HEADER OXIDOREDUCTASE 08-AUG-13 4C0W
TITLE THE CRYSTAL STRUCUTURE OF NATIVE PPAZOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FMN-DEPENDENT NADH-AZOREDUCTASE 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: AZO-DYE REDUCTASE 1, FMN-DEPENDENT NADH-AZO COMPOUND
COMPND 5 OXIDOREDUCTASE 1, AZOREDUCTASE;
COMPND 6 EC: 1.7.-.-, 1.6.5.2;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 ORGANISM_TAXID: 303;
SOURCE 4 STRAIN: MET94;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: TUNER;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-21A
KEYWDS OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.M.D.GONCALVES,D.DE SANCTIS,I.BENTO
REVDAT 3 06-MAR-19 4C0W 1 REMARK
REVDAT 2 18-DEC-13 4C0W 1 JRNL
REVDAT 1 30-OCT-13 4C0W 0
JRNL AUTH A.M.D.GONCALVES,S.MENDES,D.DE SANCTIS,L.O.MARTINS,I.BENTO
JRNL TITL THE CRYSTAL STRUCTURE OF PSEUDOMONAS PUTIDA AZOR: THE ACTIVE
JRNL TITL 2 SITE REVISITED.
JRNL REF FEBS J. V. 280 6643 2013
JRNL REFN ISSN 1742-464X
JRNL PMID 24127652
JRNL DOI 10.1111/FEBS.12568
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 26.13
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 33239
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.179
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1683
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 26.1334 - 3.6600 0.91 2536 134 0.1561 0.1922
REMARK 3 2 3.6600 - 2.9063 0.98 2645 137 0.1439 0.1627
REMARK 3 3 2.9063 - 2.5393 0.99 2673 139 0.1399 0.1420
REMARK 3 4 2.5393 - 2.3073 1.00 2623 146 0.1340 0.1529
REMARK 3 5 2.3073 - 2.1420 1.00 2613 153 0.1330 0.1670
REMARK 3 6 2.1420 - 2.0157 1.00 2666 140 0.1450 0.1901
REMARK 3 7 2.0157 - 1.9148 1.00 2634 143 0.1677 0.2139
REMARK 3 8 1.9148 - 1.8315 1.00 2650 128 0.1760 0.1823
REMARK 3 9 1.8315 - 1.7610 1.00 2618 147 0.1790 0.2120
REMARK 3 10 1.7610 - 1.7002 1.00 2638 141 0.1910 0.2516
REMARK 3 11 1.7002 - 1.6471 1.00 2652 118 0.1925 0.2154
REMARK 3 12 1.6471 - 1.6000 1.00 2608 157 0.1955 0.2221
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.150
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.950
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 17.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.010 1673
REMARK 3 ANGLE : 1.280 2288
REMARK 3 CHIRALITY : 0.080 261
REMARK 3 PLANARITY : 0.006 292
REMARK 3 DIHEDRAL : 13.212 621
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4C0W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-AUG-13.
REMARK 100 THE DEPOSITION ID IS D_1290057952.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33249
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 53.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.300
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 4% PEG 400, 2M AMMONIUM SULPHATE, 0.1M
REMARK 280 HEPES PH 7.0 AT 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: F 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z+1/2
REMARK 290 7555 -X,Y+1/2,-Z+1/2
REMARK 290 8555 X,-Y+1/2,-Z+1/2
REMARK 290 9555 X+1/2,Y,Z+1/2
REMARK 290 10555 -X+1/2,-Y,Z+1/2
REMARK 290 11555 -X+1/2,Y,-Z+1/2
REMARK 290 12555 X+1/2,-Y,-Z+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z
REMARK 290 14555 -X+1/2,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y+1/2,-Z
REMARK 290 16555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.87150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 73.26950
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.87150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 73.26950
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.87150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 73.26950
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 47.87150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 73.26950
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 36.14950
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 73.26950
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 36.14950
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 73.26950
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 36.14950
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 73.26950
REMARK 290 SMTRY1 12 1.000000 0.000000 0.000000 36.14950
REMARK 290 SMTRY2 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 73.26950
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 36.14950
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 47.87150
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 36.14950
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 47.87150
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 36.14950
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 47.87150
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 36.14950
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 47.87150
REMARK 290 SMTRY3 16 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17090 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.9 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 350 BIOMT1 2 -1.000000 0.000000 0.000000 72.29900
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2055 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2080 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2154 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2198 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2275 LIES ON A SPECIAL POSITION.
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 VAL A 202
REMARK 465 ALA A 203
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 ALA A 201 CA C O CB
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 2031 O HOH A 2032 1.81
REMARK 500 O HOH A 2072 O HOH A 2165 1.87
REMARK 500 O HOH A 2013 O HOH A 2036 1.98
REMARK 500 O HOH A 2033 O HOH A 2035 2.03
REMARK 500 OH TYR A 179 O HOH A 2225 2.05
REMARK 500 O22 12P A 1202 O HOH A 2301 2.06
REMARK 500 O HOH A 2142 O HOH A 2233 2.09
REMARK 500 O HOH A 2287 O HOH A 2288 2.10
REMARK 500 OE1 GLU A 26 O HOH A 2091 2.13
REMARK 500 O HOH A 2133 O HOH A 2134 2.13
REMARK 500 O HOH A 2246 O HOH A 2249 2.15
REMARK 500 O HOH A 2008 O HOH A 2011 2.16
REMARK 500 O HOH A 2010 O HOH A 2096 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2262 O HOH A 2288 11555 1.99
REMARK 500 O HOH A 2139 O HOH A 2242 2655 2.09
REMARK 500 O HOH A 2142 O HOH A 2144 2655 2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 116 -56.16 -121.38
REMARK 500 HIS A 153 -98.41 -106.38
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 A2043 DISTANCE = 6.05 ANGSTROMS
REMARK 525 HOH A2055 DISTANCE = 7.03 ANGSTROMS
REMARK 525 HOH A2068 DISTANCE = 6.22 ANGSTROMS
REMARK 525 HOH A2080 DISTANCE = 6.75 ANGSTROMS
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 12P A 1202
REMARK 610 12P A 1203
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 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 12P A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 12P A 1203
DBREF 4C0W A 1 203 UNP Q88IY3 AZOR1_PSEPK 1 203
SEQADV 4C0W VAL A 202 UNP Q88IY3 ALA 202 CONFLICT
SEQRES 1 A 203 MET LYS LEU LEU HIS ILE ASP SER SER ILE LEU GLY ASP
SEQRES 2 A 203 ASN SER ALA SER ARG GLN LEU SER ARG GLU VAL VAL GLU
SEQRES 3 A 203 ALA TRP LYS ALA ALA ASP PRO SER VAL GLU VAL VAL TYR
SEQRES 4 A 203 ARG ASP LEU ALA ALA ASP ALA ILE ALA HIS PHE SER ALA
SEQRES 5 A 203 ALA THR LEU VAL ALA ALA GLY THR PRO GLU ASP VAL ARG
SEQRES 6 A 203 ASP ALA ALA GLN ALA PHE GLU ALA LYS LEU SER ALA GLU
SEQRES 7 A 203 THR LEU GLU GLU PHE LEU ALA ALA ASP ALA VAL VAL ILE
SEQRES 8 A 203 GLY ALA PRO MET TYR ASN PHE THR VAL PRO THR GLN LEU
SEQRES 9 A 203 LYS ALA TRP ILE ASP ARG VAL ALA VAL ALA GLY LYS THR
SEQRES 10 A 203 PHE ARG TYR THR GLU ALA GLY PRO GLN GLY LEU CYS GLY
SEQRES 11 A 203 ASN LYS LYS VAL VAL LEU VAL SER THR ALA GLY GLY LEU
SEQRES 12 A 203 HIS ALA GLY GLN PRO THR GLY ALA GLY HIS GLU ASP PHE
SEQRES 13 A 203 LEU LYS VAL PHE LEU GLY PHE ILE GLY ILE THR ASP LEU
SEQRES 14 A 203 GLU ILE VAL ARG ALA HIS GLY LEU ALA TYR GLY PRO GLU
SEQRES 15 A 203 GLN ARG SER GLN ALA ILE ASP ALA ALA GLN ALA GLN ILE
SEQRES 16 A 203 ALA SER GLU LEU PHE ALA VAL ALA
HET FMN A1201 50
HET 12P A1202 16
HET 12P A1203 10
HETNAM FMN FLAVIN MONONUCLEOTIDE
HETNAM 12P DODECAETHYLENE GLYCOL
HETSYN FMN RIBOFLAVIN MONOPHOSPHATE
HETSYN 12P POLYETHYLENE GLYCOL PEG400
FORMUL 2 FMN C17 H21 N4 O9 P
FORMUL 3 12P 2(C24 H50 O13)
FORMUL 5 HOH *302(H2 O)
HELIX 1 1 LEU A 11 ASN A 14 5 4
HELIX 2 2 SER A 15 ASP A 32 1 18
HELIX 3 3 SER A 51 GLY A 59 1 9
HELIX 4 4 ASP A 66 ALA A 86 1 21
HELIX 5 5 PRO A 101 ALA A 112 1 12
HELIX 6 6 GLN A 147 ALA A 151 5 5
HELIX 7 7 HIS A 153 ILE A 164 1 12
HELIX 8 8 GLY A 180 LEU A 199 1 20
SHEET 1 AA 5 GLU A 36 ASP A 41 0
SHEET 2 AA 5 LYS A 2 ASP A 7 1 O LEU A 3 N VAL A 38
SHEET 3 AA 5 ALA A 88 PRO A 94 1 O ALA A 88 N LEU A 4
SHEET 4 AA 5 LYS A 133 THR A 139 1 O LYS A 133 N VAL A 89
SHEET 5 AA 5 ASP A 168 ALA A 174 1 O ASP A 168 N VAL A 134
SHEET 1 AB 2 PHE A 118 THR A 121 0
SHEET 2 AB 2 GLY A 124 GLY A 127 -1 O GLY A 124 N THR A 121
SITE 1 AC1 20 SER A 9 LEU A 11 SER A 15 ALA A 16
SITE 2 AC1 20 SER A 17 PRO A 94 MET A 95 TYR A 96
SITE 3 AC1 20 ASN A 97 PHE A 98 THR A 139 ALA A 140
SITE 4 AC1 20 GLY A 141 GLY A 142 LEU A 177 12P A1202
SITE 5 AC1 20 HOH A2045 HOH A2196 HOH A2296 HOH A2298
SITE 1 AC2 9 ASN A 97 GLY A 142 ALA A 178 TYR A 179
SITE 2 AC2 9 FMN A1201 HOH A2228 HOH A2299 HOH A2300
SITE 3 AC2 9 HOH A2301
SITE 1 AC3 2 LEU A 55 HOH A2027
CRYST1 72.299 95.743 146.539 90.00 90.00 90.00 F 2 2 2 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 0.013831 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010445 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006824 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
