HEADER OXIDOREDUCTASE 11-APR-11 2YG4
TITLE STRUCTURE-BASED REDESIGN OF COFACTOR BINDING IN PUTRESCINE OXIDASE:
TITLE 2 WILD TYPE BOUND TO PUTRESCINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTRESCINE OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.4.3.10;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RHODOCOCCUS ERYTHROPOLIS;
SOURCE 3 ORGANISM_TAXID: 1833;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 83333;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: K-12;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: TOP10
KEYWDS OXIDOREDUCTASE, FLAVIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.M.KOPACZ,S.ROVIDA,E.VAN DUIJN,M.W.FRAAIJE,A.MATTEVI
REVDAT 2 20-DEC-23 2YG4 1 REMARK
REVDAT 1 18-MAY-11 2YG4 0
JRNL AUTH M.M.KOPACZ,S.ROVIDA,E.VAN DUIJN,M.W.FRAAIJE,A.MATTEVI
JRNL TITL STRUCTURE-BASED REDESIGN OF COFACTOR BINDING IN PUTRESCINE
JRNL TITL 2 OXIDASE.
JRNL REF BIOCHEMISTRY V. 50 4209 2011
JRNL REFN ISSN 0006-2960
JRNL PMID 21486042
JRNL DOI 10.1021/BI200372U
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.61
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 63019
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) : 0.159
REMARK 3 R VALUE (WORKING SET) : 0.157
REMARK 3 FREE R VALUE : 0.197
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3330
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4558
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.1950
REMARK 3 BIN FREE R VALUE SET COUNT : 231
REMARK 3 BIN FREE R VALUE : 0.2490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6906
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 162
REMARK 3 SOLVENT ATOMS : 705
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.82000
REMARK 3 B22 (A**2) : -0.64000
REMARK 3 B33 (A**2) : -0.18000
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): 0.183
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.163
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.104
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.288
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7203 ; 0.023 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9793 ; 1.985 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 897 ; 6.317 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 334 ;37.941 ;23.772
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1120 ;15.049 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;18.821 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1071 ; 0.137 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5482 ; 0.010 ; 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): 4453 ; 1.024 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 7114 ; 1.918 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2750 ; 3.603 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2679 ; 5.615 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): 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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 460 1
REMARK 3 1 B 1 B 460 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 3445 ; 0.00 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 B (A): 3445 ; 0.00 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 3445 ; 0.00 ; 0.50
REMARK 3 TIGHT THERMAL 1 B (A**2): 3445 ; 0.00 ; 0.50
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 : 1.40
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 2YG4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1290047996.
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 : 6.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 66382
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 34.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.01000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.40
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.39000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 2YG3
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.4
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
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+1/2,Y+1/2,-Z
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 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 99.29500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.30500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 99.29500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.30500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 9380 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.5 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 VAL A 1
REMARK 465 SER A 451
REMARK 465 LYS A 452
REMARK 465 ALA A 453
REMARK 465 VAL B 1
REMARK 465 LYS B 452
REMARK 465 ALA B 453
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 OE2 GLU A 302 O HOH A 2301 1.41
REMARK 500 O SER B 451 O HOH B 2299 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 64 CB ASP A 64 CG 0.131
REMARK 500 GLU A 302 CB GLU A 302 CG 0.138
REMARK 500 GLU A 302 CG GLU A 302 CD 0.123
REMARK 500 GLU A 356 CG GLU A 356 CD 0.096
REMARK 500 GLU B 242 CG GLU B 242 CD 0.093
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 25 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 25 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP A 64 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG A 99 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 MET A 115 CG - SD - CE ANGL. DEV. = -15.9 DEGREES
REMARK 500 ARG A 141 CG - CD - NE ANGL. DEV. = 13.4 DEGREES
REMARK 500 ARG A 141 NE - CZ - NH1 ANGL. DEV. = -5.3 DEGREES
REMARK 500 ARG A 259 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG A 259 NE - CZ - NH2 ANGL. DEV. = -3.0 DEGREES
REMARK 500 ARG A 280 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 281 CG - CD - NE ANGL. DEV. = -13.1 DEGREES
REMARK 500 ARG A 281 NE - CZ - NH1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 ARG A 281 NE - CZ - NH2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 ARG A 335 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG A 368 NE - CZ - NH1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 25 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 280 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG B 281 CG - CD - NE ANGL. DEV. = -15.7 DEGREES
REMARK 500 ARG B 281 NE - CZ - NH1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 ARG B 281 NE - CZ - NH2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 ASP B 348 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG B 368 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 412 NE - CZ - NH2 ANGL. DEV. = -3.7 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 ALA A 13 48.79 -104.24
REMARK 500 GLN A 59 -21.32 -152.55
REMARK 500 GLU A 133 68.85 -155.98
REMARK 500 MET A 173 -64.37 -130.77
REMARK 500 SER A 195 165.40 167.41
REMARK 500 PHE A 204 -66.79 -94.54
REMARK 500 ALA A 263 53.80 -105.31
REMARK 500 ASP A 344 -121.02 43.49
REMARK 500 THR A 391 -68.72 -128.38
REMARK 500 ARG A 392 22.72 82.06
REMARK 500 ALA A 427 -102.30 -97.27
REMARK 500 TYR A 430 127.21 -32.34
REMARK 500 GLN A 431 -4.97 72.44
REMARK 500 ALA B 13 46.84 -107.87
REMARK 500 GLN B 59 -32.99 -154.05
REMARK 500 ARG B 84 15.32 -141.60
REMARK 500 GLU B 133 61.91 -150.20
REMARK 500 MET B 173 -64.00 -132.26
REMARK 500 PHE B 204 -64.61 -96.43
REMARK 500 ALA B 263 56.68 -99.78
REMARK 500 ASP B 344 -112.24 38.75
REMARK 500 THR B 391 -71.67 -129.04
REMARK 500 ARG B 392 22.75 88.78
REMARK 500 ALA B 427 -97.37 -89.83
REMARK 500 TYR B 430 128.08 -27.96
REMARK 500 GLN B 431 -7.25 74.64
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 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4HA A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4HA B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1451
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1452
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1453
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1454
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1455
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 1452
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1453
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1454
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2YG3 RELATED DB: PDB
REMARK 900 STRUCTURE-BASED REDESIGN OF COFACTOR BINDING IN PUTRESCINE OXIDASE:
REMARK 900 WILD TYPE ENZYME
REMARK 900 RELATED ID: 2YG5 RELATED DB: PDB
REMARK 900 STRUCTURE-BASED REDESIGN OF COFACTOR BINDING IN PUTRESCINE OXIDASE:
REMARK 900 A394C MUTANT
REMARK 900 RELATED ID: 2YG6 RELATED DB: PDB
REMARK 900 STRUCTURE-BASED REDESIGN OF COFACTOR BINDING IN PUTRESCINE OXIDASE:
REMARK 900 P15I-A394C DOUBLE MUTANT
REMARK 900 RELATED ID: 2YG7 RELATED DB: PDB
REMARK 900 STRUCTURE-BASED REDESIGN OF COFACTOR BINDING IN PUTRESCINE OXIDASE:
REMARK 900 A394C-A396T-Q431G TRIPLE MUTANT
DBREF 2YG4 A 1 453 UNP B0F9F6 B0F9F6_RHOER 1 453
DBREF 2YG4 B 1 453 UNP B0F9F6 B0F9F6_RHOER 1 453
SEQRES 1 A 453 VAL PRO THR LEU GLN ARG ASP VAL ALA ILE VAL GLY ALA
SEQRES 2 A 453 GLY PRO SER GLY LEU ALA ALA ALA THR ALA LEU ARG LYS
SEQRES 3 A 453 ALA GLY LEU SER VAL ALA VAL ILE GLU ALA ARG ASP ARG
SEQRES 4 A 453 VAL GLY GLY ARG THR TRP THR ASP THR ILE ASP GLY ALA
SEQRES 5 A 453 VAL LEU GLU ILE GLY GLY GLN TRP VAL SER PRO ASP GLN
SEQRES 6 A 453 THR ALA LEU ILE SER LEU LEU ASP GLU LEU GLY LEU LYS
SEQRES 7 A 453 THR PHE GLU ARG TYR ARG GLU GLY GLU SER VAL TYR ILE
SEQRES 8 A 453 SER SER ALA GLY GLU ARG THR ARG TYR THR GLY ASP SER
SEQRES 9 A 453 PHE PRO THR ASN GLU THR THR LYS LYS GLU MET ASP ARG
SEQRES 10 A 453 LEU ILE ASP GLU MET ASP ASP LEU ALA ALA GLN ILE GLY
SEQRES 11 A 453 ALA GLU GLU PRO TRP ALA HIS PRO LEU ALA ARG ASP LEU
SEQRES 12 A 453 ASP THR VAL SER PHE LYS GLN TRP LEU ILE ASN GLN SER
SEQRES 13 A 453 ASP ASP ALA GLU ALA ARG ASP ASN ILE GLY LEU PHE ILE
SEQRES 14 A 453 ALA GLY GLY MET LEU THR LYS PRO ALA HIS SER PHE SER
SEQRES 15 A 453 ALA LEU GLN ALA VAL LEU MET ALA ALA SER ALA GLY SER
SEQRES 16 A 453 PHE SER HIS LEU VAL ASP GLU ASP PHE ILE LEU ASP LYS
SEQRES 17 A 453 ARG VAL ILE GLY GLY MET GLN GLN VAL SER ILE ARG MET
SEQRES 18 A 453 ALA GLU ALA LEU GLY ASP ASP VAL PHE LEU ASN ALA PRO
SEQRES 19 A 453 VAL ARG THR VAL LYS TRP ASN GLU SER GLY ALA THR VAL
SEQRES 20 A 453 LEU ALA ASP GLY ASP ILE ARG VAL GLU ALA SER ARG VAL
SEQRES 21 A 453 ILE LEU ALA VAL PRO PRO ASN LEU TYR SER ARG ILE SER
SEQRES 22 A 453 TYR ASP PRO PRO LEU PRO ARG ARG GLN HIS GLN MET HIS
SEQRES 23 A 453 GLN HIS GLN SER LEU GLY LEU VAL ILE LYS VAL HIS ALA
SEQRES 24 A 453 VAL TYR GLU THR PRO PHE TRP ARG GLU ASP GLY LEU SER
SEQRES 25 A 453 GLY THR GLY PHE GLY ALA SER GLU VAL VAL GLN GLU VAL
SEQRES 26 A 453 TYR ASP ASN THR ASN HIS GLU ASP ASP ARG GLY THR LEU
SEQRES 27 A 453 VAL ALA PHE VAL SER ASP GLU LYS ALA ASP ALA MET PHE
SEQRES 28 A 453 GLU LEU SER ALA GLU GLU ARG LYS ALA THR ILE LEU ALA
SEQRES 29 A 453 SER LEU ALA ARG TYR LEU GLY PRO LYS ALA GLU GLU PRO
SEQRES 30 A 453 VAL VAL TYR TYR GLU SER ASP TRP GLY SER GLU GLU TRP
SEQRES 31 A 453 THR ARG GLY ALA TYR ALA ALA SER PHE ASP LEU GLY GLY
SEQRES 32 A 453 LEU HIS ARG TYR GLY ALA ASP SER ARG THR PRO VAL GLY
SEQRES 33 A 453 PRO ILE HIS PHE SER CYS SER ASP ILE ALA ALA GLU GLY
SEQRES 34 A 453 TYR GLN HIS VAL ASP GLY ALA VAL ARG MET GLY GLN ARG
SEQRES 35 A 453 THR ALA ALA ASP ILE ILE ALA ARG SER LYS ALA
SEQRES 1 B 453 VAL PRO THR LEU GLN ARG ASP VAL ALA ILE VAL GLY ALA
SEQRES 2 B 453 GLY PRO SER GLY LEU ALA ALA ALA THR ALA LEU ARG LYS
SEQRES 3 B 453 ALA GLY LEU SER VAL ALA VAL ILE GLU ALA ARG ASP ARG
SEQRES 4 B 453 VAL GLY GLY ARG THR TRP THR ASP THR ILE ASP GLY ALA
SEQRES 5 B 453 VAL LEU GLU ILE GLY GLY GLN TRP VAL SER PRO ASP GLN
SEQRES 6 B 453 THR ALA LEU ILE SER LEU LEU ASP GLU LEU GLY LEU LYS
SEQRES 7 B 453 THR PHE GLU ARG TYR ARG GLU GLY GLU SER VAL TYR ILE
SEQRES 8 B 453 SER SER ALA GLY GLU ARG THR ARG TYR THR GLY ASP SER
SEQRES 9 B 453 PHE PRO THR ASN GLU THR THR LYS LYS GLU MET ASP ARG
SEQRES 10 B 453 LEU ILE ASP GLU MET ASP ASP LEU ALA ALA GLN ILE GLY
SEQRES 11 B 453 ALA GLU GLU PRO TRP ALA HIS PRO LEU ALA ARG ASP LEU
SEQRES 12 B 453 ASP THR VAL SER PHE LYS GLN TRP LEU ILE ASN GLN SER
SEQRES 13 B 453 ASP ASP ALA GLU ALA ARG ASP ASN ILE GLY LEU PHE ILE
SEQRES 14 B 453 ALA GLY GLY MET LEU THR LYS PRO ALA HIS SER PHE SER
SEQRES 15 B 453 ALA LEU GLN ALA VAL LEU MET ALA ALA SER ALA GLY SER
SEQRES 16 B 453 PHE SER HIS LEU VAL ASP GLU ASP PHE ILE LEU ASP LYS
SEQRES 17 B 453 ARG VAL ILE GLY GLY MET GLN GLN VAL SER ILE ARG MET
SEQRES 18 B 453 ALA GLU ALA LEU GLY ASP ASP VAL PHE LEU ASN ALA PRO
SEQRES 19 B 453 VAL ARG THR VAL LYS TRP ASN GLU SER GLY ALA THR VAL
SEQRES 20 B 453 LEU ALA ASP GLY ASP ILE ARG VAL GLU ALA SER ARG VAL
SEQRES 21 B 453 ILE LEU ALA VAL PRO PRO ASN LEU TYR SER ARG ILE SER
SEQRES 22 B 453 TYR ASP PRO PRO LEU PRO ARG ARG GLN HIS GLN MET HIS
SEQRES 23 B 453 GLN HIS GLN SER LEU GLY LEU VAL ILE LYS VAL HIS ALA
SEQRES 24 B 453 VAL TYR GLU THR PRO PHE TRP ARG GLU ASP GLY LEU SER
SEQRES 25 B 453 GLY THR GLY PHE GLY ALA SER GLU VAL VAL GLN GLU VAL
SEQRES 26 B 453 TYR ASP ASN THR ASN HIS GLU ASP ASP ARG GLY THR LEU
SEQRES 27 B 453 VAL ALA PHE VAL SER ASP GLU LYS ALA ASP ALA MET PHE
SEQRES 28 B 453 GLU LEU SER ALA GLU GLU ARG LYS ALA THR ILE LEU ALA
SEQRES 29 B 453 SER LEU ALA ARG TYR LEU GLY PRO LYS ALA GLU GLU PRO
SEQRES 30 B 453 VAL VAL TYR TYR GLU SER ASP TRP GLY SER GLU GLU TRP
SEQRES 31 B 453 THR ARG GLY ALA TYR ALA ALA SER PHE ASP LEU GLY GLY
SEQRES 32 B 453 LEU HIS ARG TYR GLY ALA ASP SER ARG THR PRO VAL GLY
SEQRES 33 B 453 PRO ILE HIS PHE SER CYS SER ASP ILE ALA ALA GLU GLY
SEQRES 34 B 453 TYR GLN HIS VAL ASP GLY ALA VAL ARG MET GLY GLN ARG
SEQRES 35 B 453 THR ALA ALA ASP ILE ILE ALA ARG SER LYS ALA
HET FAD A 600 53
HET 4HA A 601 6
HET GOL A1451 6
HET GOL A1452 6
HET SO4 A1453 5
HET SO4 A1454 5
HET GOL A1455 6
HET FAD B 600 53
HET 4HA B 601 6
HET GOL B1452 6
HET SO4 B1453 5
HET SO4 B1454 5
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM 4HA 4-HYDROXYBUTAN-1-AMINIUM
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 4HA 2(C4 H12 N O 1+)
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 7 SO4 4(O4 S 2-)
FORMUL 15 HOH *705(H2 O)
HELIX 1 1 GLY A 14 ALA A 27 1 14
HELIX 2 2 GLN A 65 LEU A 75 1 11
HELIX 3 3 ASN A 108 GLY A 130 1 23
HELIX 4 4 GLU A 133 HIS A 137 5 5
HELIX 5 5 LEU A 139 THR A 145 1 7
HELIX 6 6 SER A 147 SER A 156 1 10
HELIX 7 7 ASP A 158 ALA A 170 1 13
HELIX 8 8 GLY A 171 THR A 175 1 5
HELIX 9 9 SER A 182 ALA A 193 1 12
HELIX 10 10 SER A 195 ASP A 201 1 7
HELIX 11 11 ASP A 201 LEU A 206 1 6
HELIX 12 12 MET A 214 GLY A 226 1 13
HELIX 13 13 PRO A 265 ILE A 272 5 8
HELIX 14 14 PRO A 279 HIS A 288 1 10
HELIX 15 15 PRO A 304 ASP A 309 1 6
HELIX 16 16 ASP A 344 LEU A 353 1 10
HELIX 17 17 SER A 354 GLY A 371 1 18
HELIX 18 18 PRO A 372 GLU A 376 5 5
HELIX 19 19 GLY A 402 GLY A 408 1 7
HELIX 20 20 ALA A 409 SER A 411 5 3
HELIX 21 21 CYS A 422 ALA A 426 5 5
HELIX 22 22 HIS A 432 ARG A 450 1 19
HELIX 23 23 GLY B 14 ALA B 27 1 14
HELIX 24 24 GLN B 65 LEU B 75 1 11
HELIX 25 25 ASN B 108 GLY B 130 1 23
HELIX 26 26 GLU B 133 HIS B 137 5 5
HELIX 27 27 LEU B 139 THR B 145 1 7
HELIX 28 28 SER B 147 SER B 156 1 10
HELIX 29 29 ASP B 158 ALA B 170 1 13
HELIX 30 30 GLY B 171 THR B 175 1 5
HELIX 31 31 SER B 182 ALA B 193 1 12
HELIX 32 32 SER B 195 ASP B 201 1 7
HELIX 33 33 ASP B 201 LEU B 206 1 6
HELIX 34 34 MET B 214 GLY B 226 1 13
HELIX 35 35 PRO B 265 ILE B 272 5 8
HELIX 36 36 PRO B 279 HIS B 288 1 10
HELIX 37 37 PRO B 304 ASP B 309 5 6
HELIX 38 38 ASP B 344 GLU B 352 1 9
HELIX 39 39 SER B 354 GLY B 371 1 18
HELIX 40 40 PRO B 372 GLU B 376 5 5
HELIX 41 41 GLY B 402 GLY B 408 1 7
HELIX 42 42 ALA B 409 SER B 411 5 3
HELIX 43 43 CYS B 422 ALA B 426 5 5
HELIX 44 44 HIS B 432 SER B 451 1 20
SHEET 1 AA 5 VAL A 229 PHE A 230 0
SHEET 2 AA 5 VAL A 31 ILE A 34 1 O VAL A 33 N PHE A 230
SHEET 3 AA 5 THR A 3 VAL A 11 1 O VAL A 8 N ALA A 32
SHEET 4 AA 5 ILE A 253 LEU A 262 1 O ARG A 254 N LEU A 4
SHEET 5 AA 5 ILE A 418 PHE A 420 -1 O HIS A 419 N LEU A 262
SHEET 1 AB 7 VAL A 229 PHE A 230 0
SHEET 2 AB 7 VAL A 31 ILE A 34 1 O VAL A 33 N PHE A 230
SHEET 3 AB 7 THR A 3 VAL A 11 1 O VAL A 8 N ALA A 32
SHEET 4 AB 7 ILE A 253 LEU A 262 1 O ARG A 254 N LEU A 4
SHEET 5 AB 7 GLY A 244 ALA A 249 -1 O ALA A 245 N ALA A 257
SHEET 6 AB 7 VAL A 235 ASN A 241 -1 N ARG A 236 O LEU A 248
SHEET 7 AB 7 SER A 273 ASP A 275 1 O SER A 273 N VAL A 238
SHEET 1 AC 2 ILE A 418 PHE A 420 0
SHEET 2 AC 2 ILE A 253 LEU A 262 -1 O VAL A 260 N HIS A 419
SHEET 1 AD 2 THR A 46 ILE A 49 0
SHEET 2 AD 2 ALA A 52 GLU A 55 -1 O ALA A 52 N ILE A 49
SHEET 1 AE 2 THR A 79 GLU A 81 0
SHEET 2 AE 2 LYS A 208 VAL A 210 -1 O ARG A 209 N PHE A 80
SHEET 1 AF 7 ARG A 97 TYR A 100 0
SHEET 2 AF 7 GLU A 87 ILE A 91 -1 O SER A 88 N TYR A 100
SHEET 3 AF 7 LEU A 311 PHE A 316 1 N SER A 312 O GLU A 87
SHEET 4 AF 7 GLU A 324 ASP A 327 -1 O VAL A 325 N GLY A 315
SHEET 5 AF 7 GLY A 336 SER A 343 -1 O VAL A 339 N TYR A 326
SHEET 6 AF 7 VAL A 294 TYR A 301 -1 O ILE A 295 N VAL A 342
SHEET 7 AF 7 VAL A 379 SER A 383 -1 O VAL A 379 N VAL A 300
SHEET 1 AG 2 GLN A 289 LEU A 291 0
SHEET 2 AG 2 ALA A 397 PHE A 399 -1 O SER A 398 N SER A 290
SHEET 1 BA 5 VAL B 229 PHE B 230 0
SHEET 2 BA 5 VAL B 31 ILE B 34 1 O VAL B 33 N PHE B 230
SHEET 3 BA 5 THR B 3 VAL B 11 1 O VAL B 8 N ALA B 32
SHEET 4 BA 5 ILE B 253 LEU B 262 1 O ARG B 254 N LEU B 4
SHEET 5 BA 5 ILE B 418 PHE B 420 -1 O HIS B 419 N LEU B 262
SHEET 1 BB 7 VAL B 229 PHE B 230 0
SHEET 2 BB 7 VAL B 31 ILE B 34 1 O VAL B 33 N PHE B 230
SHEET 3 BB 7 THR B 3 VAL B 11 1 O VAL B 8 N ALA B 32
SHEET 4 BB 7 ILE B 253 LEU B 262 1 O ARG B 254 N LEU B 4
SHEET 5 BB 7 GLY B 244 ALA B 249 -1 O ALA B 245 N ALA B 257
SHEET 6 BB 7 VAL B 235 ASN B 241 -1 N ARG B 236 O LEU B 248
SHEET 7 BB 7 SER B 273 ASP B 275 1 O SER B 273 N VAL B 238
SHEET 1 BC 2 ILE B 418 PHE B 420 0
SHEET 2 BC 2 ILE B 253 LEU B 262 -1 O VAL B 260 N HIS B 419
SHEET 1 BD 2 THR B 46 ILE B 49 0
SHEET 2 BD 2 ALA B 52 GLU B 55 -1 O ALA B 52 N ILE B 49
SHEET 1 BE 2 THR B 79 GLU B 81 0
SHEET 2 BE 2 LYS B 208 VAL B 210 -1 O ARG B 209 N PHE B 80
SHEET 1 BF 7 ARG B 97 TYR B 100 0
SHEET 2 BF 7 GLU B 87 ILE B 91 -1 O SER B 88 N TYR B 100
SHEET 3 BF 7 LEU B 311 PHE B 316 1 N SER B 312 O GLU B 87
SHEET 4 BF 7 GLU B 324 ASP B 327 -1 O VAL B 325 N GLY B 315
SHEET 5 BF 7 GLY B 336 SER B 343 -1 O VAL B 339 N TYR B 326
SHEET 6 BF 7 VAL B 294 TYR B 301 -1 O ILE B 295 N VAL B 342
SHEET 7 BF 7 VAL B 379 SER B 383 -1 O VAL B 379 N VAL B 300
SHEET 1 BG 2 GLN B 289 LEU B 291 0
SHEET 2 BG 2 ALA B 397 PHE B 399 -1 O SER B 398 N SER B 290
CISPEP 1 ASP A 275 PRO A 276 0 2.21
CISPEP 2 ALA A 394 TYR A 395 0 -0.47
CISPEP 3 ASP B 275 PRO B 276 0 5.41
CISPEP 4 ALA B 394 TYR B 395 0 -4.41
SITE 1 AC1 35 VAL A 11 GLY A 12 GLY A 14 PRO A 15
SITE 2 AC1 35 SER A 16 ILE A 34 GLU A 35 ALA A 36
SITE 3 AC1 35 ARG A 37 GLY A 41 GLY A 42 ARG A 43
SITE 4 AC1 35 GLY A 57 GLY A 58 GLN A 59 TRP A 60
SITE 5 AC1 35 VAL A 235 ALA A 263 VAL A 264 TRP A 385
SITE 6 AC1 35 TRP A 390 TYR A 395 CYS A 422 SER A 423
SITE 7 AC1 35 GLN A 431 HIS A 432 VAL A 433 ALA A 436
SITE 8 AC1 35 HOH A2010 HOH A2025 HOH A2030 HOH A2077
SITE 9 AC1 35 HOH A2260 HOH A2299 4HA B 601
SITE 1 AC2 7 HOH A2395 HOH A2396 GLY B 172 GLU B 324
SITE 2 AC2 7 TYR B 395 HIS B 432 FAD B 600
SITE 1 AC3 36 4HA A 601 VAL B 11 GLY B 12 GLY B 14
SITE 2 AC3 36 PRO B 15 SER B 16 ILE B 34 GLU B 35
SITE 3 AC3 36 ALA B 36 ARG B 37 GLY B 41 GLY B 42
SITE 4 AC3 36 ARG B 43 THR B 44 GLY B 57 GLY B 58
SITE 5 AC3 36 GLN B 59 TRP B 60 VAL B 235 ALA B 263
SITE 6 AC3 36 VAL B 264 TRP B 385 TRP B 390 ALA B 394
SITE 7 AC3 36 TYR B 395 CYS B 422 SER B 423 GLN B 431
SITE 8 AC3 36 HIS B 432 VAL B 433 ALA B 436 HOH B2009
SITE 9 AC3 36 HOH B2023 HOH B2027 HOH B2061 HOH B2209
SITE 1 AC4 6 GLY A 172 GLU A 324 TYR A 395 FAD A 600
SITE 2 AC4 6 HOH A2387 HOH B2303
SITE 1 AC5 8 ALA A 131 GLU A 132 TRP A 135 SER A 411
SITE 2 AC5 8 ARG A 412 ALA A 426 TYR A 430 HOH A2397
SITE 1 AC6 5 ARG A 412 HIS A 419 PHE A 420 ARG A 442
SITE 2 AC6 5 ASP A 446
SITE 1 AC7 2 ARG A 141 HOH A2398
SITE 1 AC8 5 LEU A 353 ALA A 355 ARG A 358 HOH A2328
SITE 2 AC8 5 HOH A2329
SITE 1 AC9 5 VAL A 53 GLY A 212 ASN A 330 HOH A2316
SITE 2 AC9 5 HOH A2399
SITE 1 BC1 7 ARG B 412 HIS B 419 PHE B 420 MET B 439
SITE 2 BC1 7 THR B 443 ASP B 446 HOH B2304
SITE 1 BC2 6 ASP A 348 PHE A 351 ARG B 280 ARG B 281
SITE 2 BC2 6 HOH B2216 HOH B2305
SITE 1 BC3 5 HOH A2278 LEU B 353 ALA B 355 ARG B 358
SITE 2 BC3 5 HOH B2306
CRYST1 198.590 80.610 92.120 90.00 90.00 90.00 P 21 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.005036 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012405 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010855 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
