHEET 2 BE 7 GLY B 233 SER B 235 -1 O LEU B 234 N LEU B 197
SHEET 3 BE 7 HIS B 221 PHE B 229 -1 O LEU B 228 N SER B 235
SHEET 4 BE 7 SER B 210 TYR B 218 -1 O LEU B 211 N LEU B 227
SHEET 5 BE 7 THR B 251 ASP B 255 -1 O TYR B 253 N SER B 217
SHEET 6 BE 7 LEU B 319 LYS B 326 -1 O LEU B 319 N LEU B 254
SHEET 7 BE 7 LEU B 197 ASP B 200 -1 O LEU B 198 N THR B 324
SHEET 1 CA 5 THR C 127 ILE C 129 0
SHEET 2 CA 5 THR C 29 LEU C 32 1 O THR C 29 N THR C 127
SHEET 3 CA 5 HIS C 3 ILE C 9 1 O THR C 6 N LEU C 30
SHEET 4 CA 5 ALA C 152 VAL C 160 1 O THR C 154 N PHE C 4
SHEET 5 CA 5 LEU C 357 PHE C 359 -1 O HIS C 358 N VAL C 160
SHEET 1 CB 6 THR C 127 ILE C 129 0
SHEET 2 CB 6 THR C 29 LEU C 32 1 O THR C 29 N THR C 127
SHEET 3 CB 6 HIS C 3 ILE C 9 1 O THR C 6 N LEU C 30
SHEET 4 CB 6 ALA C 152 VAL C 160 1 O THR C 154 N PHE C 4
SHEET 5 CB 6 LEU C 143 ARG C 147 -1 O PHE C 144 N CYS C 155
SHEET 6 CB 6 SER C 136 THR C 140 -1 O SER C 136 N ARG C 147
SHEET 1 CC 2 LEU C 357 PHE C 359 0
SHEET 2 CC 2 ALA C 152 VAL C 160 -1 O LEU C 158 N HIS C 358
SHEET 1 CD 3 THR C 53 ASN C 54 0
SHEET 2 CD 3 ARG C 102 PRO C 105 -1 N VAL C 103 O THR C 53
SHEET 3 CD 3 LEU C 95 VAL C 97 -1 O LYS C 96 N PHE C 104
SHEET 1 CE 2 GLU C 191 ALA C 193 0
SHEET 2 CE 2 VAL C 334 LYS C 336 -1 O VAL C 334 N ALA C 193
SHEET 1 CF 7 LEU C 197 ASP C 200 0
SHEET 2 CF 7 GLY C 233 SER C 235 -1 O LEU C 234 N LEU C 197
SHEET 3 CF 7 HIS C 221 PHE C 229 -1 O LEU C 228 N SER C 235
SHEET 4 CF 7 SER C 210 TYR C 218 -1 O LEU C 211 N LEU C 227
SHEET 5 CF 7 THR C 251 ASP C 255 -1 O TYR C 253 N SER C 217
SHEET 6 CF 7 LEU C 319 LYS C 326 -1 O LEU C 319 N LEU C 254
SHEET 7 CF 7 LEU C 197 ASP C 200 -1 O LEU C 198 N THR C 324
SHEET 1 DA 5 THR D 127 ILE D 129 0
SHEET 2 DA 5 THR D 29 LEU D 32 1 O THR D 29 N THR D 127
SHEET 3 DA 5 HIS D 3 ILE D 9 1 O THR D 6 N LEU D 30
SHEET 4 DA 5 ALA D 152 VAL D 160 1 O THR D 154 N PHE D 4
SHEET 5 DA 5 LEU D 357 PHE D 359 -1 O HIS D 358 N VAL D 160
SHEET 1 DB 6 THR D 127 ILE D 129 0
SHEET 2 DB 6 THR D 29 LEU D 32 1 O THR D 29 N THR D 127
SHEET 3 DB 6 HIS D 3 ILE D 9 1 O THR D 6 N LEU D 30
SHEET 4 DB 6 ALA D 152 VAL D 160 1 O THR D 154 N PHE D 4
SHEET 5 DB 6 PHE D 144 SER D 148 -1 O PHE D 144 N CYS D 155
SHEET 6 DB 6 ILE D 134 LYS D 138 -1 N VAL D 135 O ARG D 147
SHEET 1 DC 2 LEU D 357 PHE D 359 0
SHEET 2 DC 2 ALA D 152 VAL D 160 -1 O LEU D 158 N HIS D 358
SHEET 1 DD 3 THR D 53 ASN D 54 0
SHEET 2 DD 3 ARG D 102 PRO D 105 -1 N VAL D 103 O THR D 53
SHEET 3 DD 3 LEU D 95 VAL D 97 -1 O LYS D 96 N PHE D 104
SHEET 1 DE 2 GLU D 191 ALA D 193 0
SHEET 2 DE 2 VAL D 334 LYS D 336 -1 O VAL D 334 N ALA D 193
SHEET 1 DF 7 LEU D 197 ASP D 200 0
SHEET 2 DF 7 GLY D 233 SER D 235 -1 O LEU D 234 N LEU D 197
SHEET 3 DF 7 HIS D 221 PHE D 229 -1 O LEU D 228 N SER D 235
SHEET 4 DF 7 SER D 210 TYR D 218 -1 O LEU D 211 N LEU D 227
SHEET 5 DF 7 THR D 251 ASP D 255 -1 O TYR D 253 N SER D 217
SHEET 6 DF 7 LEU D 319 LYS D 326 -1 O LEU D 319 N LEU D 254
SHEET 7 DF 7 LEU D 197 ASP D 200 -1 O LEU D 198 N THR D 324
SITE 1 AC1 27 GLY A 10 GLY A 12 PRO A 13 ALA A 14
SITE 2 AC1 27 GLU A 33 LYS A 34 ASN A 35 LYS A 41
SITE 3 AC1 27 THR A 45 ASN A 51 THR A 132 ILE A 134
SITE 4 AC1 27 THR A 161 THR A 162 GLY A 163 TYR A 167
SITE 5 AC1 27 GLY A 171 PHE A 175 PHE A 333 GLY A 361
SITE 6 AC1 27 GLU A 362 THR A 370 GLY A 371 GLY A 372
SITE 7 AC1 27 PHE A 373 ASN A 374 ILE A 375
SITE 1 AC2 27 GLY B 10 GLY B 12 PRO B 13 ALA B 14
SITE 2 AC2 27 GLU B 33 LYS B 34 ASN B 35 LYS B 41
SITE 3 AC2 27 THR B 45 ILE B 134 THR B 161 THR B 162
SITE 4 AC2 27 GLY B 163 TYR B 167 GLY B 171 SER B 172
SITE 5 AC2 27 PHE B 175 PHE B 333 GLY B 361 GLU B 362
SITE 6 AC2 27 THR B 370 GLY B 371 GLY B 372 PHE B 373
SITE 7 AC2 27 ASN B 374 ILE B 375 ALA B 378
SITE 1 AC3 28 GLY C 10 GLY C 12 PRO C 13 ALA C 14
SITE 2 AC3 28 GLU C 33 LYS C 34 ASN C 35 LYS C 41
SITE 3 AC3 28 THR C 45 GLY C 46 THR C 132 ILE C 134
SITE 4 AC3 28 THR C 161 THR C 162 GLY C 163 TYR C 167
SITE 5 AC3 28 THR C 170 GLY C 171 PHE C 175 PHE C 333
SITE 6 AC3 28 GLY C 361 GLU C 362 THR C 370 GLY C 371
SITE 7 AC3 28 GLY C 372 PHE C 373 ASN C 374 ILE C 375
SITE 1 AC4 26 GLY D 10 GLY D 12 PRO D 13 ALA D 14
SITE 2 AC4 26 LEU D 32 GLU D 33 LYS D 34 ASN D 35
SITE 3 AC4 26 LYS D 41 THR D 45 ILE D 134 THR D 161
SITE 4 AC4 26 THR D 162 GLY D 163 TYR D 167 GLY D 171
SITE 5 AC4 26 PHE D 175 PHE D 333 GLY D 361 GLU D 362
SITE 6 AC4 26 THR D 370 GLY D 371 GLY D 372 PHE D 373
SITE 7 AC4 26 ASN D 374 ILE D 375
CRYST1 79.149 130.346 224.199 90.00 90.00 90.00 P 2 21 21 16
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 0.012634 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007672 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004460 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
