HEADER OXIDOREDUCTASE 14-JUN-10 3NH3
TITLE COMPLEX OF 6-HYDROXY-L-NICOTINE OXIDASE WITH FINAL KETONE PRODUCT
TITLE 2 FORMED DURING CATALYTIC TURNOVER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 6-HYDROXY-L-NICOTINE OXIDASE;
COMPND 3 CHAIN: X;
COMPND 4 EC: 1.5.3.5;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARTHROBACTER NICOTINOVORANS;
SOURCE 3 ORGANISM_TAXID: 29320;
SOURCE 4 GENE: 6-HLNO;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM105;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRC99A
KEYWDS ENANTHIOMERIC SUBSTRATE-INHIBITOR, FLAVOENZYMES, NICOTINE
KEYWDS 2 DEGRADATION, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.S.KACHALOVA,H.D.BARTUNIK
REVDAT 4 06-SEP-23 3NH3 1 REMARK SEQADV
REVDAT 3 08-NOV-17 3NH3 1 REMARK
REVDAT 2 10-AUG-11 3NH3 1 JRNL VERSN
REVDAT 1 23-MAR-11 3NH3 0
JRNL AUTH G.S.KACHALOVA,G.P.BOURENKOV,T.MENGESDORF,S.SCHENK,H.R.MAUN,
JRNL AUTH 2 M.BURGHAMMER,C.RIEKEL,K.DECKER,H.D.BARTUNIK
JRNL TITL CRYSTAL STRUCTURE ANALYSIS OF FREE AND SUBSTRATE-BOUND
JRNL TITL 2 6-HYDROXY-L-NICOTINE OXIDASE FROM ARTHROBACTER
JRNL TITL 3 NICOTINOVORANS.
JRNL REF J.MOL.BIOL. V. 396 785 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20006620
JRNL DOI 10.1016/J.JMB.2009.12.009
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.S.KACHALOVA,G.P.BOURENKOV,T.MENGESDORF,S.SCHENK,H.R.MAUN,
REMARK 1 AUTH 2 M.BURGHAMMER,C.RIEKEL,K.DECKER,H.D.BARTUNIK
REMARK 1 TITL CRYSTAL STRUCTURE ANALYSIS OF FREE AND SUBSTRATE-BOUND
REMARK 1 TITL 2 6-HYDROXY-L-NICOTINE FROM ARTHROBACTER NICOTINOVORANS
REMARK 1 REF J.MOL.BIOL. V. 396 785 2010
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 12.22
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 41266
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) : 0.161
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.204
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2184
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2918
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 BIN R VALUE (WORKING SET) : 0.2120
REMARK 3 BIN FREE R VALUE SET COUNT : 165
REMARK 3 BIN FREE R VALUE : 0.2610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3270
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 123
REMARK 3 SOLVENT ATOMS : 393
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.53
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.133
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.087
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.264
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3526 ; 0.031 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4800 ; 2.369 ; 2.000
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 434 ; 6.630 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 156 ;40.207 ;23.462
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 536 ;16.248 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;19.739 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 522 ; 0.208 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2692 ; 0.014 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1710 ; 0.242 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2375 ; 0.327 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 334 ; 0.218 ; 0.200
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): 60 ; 0.392 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 39 ; 0.519 ; 0.200
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): 2201 ; 1.846 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3407 ; 2.740 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1603 ; 4.484 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1388 ; 6.741 ; 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 : 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 : BABINET MODEL WITH 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: NULL
REMARK 4
REMARK 4 3NH3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-10.
REMARK 100 THE DEPOSITION ID IS D_1000059820.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAR-03
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.05
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 43679
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.500
REMARK 200 R MERGE (I) : 0.11600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.14
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.50
REMARK 200 R MERGE FOR SHELL (I) : 0.70400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
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: PDB CODE 3K7M
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 67.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.83
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM SODIUM PHOSPHATE; 4M SODIUM
REMARK 280 FORMIATE, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 3 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 Y,X,-Z
REMARK 290 14555 -Y,-X,-Z
REMARK 290 15555 Y,-X,Z
REMARK 290 16555 -Y,X,Z
REMARK 290 17555 X,Z,-Y
REMARK 290 18555 -X,Z,Y
REMARK 290 19555 -X,-Z,-Y
REMARK 290 20555 X,-Z,Y
REMARK 290 21555 Z,Y,-X
REMARK 290 22555 Z,-Y,X
REMARK 290 23555 -Z,Y,X
REMARK 290 24555 -Z,-Y,-X
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 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 14 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 15 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 17 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 19 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 19 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 20 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 21 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 21 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 22 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 22 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 23 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 24 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 24 -1.000000 0.000000 0.000000 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: 1230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32590 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 163.05100
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 HIS X 426
REMARK 465 HIS X 427
REMARK 465 HIS X 428
REMARK 465 HIS X 429
REMARK 465 HIS X 430
REMARK 465 HIS X 431
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 SER X 425 CB OG
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER X 12 CA CB OG
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 CB ALA X 82 O HOH X 464 1.16
REMARK 500 OE2 GLU X 300 C12 HNM X 436 2.11
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 X 58 -39.08 -146.90
REMARK 500 ARG X 91 76.83 -116.54
REMARK 500 HIS X 187 43.06 -93.51
REMARK 500 TYR X 313 -60.74 -125.10
REMARK 500 THR X 327 -150.79 -148.60
REMARK 500 PHE X 367 -53.36 -144.22
REMARK 500 PRO X 370 -137.94 -81.65
REMARK 500 HIS X 383 -58.34 -144.80
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 GP7 X 435
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HNL X 433
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD X 434
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GP7 X 435
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HNM X 436
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3NGC RELATED DB: PDB
REMARK 900 RELATED ID: 3NHO RELATED DB: PDB
REMARK 900 RELATED ID: 3NK0 RELATED DB: PDB
REMARK 900 RELATED ID: 3NK1 RELATED DB: PDB
REMARK 900 RELATED ID: 3NK2 RELATED DB: PDB
REMARK 900 RELATED ID: 3NN0 RELATED DB: PDB
REMARK 900 RELATED ID: 3NN6 RELATED DB: PDB
REMARK 900 RELATED ID: 3K7Q RELATED DB: PDB
REMARK 900 RELATED ID: 3K7M RELATED DB: PDB
DBREF 3NH3 X 1 425 UNP Q93NH4 Q93NH4_ARTNI 1 425
SEQADV 3NH3 HIS X 426 UNP Q93NH4 EXPRESSION TAG
SEQADV 3NH3 HIS X 427 UNP Q93NH4 EXPRESSION TAG
SEQADV 3NH3 HIS X 428 UNP Q93NH4 EXPRESSION TAG
SEQADV 3NH3 HIS X 429 UNP Q93NH4 EXPRESSION TAG
SEQADV 3NH3 HIS X 430 UNP Q93NH4 EXPRESSION TAG
SEQADV 3NH3 HIS X 431 UNP Q93NH4 EXPRESSION TAG
SEQRES 1 X 431 MET TYR ASP ALA ILE VAL VAL GLY GLY GLY PHE SER GLY
SEQRES 2 X 431 LEU LYS ALA ALA ARG ASP LEU THR ASN ALA GLY LYS LYS
SEQRES 3 X 431 VAL LEU LEU LEU GLU GLY GLY GLU ARG LEU GLY GLY ARG
SEQRES 4 X 431 ALA TYR SER ARG GLU SER ARG ASN VAL PRO GLY LEU ARG
SEQRES 5 X 431 VAL GLU ILE GLY GLY ALA TYR LEU HIS ARG LYS HIS HIS
SEQRES 6 X 431 PRO ARG LEU ALA ALA GLU LEU ASP ARG TYR GLY ILE PRO
SEQRES 7 X 431 THR ALA ALA ALA SER GLU PHE THR SER PHE ARG HIS ARG
SEQRES 8 X 431 LEU GLY PRO THR ALA VAL ASP GLN ALA PHE PRO ILE PRO
SEQRES 9 X 431 GLY SER GLU ALA VAL ALA VAL GLU ALA ALA THR TYR THR
SEQRES 10 X 431 LEU LEU ARG ASP ALA HIS ARG ILE ASP LEU GLU LYS GLY
SEQRES 11 X 431 LEU GLU ASN GLN ASP LEU GLU ASP LEU ASP ILE PRO LEU
SEQRES 12 X 431 ASN GLU TYR VAL ASP LYS LEU ASP LEU PRO PRO VAL SER
SEQRES 13 X 431 ARG GLN PHE LEU LEU ALA TRP ALA TRP ASN MET LEU GLY
SEQRES 14 X 431 GLN PRO ALA ASP GLN ALA SER ALA LEU TRP MET LEU GLN
SEQRES 15 X 431 LEU VAL ALA ALA HIS HIS TYR SER ILE LEU GLY VAL VAL
SEQRES 16 X 431 LEU SER LEU ASP GLU VAL PHE SER ASN GLY SER ALA ASP
SEQRES 17 X 431 LEU VAL ASP ALA MET SER GLN GLU ILE PRO GLU ILE ARG
SEQRES 18 X 431 LEU GLN THR VAL VAL THR GLY ILE ASP GLN SER GLY ASP
SEQRES 19 X 431 VAL VAL ASN VAL THR VAL LYS ASP GLY HIS ALA PHE GLN
SEQRES 20 X 431 ALA HIS SER VAL ILE VAL ALA THR PRO MET ASN THR TRP
SEQRES 21 X 431 ARG ARG ILE VAL PHE THR PRO ALA LEU PRO GLU ARG ARG
SEQRES 22 X 431 ARG SER VAL ILE GLU GLU GLY HIS GLY GLY GLN GLY LEU
SEQRES 23 X 431 LYS ILE LEU ILE HIS VAL ARG GLY ALA GLU ALA GLY ILE
SEQRES 24 X 431 GLU CYS VAL GLY ASP GLY ILE PHE PRO THR LEU TYR ASP
SEQRES 25 X 431 TYR CYS GLU VAL SER GLU SER GLU ARG LEU LEU VAL ALA
SEQRES 26 X 431 PHE THR ASP SER GLY SER PHE ASP PRO THR ASP ILE GLY
SEQRES 27 X 431 ALA VAL LYS ASP ALA VAL LEU TYR TYR LEU PRO GLU VAL
SEQRES 28 X 431 GLU VAL LEU GLY ILE ASP TYR HIS ASP TRP ILE ALA ASP
SEQRES 29 X 431 PRO LEU PHE GLU GLY PRO TRP VAL ALA PRO ARG VAL GLY
SEQRES 30 X 431 GLN PHE SER ARG VAL HIS LYS GLU LEU GLY GLU PRO ALA
SEQRES 31 X 431 GLY ARG ILE HIS PHE VAL GLY SER ASP VAL SER LEU GLU
SEQRES 32 X 431 PHE PRO GLY TYR ILE GLU GLY ALA LEU GLU THR ALA GLU
SEQRES 33 X 431 CYS ALA VAL ASN ALA ILE LEU HIS SER HIS HIS HIS HIS
SEQRES 34 X 431 HIS HIS
HET HNL X 433 13
HET FAD X 434 53
HET GP7 X 435 43
HET HNM X 436 28
HETNAM HNL 5-[(2S)-1-METHYLPYRROLIDIN-2-YL]PYRIDIN-2-OL
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM GP7 (1R)-2-{[(S)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-
HETNAM 2 GP7 [(PENTADECANOYLOXY)METHYL]ETHYL (12E)-HEXADECA-9,12-
HETNAM 3 GP7 DIENOATE
HETNAM HNM 1-(6-HYDROXYPYRIDIN-3-YL)-4-(METHYLAMINO)BUTAN-1-ONE
HETSYN HNL 6-HYDROXY-L-NICOTINE
HETSYN GP7 1-PENTADECANOYL-2-HEXADECANOYL-SN-GLYCERO-3-
HETSYN 2 GP7 PHOSPHOETHANOLAMINE
FORMUL 2 HNL C10 H14 N2 O
FORMUL 3 FAD C27 H33 N9 O15 P2
FORMUL 4 GP7 C36 H68 N O8 P
FORMUL 5 HNM C10 H14 N2 O2
FORMUL 6 HOH *393(H2 O)
HELIX 1 1 GLY X 10 ALA X 23 1 14
HELIX 2 2 HIS X 65 GLY X 76 1 12
HELIX 3 3 PRO X 104 SER X 106 5 3
HELIX 4 4 GLU X 107 HIS X 123 1 17
HELIX 5 5 LEU X 136 ASP X 140 5 5
HELIX 6 6 PRO X 142 ASP X 151 1 10
HELIX 7 7 PRO X 153 GLY X 169 1 17
HELIX 8 8 SER X 176 HIS X 187 1 12
HELIX 9 9 SER X 190 SER X 197 1 8
HELIX 10 10 GLY X 205 GLN X 215 1 11
HELIX 11 11 PRO X 256 ILE X 263 5 8
HELIX 12 12 PRO X 270 GLY X 280 1 11
HELIX 13 13 ASP X 336 LEU X 348 1 13
HELIX 14 14 GLY X 377 VAL X 382 1 6
HELIX 15 15 LYS X 384 GLU X 388 5 5
HELIX 16 16 GLY X 397 SER X 401 5 5
HELIX 17 17 TYR X 407 HIS X 424 1 18
SHEET 1 A 7 ILE X 220 ARG X 221 0
SHEET 2 A 7 VAL X 27 LEU X 30 1 N LEU X 29 O ARG X 221
SHEET 3 A 7 TYR X 2 VAL X 7 1 N VAL X 6 O LEU X 28
SHEET 4 A 7 PHE X 246 VAL X 253 1 O ILE X 252 N VAL X 7
SHEET 5 A 7 VAL X 236 VAL X 240 -1 N VAL X 238 O PHE X 246
SHEET 6 A 7 VAL X 226 ASP X 230 -1 N ASP X 230 O ASN X 237
SHEET 7 A 7 VAL X 264 THR X 266 1 O VAL X 264 N ILE X 229
SHEET 1 B 5 ILE X 220 ARG X 221 0
SHEET 2 B 5 VAL X 27 LEU X 30 1 N LEU X 29 O ARG X 221
SHEET 3 B 5 TYR X 2 VAL X 7 1 N VAL X 6 O LEU X 28
SHEET 4 B 5 PHE X 246 VAL X 253 1 O ILE X 252 N VAL X 7
SHEET 5 B 5 ILE X 393 PHE X 395 1 O HIS X 394 N VAL X 253
SHEET 1 C 2 SER X 42 GLU X 44 0
SHEET 2 C 2 ARG X 52 GLU X 54 -1 O VAL X 53 N ARG X 43
SHEET 1 D 3 TYR X 59 LEU X 60 0
SHEET 2 D 3 GLU X 200 PHE X 202 -1 O GLU X 200 N LEU X 60
SHEET 3 D 3 THR X 79 ALA X 80 -1 N ALA X 80 O VAL X 201
SHEET 1 E 6 SER X 87 PHE X 88 0
SHEET 2 E 6 ILE X 299 VAL X 302 1 O GLU X 300 N SER X 87
SHEET 3 E 6 THR X 309 GLU X 315 -1 O ASP X 312 N ILE X 299
SHEET 4 E 6 GLU X 320 ASP X 328 -1 O LEU X 322 N CYS X 314
SHEET 5 E 6 GLY X 285 ARG X 293 -1 N ILE X 290 O LEU X 323
SHEET 6 E 6 GLU X 352 ASP X 357 -1 O LEU X 354 N HIS X 291
CISPEP 1 THR X 266 PRO X 267 0 -2.73
SITE 1 AC1 10 TYR X 59 ASN X 166 MET X 167 LEU X 198
SITE 2 AC1 10 TYR X 311 PHE X 326 TRP X 371 GLY X 406
SITE 3 AC1 10 TYR X 407 FAD X 434
SITE 1 AC2 40 GLY X 8 GLY X 9 GLY X 10 PHE X 11
SITE 2 AC2 40 SER X 12 GLU X 31 GLY X 32 GLY X 37
SITE 3 AC2 40 GLY X 38 ARG X 39 ALA X 40 GLY X 56
SITE 4 AC2 40 GLY X 57 ALA X 58 TYR X 59 THR X 224
SITE 5 AC2 40 VAL X 226 ALA X 254 THR X 255 PRO X 256
SITE 6 AC2 40 TRP X 361 LEU X 366 PHE X 367 PRO X 370
SITE 7 AC2 40 TRP X 371 GLY X 397 SER X 398 GLY X 406
SITE 8 AC2 40 TYR X 407 ILE X 408 HNL X 433 HOH X 453
SITE 9 AC2 40 HOH X 469 HOH X 476 HOH X 505 HOH X 530
SITE 10 AC2 40 HOH X 674 HOH X 746 HOH X1008 HOH X1011
SITE 1 AC3 9 GLY X 105 THR X 115 PHE X 159 MET X 180
SITE 2 AC3 9 VAL X 195 HOH X 733 HOH X 741 HOH X1032
SITE 3 AC3 9 HOH X1044
SITE 1 AC4 11 TYR X 59 PHE X 85 TRP X 163 VAL X 195
SITE 2 AC4 11 LEU X 198 GLU X 300 TYR X 311 HOH X 660
SITE 3 AC4 11 HOH X 693 HOH X 918 HOH X1151
CRYST1 163.051 163.051 163.051 90.00 90.00 90.00 P 4 3 2 24
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 0.006133 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006133 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006133 0.00000
(ATOM LINES ARE NOT SHOWN.)
END