HEADER FLAVOPROTEIN 07-JUN-18 6GPV
TITLE CRYSTAL STRUCTURE OF BLUE-LIGHT IRRADIATED MINISOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOTOTROPIN-2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DEFECTIVE IN CHLOROPLAST AVOIDANCE PROTEIN 1,NON-PHOTOTROPIC
COMPND 5 HYPOCOTYL 1-LIKE PROTEIN 1,NPH1-LIKE PROTEIN 1;
COMPND 6 EC: 2.7.11.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: EFIPNPLLG
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;
SOURCE 3 ORGANISM_COMMON: THALE CRESS;
SOURCE 4 ORGANISM_TAXID: 3702;
SOURCE 5 GENE: PHOT2, CAV1, KIN7, NPL1, AT5G58140, K21L19.6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693
KEYWDS SINGLET OXYGEN, FLUORESCENT PROTEIN, FMN, PROTEIN OXIDATION, GAMMA-
KEYWDS 2 PEROXOTYROSINE, OXIDIZED HISTIDINE, N-FORMYLKYNURENIN, FLAVOPROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.LAFAYE,L.SIGNOR,S.AUMONIER,X.SHU,G.GOTTHARD,A.ROYANT
REVDAT 3 17-JAN-24 6GPV 1 LINK
REVDAT 2 06-MAR-19 6GPV 1 JRNL
REVDAT 1 27-FEB-19 6GPV 0
JRNL AUTH J.TORRA,C.LAFAYE,L.SIGNOR,S.AUMONIER,C.FLORS,X.SHU,S.NONELL,
JRNL AUTH 2 G.GOTTHARD,A.ROYANT
JRNL TITL TAILING MINISOG: STRUCTURAL BASES OF THE COMPLEX
JRNL TITL 2 PHOTOPHYSICS OF A FLAVIN-BINDING SINGLET OXYGEN
JRNL TITL 3 PHOTOSENSITIZING PROTEIN.
JRNL REF SCI REP V. 9 2428 2019
JRNL REFN ESSN 2045-2322
JRNL PMID 30787421
JRNL DOI 10.1038/S41598-019-38955-3
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0218
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 7734
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.240
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.700
REMARK 3 FREE R VALUE TEST SET COUNT : 384
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 551
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2540
REMARK 3 BIN FREE R VALUE SET COUNT : 31
REMARK 3 BIN FREE R VALUE : 0.2780
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 913
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 51
REMARK 3 SOLVENT ATOMS : 126
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.47
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.02000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.04000
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): 0.227
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.190
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.144
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.396
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.920
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1083 ; 0.010 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 1011 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1477 ; 1.554 ; 2.085
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2355 ; 0.898 ; 3.008
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 137 ;23.658 ; 5.474
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 50 ;29.269 ;23.600
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 191 ;15.467 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;19.938 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 159 ; 0.073 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1245 ; 0.006 ; 0.022
REMARK 3 GENERAL PLANES OTHERS (A): 224 ; 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): 472 ; 2.298 ; 3.279
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 472 ; 2.298 ; 3.279
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 578 ; 3.588 ; 4.907
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 579 ; 3.585 ; 4.906
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 611 ; 2.418 ; 3.562
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 612 ; 2.416 ; 3.561
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 882 ; 4.005 ; 5.195
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 1466 ; 7.621 ;37.940
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 1450 ; 7.562 ;37.615
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 : NULL
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 6GPV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUN-18.
REMARK 100 THE DEPOSITION ID IS D_1200010385.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : SI(311)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8116
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 80.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.70
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: PHASER
REMARK 200 STARTING MODEL: 4EEP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.97
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS-HCL PH 8.0, 20 MM MGCL2,
REMARK 280 28% PEG 4000, 0 OR 15 MM COCL2, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 66.88000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 20.25000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 20.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 100.32000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 20.25000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 20.25000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.44000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 20.25000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 20.25000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 100.32000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 20.25000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 20.25000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 33.44000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 66.88000
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 TOTAL BURIED SURFACE AREA: 1610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
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 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 PRO A 110
REMARK 465 ASN A 111
REMARK 465 PRO A 112
REMARK 465 LEU A 113
REMARK 465 LEU A 114
REMARK 465 GLY A 115
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 3 CD CE NZ
REMARK 470 GLU A 33 CD OE1 OE2
REMARK 470 GLU A 65 CD OE1 OE2
REMARK 470 GLN A 92 CG CD OE1 NE2
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 O HOH A 1171 O HOH A 1220 2.18
REMARK 500 OE1 GLN A 54 NH1 ARG A 57 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 F7Q A 73 C - N - CA ANGL. DEV. = 15.3 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 F7Q A 73 -12.85
REMARK 500 PHE A 80 12.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1225 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH A1226 DISTANCE = 7.50 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A1104 O
REMARK 620 2 HOH A1114 O 87.8
REMARK 620 3 HOH A1116 O 90.4 85.0
REMARK 620 4 HOH A1212 O 165.6 85.1 101.4
REMARK 620 5 HOH A1216 O 106.8 162.8 85.9 82.3
REMARK 620 N 1 2 3 4
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 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue LUM A 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues F7Q A 73
REMARK 800 through THR A 74 bound to ASN A 72
DBREF 6GPV A 1 106 UNP P93025 PHOT2_ARATH 387 492
SEQADV 6GPV MET A 1 UNP P93025 ILE 387 CONFLICT
SEQADV 6GPV SER A 4 UNP P93025 ASN 390 CONFLICT
SEQADV 6GPV THR A 8 UNP P93025 SER 394 CONFLICT
SEQADV 6GPV GLY A 23 UNP P93025 SER 409 CONFLICT
SEQADV 6GPV GLY A 40 UNP P93025 CYS 426 CONFLICT
SEQADV 6GPV LEU A 84 UNP P93025 PHE 470 CONFLICT
SEQADV 6GPV HOO A 85 UNP P93025 HIS 471 MICROHETEROGENEITY
SEQADV 6GPV GLU A 107 UNP P93025 EXPRESSION TAG
SEQADV 6GPV PHE A 108 UNP P93025 EXPRESSION TAG
SEQADV 6GPV ILE A 109 UNP P93025 EXPRESSION TAG
SEQADV 6GPV PRO A 110 UNP P93025 EXPRESSION TAG
SEQADV 6GPV ASN A 111 UNP P93025 EXPRESSION TAG
SEQADV 6GPV PRO A 112 UNP P93025 EXPRESSION TAG
SEQADV 6GPV LEU A 113 UNP P93025 EXPRESSION TAG
SEQADV 6GPV LEU A 114 UNP P93025 EXPRESSION TAG
SEQADV 6GPV GLY A 115 UNP P93025 EXPRESSION TAG
SEQRES 1 A 115 MET GLU LYS SER PHE VAL ILE THR ASP PRO ARG LEU PRO
SEQRES 2 A 115 ASP ASN PRO ILE ILE PHE ALA SER ASP GLY PHE LEU GLU
SEQRES 3 A 115 LEU THR GLU TYR SER ARG GLU GLU ILE LEU GLY ARG ASN
SEQRES 4 A 115 GLY ARG PHE LEU GLN GLY PRO GLU THR ASP GLN ALA THR
SEQRES 5 A 115 VAL GLN LYS ILE ARG ASP ALA ILE ARG ASP GLN ARG GLU
SEQRES 6 A 115 ILE THR VAL GLN LEU ILE ASN TYR THR LYS SER GLY LYS
SEQRES 7 A 115 LYS PHE NFK ASN LEU LEU HOO LEU GLN PRO MET ARG ASP
SEQRES 8 A 115 GLN LYS GLY GLU LEU GLN TYR PHE ILE GLY VAL GLN LEU
SEQRES 9 A 115 ASP GLY GLU PHE ILE PRO ASN PRO LEU LEU GLY
MODRES 6GPV NFK A 81 TRP MODIFIED RESIDUE
MODRES 6GPV HOO A 85 HIS MODIFIED RESIDUE
HET F7Q A 73 14
HET NFK A 81 16
HET HOO A 85 12
HET OHI A 85 11
HET FMN A1001 31
HET MG A1002 1
HET CL A1003 1
HET LUM A1004 18
HETNAM F7Q (2~{S})-2-AZANYL-3-[1-(DIOXIDANYL)-4-OXIDANYLIDENE-
HETNAM 2 F7Q CYCLOHEXA-2,5-DIEN-1-YL]PROPANOIC ACID
HETNAM NFK N'-FORMYLKYNURENINE
HETNAM HOO (2~{S})-2-AZANYL-3-[2,5-BIS(OXIDANYLIDENE)IMIDAZOL-4-
HETNAM 2 HOO YL]PROPANOIC ACID
HETNAM OHI 3-(2-OXO-2H-IMIDAZOL-4-YL)-L-ALANINE
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM MG MAGNESIUM ION
HETNAM CL CHLORIDE ION
HETNAM LUM LUMICHROME
HETSYN NFK (2S)-2-AMINO-4-[2-(FORMYLAMINO)PHENYL]-4-OXOBUTANOIC
HETSYN 2 NFK ACID
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
HETSYN LUM 7,8-DIMETHYLALLOXAZINE; 6,7-DIMETHYLALLOXAZINE
FORMUL 1 F7Q C9 H11 N O5
FORMUL 1 NFK C11 H12 N2 O4
FORMUL 1 HOO C6 H7 N3 O4
FORMUL 1 OHI C6 H7 N3 O3
FORMUL 2 FMN C17 H21 N4 O9 P
FORMUL 3 MG MG 2+
FORMUL 4 CL CL 1-
FORMUL 5 LUM C12 H10 N4 O2
FORMUL 6 HOH *126(H2 O)
HELIX 1 AA1 SER A 21 GLU A 29 1 9
HELIX 2 AA2 SER A 31 ILE A 35 5 5
HELIX 3 AA3 ASN A 39 GLN A 44 5 6
HELIX 4 AA4 ASP A 49 ASP A 62 1 14
SHEET 1 AA1 5 ILE A 17 ALA A 20 0
SHEET 2 AA1 5 SER A 4 THR A 8 -1 N ILE A 7 O ILE A 18
SHEET 3 AA1 5 LEU A 96 ASP A 105 -1 O GLY A 101 N VAL A 6
SHEET 4 AA1 5 LYS A 79 ARG A 90 -1 N LEU A 83 O LEU A 104
SHEET 5 AA1 5 ILE A 66 TYR A 73 -1 N ILE A 66 O LEU A 86
LINK C ASN A 72 N BF7Q A 73 1555 1555 1.33
LINK C BF7Q A 73 N THR A 74 1555 1555 1.32
LINK C PHE A 80 N NFK A 81 1555 1555 1.32
LINK C NFK A 81 N ASN A 82 1555 1555 1.33
LINK C LEU A 84 N AHOO A 85 1555 1555 1.34
LINK C LEU A 84 N BOHI A 85 1555 1555 1.34
LINK C AHOO A 85 N LEU A 86 1555 1555 1.35
LINK C BOHI A 85 N LEU A 86 1555 1555 1.35
LINK MG A MG A1002 O AHOH A1104 1555 1555 2.07
LINK MG A MG A1002 O AHOH A1114 1555 1555 2.37
LINK MG A MG A1002 O AHOH A1116 1555 1555 2.07
LINK MG A MG A1002 O AHOH A1212 1555 1555 2.01
LINK MG A MG A1002 O AHOH A1216 1555 1555 2.05
SITE 1 AC1 28 VAL A 6 THR A 8 ASN A 39 GLY A 40
SITE 2 AC1 28 ARG A 41 LEU A 43 GLN A 44 VAL A 53
SITE 3 AC1 28 ILE A 56 ARG A 57 ILE A 60 LEU A 70
SITE 4 AC1 28 ASN A 72 ASN A 82 LEU A 84 LEU A 86
SITE 5 AC1 28 PHE A 99 ILE A 100 GLY A 101 GLN A 103
SITE 6 AC1 28 CL A1003 LUM A1004 HOH A1110 HOH A1114
SITE 7 AC1 28 HOH A1116 HOH A1157 HOH A1167 HOH A1193
SITE 1 AC2 5 HOH A1104 HOH A1114 HOH A1116 HOH A1212
SITE 2 AC2 5 HOH A1216
SITE 1 AC3 4 ASN A 15 ASN A 39 ILE A 60 FMN A1001
SITE 1 AC4 15 VAL A 6 THR A 8 ASN A 15 GLY A 40
SITE 2 AC4 15 LEU A 43 GLN A 44 ASN A 72 ASN A 82
SITE 3 AC4 15 LEU A 84 LEU A 86 PHE A 99 ILE A 100
SITE 4 AC4 15 GLY A 101 GLN A 103 FMN A1001
SITE 1 AC5 17 LEU A 27 THR A 28 GLU A 29 LEU A 43
SITE 2 AC5 17 GLY A 45 PRO A 46 GLU A 47 ILE A 71
SITE 3 AC5 17 ASN A 72 LYS A 75 SER A 76 GLY A 77
SITE 4 AC5 17 LYS A 78 LYS A 79 PHE A 80 HOH A1126
SITE 5 AC5 17 HOH A1133
CRYST1 40.500 40.500 133.760 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.024691 0.000000 0.000000 0.00000
SCALE2 0.000000 0.024691 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007476 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
