HEADER FLAVOPROTEIN, OXIDOREDUCTASE 24-SEP-10 3OZ2
TITLE CRYSTAL STRUCTURE OF A GERANYLGERANYL BACTERIOCHLOROPHYLL REDUCTASE-
TITLE 2 LIKE (TA0516) FROM THERMOPLASMA ACIDOPHILUM AT 1.60 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIGERANYLGERANYLGLYCEROPHOSPHOLIPID REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DGGGPL REDUCTASE, 2,3-DI-O-GERANYLGERANYLGLYCERYL PHOSPHATE
COMPND 5 REDUCTASE, GERANYLGERANYL REDUCTASE, GGR;
COMPND 6 EC: 1.3.1.-;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOPLASMA ACIDOPHILUM;
SOURCE 3 ORGANISM_COMMON: ARCHAEA;
SOURCE 4 ORGANISM_TAXID: 2303;
SOURCE 5 GENE: TA0516;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HK100;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: SPEEDET
KEYWDS STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, PSI-BIOLOGY, FLAVOPROTEIN,
KEYWDS 3 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 4 01-FEB-23 3OZ2 1 REMARK SEQADV LINK
REVDAT 3 20-JUL-11 3OZ2 1 KEYWDS
REVDAT 2 23-MAR-11 3OZ2 1 KEYWDS
REVDAT 1 27-OCT-10 3OZ2 0
SPRSDE 27-OCT-10 3OZ2 3CGV
JRNL AUTH Q.XU,T.EGUCHI,I.I.MATHEWS,C.L.RIFE,H.J.CHIU,C.L.FARR,
JRNL AUTH 2 J.FEUERHELM,L.JAROSZEWSKI,H.E.KLOCK,M.W.KNUTH,M.D.MILLER,
JRNL AUTH 3 D.WEEKES,M.A.ELSLIGER,A.M.DEACON,A.GODZIK,S.A.LESLEY,
JRNL AUTH 4 I.A.WILSON
JRNL TITL INSIGHTS INTO SUBSTRATE SPECIFICITY OF GERANYLGERANYL
JRNL TITL 2 REDUCTASES REVEALED BY THE STRUCTURE OF
JRNL TITL 3 DIGERANYLGERANYLGLYCEROPHOSPHOLIPID REDUCTASE, AN ESSENTIAL
JRNL TITL 4 ENZYME IN THE BIOSYNTHESIS OF ARCHAEAL MEMBRANE LIPIDS.
JRNL REF J.MOL.BIOL. V. 404 403 2010
JRNL REFN ISSN 0022-2836
JRNL PMID 20869368
JRNL DOI 10.1016/J.JMB.2010.09.032
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0110
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.26
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 55071
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) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.171
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2794
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) : 1.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3771
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE SET COUNT : 201
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3004
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 157
REMARK 3 SOLVENT ATOMS : 332
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.48
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.06
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.57000
REMARK 3 B22 (A**2) : 1.08000
REMARK 3 B33 (A**2) : -0.51000
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): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.074
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.046
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.679
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.972
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.968
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3467 ; 0.014 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2432 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4717 ; 1.608 ; 2.014
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5996 ; 0.911 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 471 ; 6.320 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 135 ;36.406 ;24.519
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 620 ;12.230 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;16.988 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 525 ; 0.094 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3826 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 657 ; 0.003 ; 0.020
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): 2096 ; 1.497 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 861 ; 0.422 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3394 ; 2.518 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1371 ; 4.121 ; 8.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1288 ; 6.476 ;11.000
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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 0 A 396
REMARK 3 RESIDUE RANGE : A 501 A 501
REMARK 3 RESIDUE RANGE : A 502 A 502
REMARK 3 ORIGIN FOR THE GROUP (A): 13.7612 50.0025 25.9353
REMARK 3 T TENSOR
REMARK 3 T11: 0.0365 T22: 0.0253
REMARK 3 T33: 0.0170 T12: 0.0052
REMARK 3 T13: -0.0031 T23: 0.0049
REMARK 3 L TENSOR
REMARK 3 L11: 0.7487 L22: 0.5438
REMARK 3 L33: 0.8513 L12: -0.1416
REMARK 3 L13: 0.2747 L23: -0.3801
REMARK 3 S TENSOR
REMARK 3 S11: -0.0504 S12: -0.1026 S13: 0.0454
REMARK 3 S21: 0.1346 S22: 0.0207 S23: -0.0113
REMARK 3 S31: -0.0587 S32: -0.0632 S33: 0.0298
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS 2. A MET-INHIBITION PROTOCOL WAS USED FOR
REMARK 3 SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE
REMARK 3 OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO
REMARK 3 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET
REMARK 3 INCORPORATION. 3. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U
REMARK 3 FACTORS. 4. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT.
REMARK 3 5. FAD IS MODELED BASED ON DENSITY AND FUNCTION. 6. A BACTERIAL
REMARK 3 LIPID FOUND IN THE ACTIVE SITE WAS TENTATIVELY ASSIGNED AS A
REMARK 3 PHOSPHATIDYLGYLCEROL (OZ2) BASED ON DENSITY AND FUNCTION. THE
REMARK 3 DENSITY FOR THE HEAD GROUP AND LIPID TAILS ARE POORLY DEFINED.
REMARK 3 7. ETHYLENE GLYCOL (EDO) AND GLYCEROL (GOL) WERE MODELED BASED
REMARK 3 ON CRYSTALLIZATION/CYRO CONDITIONS.
REMARK 4
REMARK 4 3OZ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-10.
REMARK 100 THE DEPOSITION ID IS D_1000061751.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-FEB-08
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 : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.91837,0.97920,0.97862
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 325 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 55071
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 45.257
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.1600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.46600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SHELX, SHELXD, AUTOSHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.55
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15.00% GLYCEROL, 8.50% ISO-PROPANOL,
REMARK 280 17.00% PEG-4000, 0.1M HEPES PH 7.5, NANODROP, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 24.79500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.92500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.33500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.92500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.79500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.33500
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: 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 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 LYS A 50 CG CD CE NZ
REMARK 470 ARG A 62 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 80 CG CD CE NZ
REMARK 470 GLU A 88 CG CD OE1 OE2
REMARK 470 LYS A 89 CG CD CE NZ
REMARK 470 HIS A 232 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 234 CZ NH1 NH2
REMARK 470 LYS A 348 CD CE NZ
REMARK 470 GLU A 387 CG CD OE1 OE2
REMARK 470 VAL A 388 CG1 CG2
REMARK 470 VAL A 389 CG1 CG2
REMARK 470 GLU A 391 CG CD OE1 OE2
REMARK 470 GLU A 393 CG CD OE1 OE2
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 ASP A 101 CB - CG - OD1 ANGL. DEV. = 6.6 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 LYS A 80 -135.05 -69.16
REMARK 500 TRP A 230 -61.80 -105.56
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OZ2 A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 510
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 511
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 512
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 513
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 514
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 515
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 382454 RELATED DB: TARGETDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG
REMARK 999 MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING
REMARK 999 ONLY A GLYCINE FOLLOWED BY THE TARGET SEQUENCE.
DBREF 3OZ2 A 1 396 UNP Q9HKS9 GGR_THEAC 1 396
SEQADV 3OZ2 GLY A 0 UNP Q9HKS9 EXPRESSION TAG
SEQRES 1 A 397 GLY MSE GLU THR TYR ASP VAL LEU VAL VAL GLY GLY GLY
SEQRES 2 A 397 PRO GLY GLY SER THR ALA ALA ARG TYR ALA ALA LYS TYR
SEQRES 3 A 397 GLY LEU LYS THR LEU MSE ILE GLU LYS ARG PRO GLU ILE
SEQRES 4 A 397 GLY SER PRO VAL ARG CYS GLY GLU GLY LEU SER LYS GLY
SEQRES 5 A 397 ILE LEU ASN GLU ALA ASP ILE LYS ALA ASP ARG SER PHE
SEQRES 6 A 397 ILE ALA ASN GLU VAL LYS GLY ALA ARG ILE TYR GLY PRO
SEQRES 7 A 397 SER GLU LYS ARG PRO ILE ILE LEU GLN SER GLU LYS ALA
SEQRES 8 A 397 GLY ASN GLU VAL GLY TYR VAL LEU GLU ARG ASP LYS PHE
SEQRES 9 A 397 ASP LYS HIS LEU ALA ALA LEU ALA ALA LYS ALA GLY ALA
SEQRES 10 A 397 ASP VAL TRP VAL LYS SER PRO ALA LEU GLY VAL ILE LYS
SEQRES 11 A 397 GLU ASN GLY LYS VAL ALA GLY ALA LYS ILE ARG HIS ASN
SEQRES 12 A 397 ASN GLU ILE VAL ASP VAL ARG ALA LYS MSE VAL ILE ALA
SEQRES 13 A 397 ALA ASP GLY PHE GLU SER GLU PHE GLY ARG TRP ALA GLY
SEQRES 14 A 397 LEU LYS SER VAL ILE LEU ALA ARG ASN ASP ILE ILE SER
SEQRES 15 A 397 ALA LEU GLN TYR ARG MSE ILE ASN VAL ASP VAL ASP PRO
SEQRES 16 A 397 ASP TYR THR ASP PHE TYR LEU GLY SER ILE ALA PRO ALA
SEQRES 17 A 397 GLY TYR ILE TRP VAL PHE PRO LYS GLY GLU GLY MSE ALA
SEQRES 18 A 397 ASN VAL GLY ILE GLY SER SER ILE ASN TRP ILE HIS ASN
SEQRES 19 A 397 ARG PHE GLU LEU LYS ASN TYR LEU ASP ARG PHE ILE GLU
SEQRES 20 A 397 ASN HIS PRO GLY LEU LYS LYS GLY GLN ASP ILE GLN LEU
SEQRES 21 A 397 VAL THR GLY GLY VAL SER VAL SER LYS VAL LYS MSE PRO
SEQRES 22 A 397 ILE THR MSE PRO GLY LEU MSE LEU VAL GLY ASP ALA ALA
SEQRES 23 A 397 ARG LEU ILE ASP PRO ILE THR GLY GLY GLY ILE ALA ASN
SEQRES 24 A 397 ALA ILE VAL SER GLY MSE TYR ALA ALA GLN VAL THR LYS
SEQRES 25 A 397 GLU ALA ILE GLU SER ASN ASP TYR SER PRO GLN MSE MSE
SEQRES 26 A 397 GLN LYS TYR GLU LYS LEU ILE LYS GLU ARG PHE GLU ARG
SEQRES 27 A 397 LYS HIS LEU ARG ASN TRP VAL ALA LYS GLU LYS LEU ALA
SEQRES 28 A 397 MSE LEU SER ASP ASP THR LEU ASP LYS LEU VAL ASP ILE
SEQRES 29 A 397 VAL SER GLU GLN VAL LEU THR THR ILE SER VAL GLU ALA
SEQRES 30 A 397 ILE LEU LYS ALA ILE ALA GLU LYS TYR PRO GLU VAL VAL
SEQRES 31 A 397 LYS GLU LEU GLU ASP LEU ILE
MODRES 3OZ2 MSE A 1 MET SELENOMETHIONINE
MODRES 3OZ2 MSE A 31 MET SELENOMETHIONINE
MODRES 3OZ2 MSE A 152 MET SELENOMETHIONINE
MODRES 3OZ2 MSE A 187 MET SELENOMETHIONINE
MODRES 3OZ2 MSE A 219 MET SELENOMETHIONINE
MODRES 3OZ2 MSE A 271 MET SELENOMETHIONINE
MODRES 3OZ2 MSE A 275 MET SELENOMETHIONINE
MODRES 3OZ2 MSE A 279 MET SELENOMETHIONINE
MODRES 3OZ2 MSE A 304 MET SELENOMETHIONINE
MODRES 3OZ2 MSE A 323 MET SELENOMETHIONINE
MODRES 3OZ2 MSE A 324 MET SELENOMETHIONINE
MODRES 3OZ2 MSE A 351 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 31 8
HET MSE A 152 8
HET MSE A 187 13
HET MSE A 219 13
HET MSE A 271 8
HET MSE A 275 13
HET MSE A 279 8
HET MSE A 304 13
HET MSE A 323 8
HET MSE A 324 8
HET MSE A 351 13
HET FAD A 501 53
HET OZ2 A 502 48
HET EDO A 503 4
HET EDO A 504 4
HET EDO A 505 4
HET EDO A 506 4
HET EDO A 507 4
HET EDO A 508 4
HET EDO A 509 4
HET EDO A 510 4
HET EDO A 511 4
HET EDO A 512 4
HET EDO A 513 4
HET GOL A 514 6
HET GOL A 515 6
HETNAM MSE SELENOMETHIONINE
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM OZ2 (2R)-3-{[(R)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)
HETNAM 2 OZ2 PHOSPHORYL]OXY}-2-[(6Z)-TRIDEC-6-ENOYLOXY]PROPYL (9Z)-
HETNAM 3 OZ2 OCTADEC-9-ENOATE
HETNAM EDO 1,2-ETHANEDIOL
HETNAM GOL GLYCEROL
HETSYN EDO ETHYLENE GLYCOL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 OZ2 C37 H69 O10 P
FORMUL 4 EDO 11(C2 H6 O2)
FORMUL 15 GOL 2(C3 H8 O3)
FORMUL 17 HOH *332(H2 O)
HELIX 1 1 GLY A 12 TYR A 25 1 14
HELIX 2 2 LYS A 50 ALA A 56 1 7
HELIX 3 3 GLU A 99 GLY A 115 1 17
HELIX 4 4 SER A 161 GLY A 168 1 8
HELIX 5 5 LEU A 169 ILE A 173 5 5
HELIX 6 6 ALA A 175 ASN A 177 5 3
HELIX 7 7 ASN A 233 ASN A 247 1 15
HELIX 8 8 HIS A 248 LYS A 253 1 6
HELIX 9 9 GLY A 282 ARG A 286 5 5
HELIX 10 10 GLY A 295 ASN A 317 1 23
HELIX 11 11 SER A 320 MSE A 351 1 32
HELIX 12 12 SER A 353 SER A 365 1 13
HELIX 13 13 SER A 373 TYR A 385 1 13
HELIX 14 14 PRO A 386 ILE A 396 5 11
SHEET 1 A 6 ASP A 117 TRP A 119 0
SHEET 2 A 6 THR A 29 ILE A 32 1 N THR A 29 O ASP A 117
SHEET 3 A 6 MSE A 1 VAL A 9 1 N VAL A 8 O LEU A 30
SHEET 4 A 6 GLU A 144 ALA A 155 1 O ILE A 154 N LEU A 7
SHEET 5 A 6 LYS A 133 HIS A 141 -1 N ILE A 139 O VAL A 146
SHEET 6 A 6 ALA A 124 GLU A 130 -1 N LEU A 125 O LYS A 138
SHEET 1 B 6 ASP A 117 TRP A 119 0
SHEET 2 B 6 THR A 29 ILE A 32 1 N THR A 29 O ASP A 117
SHEET 3 B 6 MSE A 1 VAL A 9 1 N VAL A 8 O LEU A 30
SHEET 4 B 6 GLU A 144 ALA A 155 1 O ILE A 154 N LEU A 7
SHEET 5 B 6 LEU A 278 LEU A 280 1 O MSE A 279 N ALA A 155
SHEET 6 B 6 THR A 274 MSE A 275 -1 N MSE A 275 O LEU A 278
SHEET 1 C 3 GLY A 47 SER A 49 0
SHEET 2 C 3 GLY A 95 LEU A 98 -1 O TYR A 96 N LEU A 48
SHEET 3 C 3 ILE A 65 VAL A 69 -1 N ASN A 67 O VAL A 97
SHEET 1 D 7 ILE A 83 GLN A 86 0
SHEET 2 D 7 GLY A 71 TYR A 75 -1 N ILE A 74 O ILE A 83
SHEET 3 D 7 TYR A 196 TYR A 200 1 O PHE A 199 N TYR A 75
SHEET 4 D 7 GLY A 208 GLY A 216 -1 O ILE A 210 N TYR A 200
SHEET 5 D 7 MSE A 219 SER A 227 -1 O ASN A 221 N PHE A 213
SHEET 6 D 7 ILE A 179 ILE A 188 -1 N TYR A 185 O VAL A 222
SHEET 7 D 7 GLN A 255 SER A 265 -1 O ILE A 257 N ARG A 186
LINK C GLY A 0 N MSE A 1 1555 1555 1.34
LINK C MSE A 1 N GLU A 2 1555 1555 1.36
LINK C LEU A 30 N MSE A 31 1555 1555 1.33
LINK C MSE A 31 N ILE A 32 1555 1555 1.33
LINK C LYS A 151 N MSE A 152 1555 1555 1.35
LINK C MSE A 152 N VAL A 153 1555 1555 1.31
LINK C ARG A 186 N MSE A 187 1555 1555 1.32
LINK C MSE A 187 N ILE A 188 1555 1555 1.33
LINK C GLY A 218 N MSE A 219 1555 1555 1.34
LINK C MSE A 219 N ALA A 220 1555 1555 1.34
LINK C LYS A 270 N MSE A 271 1555 1555 1.33
LINK C MSE A 271 N PRO A 272 1555 1555 1.34
LINK C THR A 274 N MSE A 275 1555 1555 1.32
LINK C MSE A 275 N PRO A 276 1555 1555 1.35
LINK C LEU A 278 N MSE A 279 1555 1555 1.33
LINK C MSE A 279 N LEU A 280 1555 1555 1.33
LINK C GLY A 303 N MSE A 304 1555 1555 1.33
LINK C MSE A 304 N TYR A 305 1555 1555 1.33
LINK C GLN A 322 N MSE A 323 1555 1555 1.33
LINK C MSE A 323 N MSE A 324 1555 1555 1.32
LINK C MSE A 324 N GLN A 325 1555 1555 1.33
LINK C ALA A 350 N MSE A 351 1555 1555 1.33
LINK C MSE A 351 N LEU A 352 1555 1555 1.33
CISPEP 1 SER A 40 PRO A 41 0 -2.43
CISPEP 2 MSE A 271 PRO A 272 0 0.63
SITE 1 AC1 37 GLY A 10 GLY A 12 PRO A 13 GLY A 14
SITE 2 AC1 37 GLU A 33 LYS A 34 ARG A 35 ARG A 43
SITE 3 AC1 37 CYS A 44 GLY A 45 GLU A 46 GLY A 47
SITE 4 AC1 37 ARG A 100 PRO A 123 ALA A 124 ALA A 156
SITE 5 AC1 37 ASP A 157 GLY A 158 GLU A 162 PHE A 213
SITE 6 AC1 37 VAL A 264 GLY A 282 ASP A 283 GLY A 294
SITE 7 AC1 37 GLY A 295 ILE A 296 ALA A 299 OZ2 A 502
SITE 8 AC1 37 HOH A 517 HOH A 518 HOH A 524 HOH A 528
SITE 9 AC1 37 HOH A 622 HOH A 623 HOH A 628 HOH A 630
SITE 10 AC1 37 HOH A 687
SITE 1 AC2 18 SER A 49 TYR A 209 TRP A 211 PRO A 290
SITE 2 AC2 18 ILE A 291 THR A 292 GLY A 293 LYS A 338
SITE 3 AC2 18 LEU A 349 ILE A 372 SER A 373 VAL A 374
SITE 4 AC2 18 FAD A 501 EDO A 508 GOL A 515 HOH A 655
SITE 5 AC2 18 HOH A 805 HOH A 836
SITE 1 AC3 6 VAL A 118 TRP A 119 VAL A 120 HIS A 141
SITE 2 AC3 6 HOH A 575 HOH A 790
SITE 1 AC4 4 LYS A 138 GLU A 312 GLU A 315 HOH A 616
SITE 1 AC5 5 GLY A 132 LYS A 133 VAL A 134 MSE A 275
SITE 2 AC5 5 HOH A 585
SITE 1 AC6 3 TYR A 4 HOH A 670 HOH A 747
SITE 1 AC7 6 ASN A 177 SER A 227 LYS A 346 GLU A 347
SITE 2 AC7 6 HOH A 617 HOH A 785
SITE 1 AC8 6 ASP A 289 THR A 292 GLY A 294 ASN A 298
SITE 2 AC8 6 OZ2 A 502 EDO A 509
SITE 1 AC9 6 ASN A 298 VAL A 301 ARG A 334 LYS A 338
SITE 2 AC9 6 EDO A 508 HOH A 666
SITE 1 BC1 3 ASP A 117 TRP A 119 HOH A 635
SITE 1 BC2 4 HOH A 558 HOH A 684 HOH A 769 HOH A 788
SITE 1 BC3 5 ALA A 23 LEU A 27 HOH A 557 HOH A 633
SITE 2 BC3 5 HOH A 705
SITE 1 BC4 7 GLY A 254 LYS A 270 MSE A 271 HOH A 589
SITE 2 BC4 7 HOH A 626 HOH A 672 HOH A 765
SITE 1 BC5 8 PRO A 272 THR A 274 MSE A 275 PRO A 321
SITE 2 BC5 8 MSE A 324 GLN A 325 GLU A 328 HOH A 604
SITE 1 BC6 6 GLY A 47 LEU A 48 SER A 49 VAL A 69
SITE 2 BC6 6 THR A 197 OZ2 A 502
CRYST1 49.590 70.670 117.850 90.00 90.00 90.00 P 21 21 21 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 0.020165 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014150 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008485 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
