HEADER OXIDOREDUCTASE 26-APR-11 3RPE
TITLE 1.1 ANGSTROM CRYSTAL STRUCTURE OF PUTATIVE MODULATOR OF DRUG ACTIVITY
TITLE 2 (MDAB) FROM YERSINIA PESTIS CO92.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MODULATOR OF DRUG ACTIVITY B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: MDAB;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YERSINIA PESTIS;
SOURCE 3 ORGANISM_TAXID: 632;
SOURCE 4 STRAIN: CO92;
SOURCE 5 GENE: MDA66, MDAB, MDAB3, Y3509, YPO0670, YP_2985;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: KRX;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PMCSG7
KEYWDS STRUCTURAL GENOMICS, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS
KEYWDS 2 DISEASES, CSGID, FLAVODOXIN-LIKE FOLD, NADPH DEHYDROGENASE (QUINONE)
KEYWDS 3 ACTIVITY, FLAVIN ADENINE DINUCLEOTIDE BINDING, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR G.MINASOV,A.HALAVATY,L.SHUVALOVA,I.DUBROVSKA,J.WINSOR,L.PAPAZISI,
AUTHOR 2 W.F.ANDERSON,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
AUTHOR 3 (CSGID)
REVDAT 3 13-SEP-23 3RPE 1 REMARK SEQADV
REVDAT 2 08-NOV-17 3RPE 1 REMARK
REVDAT 1 04-MAY-11 3RPE 0
JRNL AUTH G.MINASOV,A.HALAVATY,L.SHUVALOVA,I.DUBROVSKA,J.WINSOR,
JRNL AUTH 2 L.PAPAZISI,W.F.ANDERSON,
JRNL AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES
JRNL AUTH 4 (CSGID)
JRNL TITL 1.1 ANGSTROM CRYSTAL STRUCTURE OF PUTATIVE MODULATOR OF DRUG
JRNL TITL 2 ACTIVITY (MDAB) FROM YERSINIA PESTIS CO92.
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 1.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 145242
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) : 0.100
REMARK 3 R VALUE (WORKING SET) : 0.100
REMARK 3 FREE R VALUE : 0.117
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 7752
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) : 1.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10712
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.28
REMARK 3 BIN R VALUE (WORKING SET) : 0.2240
REMARK 3 BIN FREE R VALUE SET COUNT : 593
REMARK 3 BIN FREE R VALUE : 0.2570
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3125
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 113
REMARK 3 SOLVENT ATOMS : 473
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.10
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 6.91000
REMARK 3 B22 (A**2) : 6.91000
REMARK 3 B33 (A**2) : -13.82000
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): 0.005
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.005
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.013
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.639
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.989
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.985
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3643 ; 0.010 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2403 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5003 ; 1.547 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5863 ; 1.005 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 448 ; 4.301 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 179 ;33.234 ;24.525
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 589 ;11.438 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 18 ;16.461 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 510 ; 0.129 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4185 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 765 ; 0.001 ; 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): 2125 ; 1.585 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 861 ; 3.792 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3464 ; 2.222 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1518 ; 3.108 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1538 ; 4.327 ; 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): 3643 ; 1.759 ; 3.000
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 TWIN DETAILS
REMARK 3 NUMBER OF TWIN DOMAINS : 2
REMARK 3 TWIN DOMAIN : 1
REMARK 3 TWIN OPERATOR : H, K, L
REMARK 3 TWIN FRACTION : 0.615
REMARK 3 TWIN DOMAIN : 2
REMARK 3 TWIN OPERATOR : -H-K, K, -L
REMARK 3 TWIN FRACTION : 0.385
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 : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3RPE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-11.
REMARK 100 THE DEPOSITION ID IS D_1000065213.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-APR-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 21-ID-G
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97856
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : BERYLLIUM LENSES
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 153499
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.04900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 33.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.51700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.950
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 2B3D
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 37.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 7.8 MG/ML, 0.5 M SODIUM
REMARK 280 CHLORIDE, 5 MM FAD, 0.01 M TRIS, PH 8.3, SCREEN: PACT (A2), 0.1
REMARK 280 M SPG BUFFER, PH 5.0, 25% W/V PEG1500, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.80533
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 25.40267
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: 7270 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15610 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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 MET A -23
REMARK 465 HIS A -22
REMARK 465 HIS A -21
REMARK 465 HIS A -20
REMARK 465 HIS A -19
REMARK 465 HIS A -18
REMARK 465 HIS A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 GLY A -14
REMARK 465 VAL A -13
REMARK 465 ASP A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 THR A -9
REMARK 465 GLU A -8
REMARK 465 ASN A -7
REMARK 465 LEU A -6
REMARK 465 GLN A -3
REMARK 465 SER A -2
REMARK 465 ASN A -1
REMARK 465 MET B -23
REMARK 465 HIS B -22
REMARK 465 HIS B -21
REMARK 465 HIS B -20
REMARK 465 HIS B -19
REMARK 465 HIS B -18
REMARK 465 HIS B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 GLY B -14
REMARK 465 VAL B -13
REMARK 465 ASP B -12
REMARK 465 LEU B -11
REMARK 465 GLY B -10
REMARK 465 THR B -9
REMARK 465 GLU B -8
REMARK 465 ASN B -7
REMARK 465 LEU B -6
REMARK 465 TYR B -5
REMARK 465 PHE B -4
REMARK 465 GLN B -3
REMARK 465 SER B -2
REMARK 465 ASN B -1
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 PHE A -4 CA C O CB CG CD1 CD2
REMARK 470 PHE A -4 CE1 CE2 CZ
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 14 -122.86 51.07
REMARK 500 ALA B 14 -123.57 47.93
REMARK 500 ALA B 14 -121.92 47.93
REMARK 500 SER B 102 -44.77 8.99
REMARK 500 ASP B 176 71.07 -150.54
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 195
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 196
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 195
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: IDP00511 RELATED DB: TARGETDB
DBREF 3RPE A 1 194 UNP Q7CGH8 Q7CGH8_YERPE 1 194
DBREF 3RPE B 1 194 UNP Q7CGH8 Q7CGH8_YERPE 1 194
SEQADV 3RPE MET A -23 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE HIS A -22 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE HIS A -21 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE HIS A -20 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE HIS A -19 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE HIS A -18 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE HIS A -17 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE SER A -16 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE SER A -15 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE GLY A -14 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE VAL A -13 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE ASP A -12 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE LEU A -11 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE GLY A -10 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE THR A -9 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE GLU A -8 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE ASN A -7 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE LEU A -6 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE TYR A -5 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE PHE A -4 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE GLN A -3 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE SER A -2 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE ASN A -1 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE ALA A 0 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE MET B -23 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE HIS B -22 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE HIS B -21 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE HIS B -20 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE HIS B -19 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE HIS B -18 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE HIS B -17 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE SER B -16 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE SER B -15 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE GLY B -14 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE VAL B -13 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE ASP B -12 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE LEU B -11 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE GLY B -10 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE THR B -9 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE GLU B -8 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE ASN B -7 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE LEU B -6 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE TYR B -5 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE PHE B -4 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE GLN B -3 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE SER B -2 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE ASN B -1 UNP Q7CGH8 EXPRESSION TAG
SEQADV 3RPE ALA B 0 UNP Q7CGH8 EXPRESSION TAG
SEQRES 1 A 218 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 218 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 A 218 ASN VAL LEU ILE ILE ASN ALA MET LYS GLU PHE ALA HIS
SEQRES 4 A 218 SER LYS GLY ALA LEU ASN LEU THR LEU THR ASN VAL ALA
SEQRES 5 A 218 ALA ASP PHE LEU ARG GLU SER GLY HIS GLN VAL LYS ILE
SEQRES 6 A 218 THR THR VAL ASP GLN GLY TYR ASP ILE GLU SER GLU ILE
SEQRES 7 A 218 GLU ASN TYR LEU TRP ALA ASP THR ILE ILE TYR GLN MET
SEQRES 8 A 218 PRO ALA TRP TRP MET GLY GLU PRO TRP ILE LEU LYS LYS
SEQRES 9 A 218 TYR ILE ASP GLU VAL PHE THR ASP GLY HIS GLY ARG LEU
SEQRES 10 A 218 TYR GLN SER ASP GLY ARG THR ARG SER ASP ALA THR LYS
SEQRES 11 A 218 GLY TYR GLY SER GLY GLY LEU ILE GLN GLY LYS THR TYR
SEQRES 12 A 218 MET LEU SER VAL THR TRP ASN ALA PRO ARG GLU ALA PHE
SEQRES 13 A 218 THR ASP PRO GLU GLN PHE PHE HIS GLY VAL GLY VAL ASP
SEQRES 14 A 218 GLY VAL TYR LEU PRO PHE HIS LYS ALA ASN GLN PHE LEU
SEQRES 15 A 218 GLY MET LYS PRO LEU PRO THR PHE MET CYS ASN ASP VAL
SEQRES 16 A 218 ILE LYS GLN PRO ASP ILE GLU GLY ASP ILE ALA ARG TYR
SEQRES 17 A 218 ARG GLN HIS LEU ALA GLU ASN VAL ASN SER
SEQRES 1 B 218 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 218 GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA MET SER
SEQRES 3 B 218 ASN VAL LEU ILE ILE ASN ALA MET LYS GLU PHE ALA HIS
SEQRES 4 B 218 SER LYS GLY ALA LEU ASN LEU THR LEU THR ASN VAL ALA
SEQRES 5 B 218 ALA ASP PHE LEU ARG GLU SER GLY HIS GLN VAL LYS ILE
SEQRES 6 B 218 THR THR VAL ASP GLN GLY TYR ASP ILE GLU SER GLU ILE
SEQRES 7 B 218 GLU ASN TYR LEU TRP ALA ASP THR ILE ILE TYR GLN MET
SEQRES 8 B 218 PRO ALA TRP TRP MET GLY GLU PRO TRP ILE LEU LYS LYS
SEQRES 9 B 218 TYR ILE ASP GLU VAL PHE THR ASP GLY HIS GLY ARG LEU
SEQRES 10 B 218 TYR GLN SER ASP GLY ARG THR ARG SER ASP ALA THR LYS
SEQRES 11 B 218 GLY TYR GLY SER GLY GLY LEU ILE GLN GLY LYS THR TYR
SEQRES 12 B 218 MET LEU SER VAL THR TRP ASN ALA PRO ARG GLU ALA PHE
SEQRES 13 B 218 THR ASP PRO GLU GLN PHE PHE HIS GLY VAL GLY VAL ASP
SEQRES 14 B 218 GLY VAL TYR LEU PRO PHE HIS LYS ALA ASN GLN PHE LEU
SEQRES 15 B 218 GLY MET LYS PRO LEU PRO THR PHE MET CYS ASN ASP VAL
SEQRES 16 B 218 ILE LYS GLN PRO ASP ILE GLU GLY ASP ILE ALA ARG TYR
SEQRES 17 B 218 ARG GLN HIS LEU ALA GLU ASN VAL ASN SER
HET FAD A 195 53
HET PEG A 196 7
HET FAD B 195 53
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM PEG DI(HYDROXYETHYL)ETHER
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 PEG C4 H10 O3
FORMUL 6 HOH *473(H2 O)
HELIX 1 1 GLY A 18 SER A 35 1 18
HELIX 2 2 ASP A 45 GLY A 47 5 3
HELIX 3 3 ASP A 49 ALA A 60 1 12
HELIX 4 4 PRO A 75 GLY A 89 1 15
HELIX 5 5 ARG A 129 ASP A 134 1 6
HELIX 6 6 VAL A 142 TYR A 148 1 7
HELIX 7 7 TYR A 148 LEU A 158 1 11
HELIX 8 8 ASP A 176 VAL A 192 1 17
HELIX 9 9 GLY B 18 SER B 35 1 18
HELIX 10 10 ASP B 45 GLY B 47 5 3
HELIX 11 11 ASP B 49 ALA B 60 1 12
HELIX 12 12 PRO B 75 GLY B 89 1 15
HELIX 13 13 ARG B 129 ASP B 134 1 6
HELIX 14 14 VAL B 142 TYR B 148 1 7
HELIX 15 15 TYR B 148 LEU B 158 1 11
HELIX 16 16 ASP B 176 VAL B 192 1 17
SHEET 1 A 5 VAL A 39 THR A 43 0
SHEET 2 A 5 VAL A 4 ASN A 8 1 N ASN A 8 O THR A 42
SHEET 3 A 5 THR A 62 PRO A 68 1 O ILE A 64 N ILE A 7
SHEET 4 A 5 THR A 118 THR A 124 1 O SER A 122 N TYR A 65
SHEET 5 A 5 LYS A 161 PRO A 162 1 O LYS A 161 N TYR A 119
SHEET 1 B 5 VAL A 39 THR A 43 0
SHEET 2 B 5 VAL A 4 ASN A 8 1 N ASN A 8 O THR A 42
SHEET 3 B 5 THR A 62 PRO A 68 1 O ILE A 64 N ILE A 7
SHEET 4 B 5 THR A 118 THR A 124 1 O SER A 122 N TYR A 65
SHEET 5 B 5 PHE A 166 CYS A 168 1 O PHE A 166 N LEU A 121
SHEET 1 C 5 VAL B 39 THR B 43 0
SHEET 2 C 5 VAL B 4 ASN B 8 1 N ASN B 8 O THR B 42
SHEET 3 C 5 THR B 62 PRO B 68 1 O ILE B 64 N ILE B 7
SHEET 4 C 5 THR B 118 THR B 124 1 O MET B 120 N TYR B 65
SHEET 5 C 5 LYS B 161 PRO B 162 1 O LYS B 161 N TYR B 119
SHEET 1 D 5 VAL B 39 THR B 43 0
SHEET 2 D 5 VAL B 4 ASN B 8 1 N ASN B 8 O THR B 42
SHEET 3 D 5 THR B 62 PRO B 68 1 O ILE B 64 N ILE B 7
SHEET 4 D 5 THR B 118 THR B 124 1 O MET B 120 N TYR B 65
SHEET 5 D 5 PHE B 166 CYS B 168 1 O PHE B 166 N LEU B 121
SITE 1 AC1 34 PHE A 13 HIS A 15 SER A 16 LYS A 17
SITE 2 AC1 34 GLY A 18 ALA A 19 LEU A 20 ASN A 21
SITE 3 AC1 34 THR A 23 PRO A 68 ALA A 69 TRP A 70
SITE 4 AC1 34 TRP A 71 MET A 72 THR A 124 TRP A 125
SITE 5 AC1 34 ASN A 126 ALA A 127 VAL A 171 PRO A 175
SITE 6 AC1 34 ILE A 177 HOH A 197 HOH A 209 HOH A 225
SITE 7 AC1 34 HOH A 228 HOH A 231 HOH A 232 HOH A 233
SITE 8 AC1 34 HOH A 234 HOH A 235 HOH A 260 HOH A 463
SITE 9 AC1 34 THR B 87 TYR B 108
SITE 1 AC2 5 VAL A 27 ASP A 30 ILE A 181 HOH A 234
SITE 2 AC2 5 HOH A 301
SITE 1 AC3 31 TYR A -5 THR A 87 TYR A 108 PHE B 13
SITE 2 AC3 31 HIS B 15 SER B 16 LYS B 17 GLY B 18
SITE 3 AC3 31 ALA B 19 LEU B 20 ASN B 21 THR B 23
SITE 4 AC3 31 PRO B 68 ALA B 69 TRP B 70 TRP B 71
SITE 5 AC3 31 MET B 72 THR B 124 TRP B 125 ASN B 126
SITE 6 AC3 31 ALA B 127 VAL B 171 PRO B 175 ILE B 177
SITE 7 AC3 31 HOH B 223 HOH B 241 HOH B 243 HOH B 274
SITE 8 AC3 31 HOH B 340 HOH B 348 HOH B 404
CRYST1 66.497 66.497 76.208 90.00 90.00 120.00 P 32 6
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 0.015038 0.008682 0.000000 0.00000
SCALE2 0.000000 0.017365 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013122 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
