HEADER ELECTRON TRANSPORT 06-OCT-08 3ESY
TITLE E16KE61K FLAVODOXIN FROM ANABAENA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAVODOXIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ANABAENA SP.;
SOURCE 3 ORGANISM_TAXID: 1168;
SOURCE 4 STRAIN: PCC 7119;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TG1;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTRC99A
KEYWDS ALPHA AND BETA PROTEIN, ELECTRON TRANSPORT, FLAVOPROTEIN, FMN,
KEYWDS 2 TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR B.HERGUEDAS,M.MARTINEZ-JULVEZ,J.A.HERMOSO,G.GONI,M.MEDINA
REVDAT 5 01-NOV-23 3ESY 1 REMARK
REVDAT 4 10-NOV-21 3ESY 1 REMARK SEQADV
REVDAT 3 13-JUL-11 3ESY 1 VERSN
REVDAT 2 03-MAR-09 3ESY 1 JRNL
REVDAT 1 10-FEB-09 3ESY 0
JRNL AUTH G.GONI,B.HERGUEDAS,M.HERVAS,J.R.PEREGRINA,M.A.DE LA ROSA,
JRNL AUTH 2 C.GOMEZ-MORENO,J.A.NAVARRO,J.A.HERMOSO,M.MARTINEZ-JULVEZ,
JRNL AUTH 3 M.MEDINA
JRNL TITL FLAVODOXIN: A COMPROMISE BETWEEN EFFICIENCY AND VERSATILITY
JRNL TITL 2 IN THE ELECTRON TRANSFER FROM PHOTOSYSTEM I TO
JRNL TITL 3 FERREDOXIN-NADP(+) REDUCTASE
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1787 144 2009
JRNL REFN ISSN 0006-3002
JRNL PMID 19150326
JRNL DOI 10.1016/J.BBABIO.2008.12.006
REMARK 2
REMARK 2 RESOLUTION. 2.39 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) : 2.39
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 22.72
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 22468
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.250
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1748
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) : 2.39
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1577
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 111
REMARK 3 BIN FREE R VALUE : 0.4090
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5304
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 136
REMARK 3 SOLVENT ATOMS : 297
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 21.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : -0.02000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.311
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.205
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.204
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.935
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5542 ; 0.013 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 7510 ; 1.496 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 668 ; 6.095 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 284 ;39.385 ;25.915
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 912 ;18.544 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;27.086 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 792 ; 0.098 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4228 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2779 ; 0.220 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3714 ; 0.306 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 236 ; 0.152 ; 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): 92 ; 0.198 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 17 ; 0.209 ; 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): 3362 ; 0.703 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5240 ; 1.252 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2665 ; 1.781 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2270 ; 2.848 ; 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 : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 4
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 169
REMARK 3 RESIDUE RANGE : B 2 B 169
REMARK 3 RESIDUE RANGE : C 2 C 169
REMARK 3 RESIDUE RANGE : D 2 D 169
REMARK 3 ORIGIN FOR THE GROUP (A): 37.6871 19.4711 68.8769
REMARK 3 T TENSOR
REMARK 3 T11: 0.0067 T22: -0.0147
REMARK 3 T33: 0.0014 T12: 0.0179
REMARK 3 T13: -0.0099 T23: 0.0042
REMARK 3 L TENSOR
REMARK 3 L11: 0.0316 L22: 0.0318
REMARK 3 L33: 0.2243 L12: 0.0033
REMARK 3 L13: -0.0755 L23: 0.0292
REMARK 3 S TENSOR
REMARK 3 S11: 0.0000 S12: -0.0071 S13: -0.0047
REMARK 3 S21: -0.0003 S22: -0.0046 S23: -0.0104
REMARK 3 S31: -0.0122 S32: -0.0080 S33: 0.0046
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 3ESY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049727.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-DEC-07
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NONIUS KAPPA CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22468
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.390
REMARK 200 RESOLUTION RANGE LOW (A) : 47.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 7.800
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.39
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.48
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : 4.80
REMARK 200 R MERGE FOR SHELL (I) : 0.38700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1FLV
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 38.02
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 4000, 0.2-0.3M MAGNESIUM
REMARK 280 CHLORIDE, 0.1M TRIS/HCL PH 8.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 36.64350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 54.57200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.41150
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 54.57200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.64350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.41150
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 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 350
REMARK 350 BIOMOLECULE: 2
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: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 SER A 1
REMARK 465 SER B 1
REMARK 465 SER C 1
REMARK 465 SER D 1
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 155 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 LEU D 6 CA - CB - CG ANGL. DEV. = 14.4 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 ILE B 59 71.55 66.33
REMARK 500 ASN B 97 38.88 -140.43
REMARK 500 ILE C 59 80.79 59.62
REMARK 500 GLN C 148 42.17 -143.30
REMARK 500 ILE D 59 74.47 52.71
REMARK 500 SER D 71 -39.46 -34.06
REMARK 500 ASN D 97 34.91 -140.02
REMARK 500 GLN D 148 43.70 -140.97
REMARK 500 SER D 165 -70.97 -61.76
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 FMN A 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2431
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN B 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN C 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN D 170
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 2432
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ESX RELATED DB: PDB
REMARK 900 E16KE61KD126KD150K FLAVODOXIN FROM ANABAENA
REMARK 900 RELATED ID: 3ESZ RELATED DB: PDB
REMARK 900 K2AK3A FLAVODOXIN FROM ANABAENA
DBREF 3ESY A 1 169 UNP P0A3E0 FLAV_ANASO 2 170
DBREF 3ESY B 1 169 UNP P0A3E0 FLAV_ANASO 2 170
DBREF 3ESY C 1 169 UNP P0A3E0 FLAV_ANASO 2 170
DBREF 3ESY D 1 169 UNP P0A3E0 FLAV_ANASO 2 170
SEQADV 3ESY LYS A 16 UNP P0A3E0 GLU 17 ENGINEERED MUTATION
SEQADV 3ESY LYS A 61 UNP P0A3E0 GLU 62 ENGINEERED MUTATION
SEQADV 3ESY LYS B 16 UNP P0A3E0 GLU 17 ENGINEERED MUTATION
SEQADV 3ESY LYS B 61 UNP P0A3E0 GLU 62 ENGINEERED MUTATION
SEQADV 3ESY LYS C 16 UNP P0A3E0 GLU 17 ENGINEERED MUTATION
SEQADV 3ESY LYS C 61 UNP P0A3E0 GLU 62 ENGINEERED MUTATION
SEQADV 3ESY LYS D 16 UNP P0A3E0 GLU 17 ENGINEERED MUTATION
SEQADV 3ESY LYS D 61 UNP P0A3E0 GLU 62 ENGINEERED MUTATION
SEQRES 1 A 169 SER LYS LYS ILE GLY LEU PHE TYR GLY THR GLN THR GLY
SEQRES 2 A 169 LYS THR LYS SER VAL ALA GLU ILE ILE ARG ASP GLU PHE
SEQRES 3 A 169 GLY ASN ASP VAL VAL THR LEU HIS ASP VAL SER GLN ALA
SEQRES 4 A 169 GLU VAL THR ASP LEU ASN ASP TYR GLN TYR LEU ILE ILE
SEQRES 5 A 169 GLY CYS PRO THR TRP ASN ILE GLY LYS LEU GLN SER ASP
SEQRES 6 A 169 TRP GLU GLY LEU TYR SER GLU LEU ASP ASP VAL ASP PHE
SEQRES 7 A 169 ASN GLY LYS LEU VAL ALA TYR PHE GLY THR GLY ASP GLN
SEQRES 8 A 169 ILE GLY TYR ALA ASP ASN PHE GLN ASP ALA ILE GLY ILE
SEQRES 9 A 169 LEU GLU GLU LYS ILE SER GLN ARG GLY GLY LYS THR VAL
SEQRES 10 A 169 GLY TYR TRP SER THR ASP GLY TYR ASP PHE ASN ASP SER
SEQRES 11 A 169 LYS ALA LEU ARG ASN GLY LYS PHE VAL GLY LEU ALA LEU
SEQRES 12 A 169 ASP GLU ASP ASN GLN SER ASP LEU THR ASP ASP ARG ILE
SEQRES 13 A 169 LYS SER TRP VAL ALA GLN LEU LYS SER GLU PHE GLY LEU
SEQRES 1 B 169 SER LYS LYS ILE GLY LEU PHE TYR GLY THR GLN THR GLY
SEQRES 2 B 169 LYS THR LYS SER VAL ALA GLU ILE ILE ARG ASP GLU PHE
SEQRES 3 B 169 GLY ASN ASP VAL VAL THR LEU HIS ASP VAL SER GLN ALA
SEQRES 4 B 169 GLU VAL THR ASP LEU ASN ASP TYR GLN TYR LEU ILE ILE
SEQRES 5 B 169 GLY CYS PRO THR TRP ASN ILE GLY LYS LEU GLN SER ASP
SEQRES 6 B 169 TRP GLU GLY LEU TYR SER GLU LEU ASP ASP VAL ASP PHE
SEQRES 7 B 169 ASN GLY LYS LEU VAL ALA TYR PHE GLY THR GLY ASP GLN
SEQRES 8 B 169 ILE GLY TYR ALA ASP ASN PHE GLN ASP ALA ILE GLY ILE
SEQRES 9 B 169 LEU GLU GLU LYS ILE SER GLN ARG GLY GLY LYS THR VAL
SEQRES 10 B 169 GLY TYR TRP SER THR ASP GLY TYR ASP PHE ASN ASP SER
SEQRES 11 B 169 LYS ALA LEU ARG ASN GLY LYS PHE VAL GLY LEU ALA LEU
SEQRES 12 B 169 ASP GLU ASP ASN GLN SER ASP LEU THR ASP ASP ARG ILE
SEQRES 13 B 169 LYS SER TRP VAL ALA GLN LEU LYS SER GLU PHE GLY LEU
SEQRES 1 C 169 SER LYS LYS ILE GLY LEU PHE TYR GLY THR GLN THR GLY
SEQRES 2 C 169 LYS THR LYS SER VAL ALA GLU ILE ILE ARG ASP GLU PHE
SEQRES 3 C 169 GLY ASN ASP VAL VAL THR LEU HIS ASP VAL SER GLN ALA
SEQRES 4 C 169 GLU VAL THR ASP LEU ASN ASP TYR GLN TYR LEU ILE ILE
SEQRES 5 C 169 GLY CYS PRO THR TRP ASN ILE GLY LYS LEU GLN SER ASP
SEQRES 6 C 169 TRP GLU GLY LEU TYR SER GLU LEU ASP ASP VAL ASP PHE
SEQRES 7 C 169 ASN GLY LYS LEU VAL ALA TYR PHE GLY THR GLY ASP GLN
SEQRES 8 C 169 ILE GLY TYR ALA ASP ASN PHE GLN ASP ALA ILE GLY ILE
SEQRES 9 C 169 LEU GLU GLU LYS ILE SER GLN ARG GLY GLY LYS THR VAL
SEQRES 10 C 169 GLY TYR TRP SER THR ASP GLY TYR ASP PHE ASN ASP SER
SEQRES 11 C 169 LYS ALA LEU ARG ASN GLY LYS PHE VAL GLY LEU ALA LEU
SEQRES 12 C 169 ASP GLU ASP ASN GLN SER ASP LEU THR ASP ASP ARG ILE
SEQRES 13 C 169 LYS SER TRP VAL ALA GLN LEU LYS SER GLU PHE GLY LEU
SEQRES 1 D 169 SER LYS LYS ILE GLY LEU PHE TYR GLY THR GLN THR GLY
SEQRES 2 D 169 LYS THR LYS SER VAL ALA GLU ILE ILE ARG ASP GLU PHE
SEQRES 3 D 169 GLY ASN ASP VAL VAL THR LEU HIS ASP VAL SER GLN ALA
SEQRES 4 D 169 GLU VAL THR ASP LEU ASN ASP TYR GLN TYR LEU ILE ILE
SEQRES 5 D 169 GLY CYS PRO THR TRP ASN ILE GLY LYS LEU GLN SER ASP
SEQRES 6 D 169 TRP GLU GLY LEU TYR SER GLU LEU ASP ASP VAL ASP PHE
SEQRES 7 D 169 ASN GLY LYS LEU VAL ALA TYR PHE GLY THR GLY ASP GLN
SEQRES 8 D 169 ILE GLY TYR ALA ASP ASN PHE GLN ASP ALA ILE GLY ILE
SEQRES 9 D 169 LEU GLU GLU LYS ILE SER GLN ARG GLY GLY LYS THR VAL
SEQRES 10 D 169 GLY TYR TRP SER THR ASP GLY TYR ASP PHE ASN ASP SER
SEQRES 11 D 169 LYS ALA LEU ARG ASN GLY LYS PHE VAL GLY LEU ALA LEU
SEQRES 12 D 169 ASP GLU ASP ASN GLN SER ASP LEU THR ASP ASP ARG ILE
SEQRES 13 D 169 LYS SER TRP VAL ALA GLN LEU LYS SER GLU PHE GLY LEU
HET FMN A 170 31
HET GOL A2431 6
HET FMN B 170 31
HET FMN C 170 31
HET FMN D 170 31
HET GOL D2432 6
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM GOL GLYCEROL
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 FMN 4(C17 H21 N4 O9 P)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 11 HOH *297(H2 O)
HELIX 1 1 GLY A 13 GLY A 27 1 15
HELIX 2 2 GLU A 40 TYR A 47 5 8
HELIX 3 3 GLN A 63 SER A 71 1 9
HELIX 4 4 GLU A 72 VAL A 76 5 5
HELIX 5 5 GLN A 99 ARG A 112 1 14
HELIX 6 6 GLN A 148 ASP A 150 5 3
HELIX 7 7 LEU A 151 GLY A 168 1 18
HELIX 8 8 GLY B 13 GLY B 27 1 15
HELIX 9 9 GLU B 40 TYR B 47 5 8
HELIX 10 10 GLN B 63 SER B 71 1 9
HELIX 11 11 GLU B 72 VAL B 76 5 5
HELIX 12 12 GLN B 99 ARG B 112 1 14
HELIX 13 13 LEU B 151 PHE B 167 1 17
HELIX 14 14 GLY C 13 GLY C 27 1 15
HELIX 15 15 SER C 37 ALA C 39 5 3
HELIX 16 16 GLU C 40 TYR C 47 5 8
HELIX 17 17 GLN C 63 SER C 71 1 9
HELIX 18 18 GLU C 72 VAL C 76 5 5
HELIX 19 19 GLN C 99 ARG C 112 1 14
HELIX 20 20 LEU C 151 GLY C 168 1 18
HELIX 21 21 GLY D 13 GLY D 27 1 15
HELIX 22 22 SER D 37 ALA D 39 5 3
HELIX 23 23 GLU D 40 TYR D 47 5 8
HELIX 24 24 GLN D 63 SER D 71 1 9
HELIX 25 25 GLU D 72 VAL D 76 5 5
HELIX 26 26 GLN D 99 ARG D 112 1 14
HELIX 27 27 LEU D 151 GLY D 168 1 18
SHEET 1 A 5 VAL A 31 ASP A 35 0
SHEET 2 A 5 ILE A 4 TYR A 8 1 N LEU A 6 O HIS A 34
SHEET 3 A 5 TYR A 49 GLY A 53 1 O ILE A 51 N PHE A 7
SHEET 4 A 5 LEU A 82 THR A 88 1 O ALA A 84 N ILE A 52
SHEET 5 A 5 LYS A 115 THR A 116 1 O LYS A 115 N VAL A 83
SHEET 1 B 5 VAL A 31 ASP A 35 0
SHEET 2 B 5 ILE A 4 TYR A 8 1 N LEU A 6 O HIS A 34
SHEET 3 B 5 TYR A 49 GLY A 53 1 O ILE A 51 N PHE A 7
SHEET 4 B 5 LEU A 82 THR A 88 1 O ALA A 84 N ILE A 52
SHEET 5 B 5 LEU A 141 LEU A 143 1 O LEU A 143 N GLY A 87
SHEET 1 C 2 THR A 56 TRP A 57 0
SHEET 2 C 2 LYS A 61 LEU A 62 -1 O LYS A 61 N TRP A 57
SHEET 1 D 2 LEU A 133 ARG A 134 0
SHEET 2 D 2 LYS A 137 PHE A 138 -1 O LYS A 137 N ARG A 134
SHEET 1 E 5 VAL B 31 ASP B 35 0
SHEET 2 E 5 ILE B 4 TYR B 8 1 N LEU B 6 O HIS B 34
SHEET 3 E 5 TYR B 49 GLY B 53 1 O ILE B 51 N PHE B 7
SHEET 4 E 5 LEU B 82 THR B 88 1 O ALA B 84 N ILE B 52
SHEET 5 E 5 LYS B 115 THR B 116 1 O LYS B 115 N VAL B 83
SHEET 1 F 5 VAL B 31 ASP B 35 0
SHEET 2 F 5 ILE B 4 TYR B 8 1 N LEU B 6 O HIS B 34
SHEET 3 F 5 TYR B 49 GLY B 53 1 O ILE B 51 N PHE B 7
SHEET 4 F 5 LEU B 82 THR B 88 1 O ALA B 84 N ILE B 52
SHEET 5 F 5 LEU B 141 LEU B 143 1 O LEU B 143 N GLY B 87
SHEET 1 G 2 THR B 56 TRP B 57 0
SHEET 2 G 2 LYS B 61 LEU B 62 -1 O LYS B 61 N TRP B 57
SHEET 1 H 2 LEU B 133 ARG B 134 0
SHEET 2 H 2 LYS B 137 PHE B 138 -1 O LYS B 137 N ARG B 134
SHEET 1 I 5 VAL C 31 ASP C 35 0
SHEET 2 I 5 ILE C 4 TYR C 8 1 N LEU C 6 O HIS C 34
SHEET 3 I 5 TYR C 49 GLY C 53 1 O TYR C 49 N GLY C 5
SHEET 4 I 5 LEU C 82 THR C 88 1 O ALA C 84 N LEU C 50
SHEET 5 I 5 LYS C 115 THR C 116 1 O LYS C 115 N VAL C 83
SHEET 1 J 5 VAL C 31 ASP C 35 0
SHEET 2 J 5 ILE C 4 TYR C 8 1 N LEU C 6 O HIS C 34
SHEET 3 J 5 TYR C 49 GLY C 53 1 O TYR C 49 N GLY C 5
SHEET 4 J 5 LEU C 82 THR C 88 1 O ALA C 84 N LEU C 50
SHEET 5 J 5 LEU C 141 LEU C 143 1 O LEU C 143 N GLY C 87
SHEET 1 K 2 THR C 56 TRP C 57 0
SHEET 2 K 2 LYS C 61 LEU C 62 -1 O LYS C 61 N TRP C 57
SHEET 1 L 3 TRP C 120 SER C 121 0
SHEET 2 L 3 LYS C 137 PHE C 138 -1 O PHE C 138 N TRP C 120
SHEET 3 L 3 LEU C 133 ARG C 134 -1 N ARG C 134 O LYS C 137
SHEET 1 M 5 VAL D 31 ASP D 35 0
SHEET 2 M 5 ILE D 4 TYR D 8 1 N LEU D 6 O HIS D 34
SHEET 3 M 5 TYR D 49 GLY D 53 1 O TYR D 49 N GLY D 5
SHEET 4 M 5 LEU D 82 THR D 88 1 O ALA D 84 N ILE D 52
SHEET 5 M 5 LYS D 115 THR D 116 1 O LYS D 115 N VAL D 83
SHEET 1 N 5 VAL D 31 ASP D 35 0
SHEET 2 N 5 ILE D 4 TYR D 8 1 N LEU D 6 O HIS D 34
SHEET 3 N 5 TYR D 49 GLY D 53 1 O TYR D 49 N GLY D 5
SHEET 4 N 5 LEU D 82 THR D 88 1 O ALA D 84 N ILE D 52
SHEET 5 N 5 LEU D 141 LEU D 143 1 O LEU D 143 N GLY D 87
SHEET 1 O 2 THR D 56 TRP D 57 0
SHEET 2 O 2 LYS D 61 LEU D 62 -1 O LYS D 61 N TRP D 57
SHEET 1 P 2 TRP D 120 SER D 121 0
SHEET 2 P 2 LYS D 137 PHE D 138 -1 O PHE D 138 N TRP D 120
CISPEP 1 ASN A 58 ILE A 59 0 -7.57
SITE 1 AC1 23 THR A 10 GLN A 11 THR A 12 GLY A 13
SITE 2 AC1 23 LYS A 14 THR A 15 TYR A 49 PRO A 55
SITE 3 AC1 23 THR A 56 TRP A 57 ASN A 58 THR A 88
SITE 4 AC1 23 GLY A 89 ASP A 90 TYR A 94 ASN A 97
SITE 5 AC1 23 PHE A 98 GLN A 99 ASP A 146 HOH A2466
SITE 6 AC1 23 HOH A2470 HOH A2481 HOH A2491
SITE 1 AC2 2 THR A 12 HOH A2452
SITE 1 AC3 22 THR B 10 GLN B 11 THR B 12 GLY B 13
SITE 2 AC3 22 LYS B 14 THR B 15 PRO B 55 THR B 56
SITE 3 AC3 22 TRP B 57 ASN B 58 ILE B 59 GLY B 60
SITE 4 AC3 22 THR B 88 GLY B 89 ASP B 90 TYR B 94
SITE 5 AC3 22 ASN B 97 PHE B 98 GLN B 99 ASP B 146
SITE 6 AC3 22 HOH B 200 GLU C 67
SITE 1 AC4 23 THR C 10 GLN C 11 THR C 12 GLY C 13
SITE 2 AC4 23 LYS C 14 THR C 15 PRO C 55 THR C 56
SITE 3 AC4 23 TRP C 57 ASN C 58 ILE C 59 GLY C 60
SITE 4 AC4 23 THR C 88 GLY C 89 ASP C 90 TYR C 94
SITE 5 AC4 23 ASN C 97 PHE C 98 GLN C 99 ASP C 146
SITE 6 AC4 23 HOH C 188 HOH C 196 HOH C 315
SITE 1 AC5 22 THR D 10 GLN D 11 THR D 12 GLY D 13
SITE 2 AC5 22 LYS D 14 THR D 15 PRO D 55 THR D 56
SITE 3 AC5 22 TRP D 57 ASN D 58 ILE D 59 GLY D 60
SITE 4 AC5 22 THR D 88 GLY D 89 ASP D 90 TYR D 94
SITE 5 AC5 22 ASN D 97 PHE D 98 GLN D 99 ASP D 146
SITE 6 AC5 22 HOH D 173 HOH D 320
SITE 1 AC6 5 THR C 116 TYR C 119 THR D 10 GLN D 11
SITE 2 AC6 5 HOH D2445
CRYST1 73.287 74.823 109.144 90.00 90.00 90.00 P 21 21 21 16
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013645 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013365 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009162 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
