HEADER OXIDOREDUCTASE, ISOMERASE 18-JUL-16 5KWF
TITLE JOINT X-RAY NEUTRON STRUCTURE OF CHOLESTEROL OXIDASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHOLESTEROL OXIDASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CHOD,CHOLESTEROL ISOMERASE;
COMPND 5 EC: 1.1.3.6,5.3.3.1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: STREPTOMYCES SP. (STRAIN SA-COO);
SOURCE 3 ORGANISM_TAXID: 74576;
SOURCE 4 STRAIN: SA-COO;
SOURCE 5 GENE: CHOA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE, ISOMERASE
EXPDTA X-RAY DIFFRACTION; NEUTRON DIFFRACTION
AUTHOR E.GOLDEN,A.VRIELINK,F.MEILLEUR,M.BLAKELEY
REVDAT 3 06-MAR-24 5KWF 1 REMARK
REVDAT 2 27-SEP-17 5KWF 1 REMARK
REVDAT 1 01-FEB-17 5KWF 0
JRNL AUTH E.GOLDEN,L.J.YU,F.MEILLEUR,M.P.BLAKELEY,A.P.DUFF,A.KARTON,
JRNL AUTH 2 A.VRIELINK
JRNL TITL AN EXTENDED N-H BOND, DRIVEN BY A CONSERVED SECOND-ORDER
JRNL TITL 2 INTERACTION, ORIENTS THE FLAVIN N5 ORBITAL IN CHOLESTEROL
JRNL TITL 3 OXIDASE.
JRNL REF SCI REP V. 7 40517 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 28098177
JRNL DOI 10.1038/SREP40517
REMARK 2
REMARK 2 RESOLUTION. 1.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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 X-RAY DATA.
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 67641
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3376
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 25.2679 - 4.3172 0.96 2901 150 0.2865 0.3096
REMARK 3 2 4.3172 - 3.4294 0.96 2854 151 0.1703 0.2088
REMARK 3 3 3.4294 - 2.9967 0.96 2849 149 0.1846 0.2057
REMARK 3 4 2.9967 - 2.7231 0.95 2798 149 0.1691 0.1881
REMARK 3 5 2.7231 - 2.5281 0.94 2792 148 0.1536 0.1895
REMARK 3 6 2.5281 - 2.3792 0.94 2768 140 0.1516 0.1837
REMARK 3 7 2.3792 - 2.2601 0.94 2755 144 0.1550 0.2009
REMARK 3 8 2.2601 - 2.1618 0.93 2747 144 0.1581 0.2170
REMARK 3 9 2.1618 - 2.0786 0.93 2704 142 0.1586 0.2086
REMARK 3 10 2.0786 - 2.0069 0.92 2702 143 0.1489 0.1981
REMARK 3 11 2.0069 - 1.9442 0.91 2704 142 0.1392 0.1769
REMARK 3 12 1.9442 - 1.8886 0.91 2687 141 0.1338 0.1668
REMARK 3 13 1.8886 - 1.8389 0.91 2636 139 0.1375 0.1706
REMARK 3 14 1.8389 - 1.7941 0.90 2655 140 0.1355 0.1903
REMARK 3 15 1.7941 - 1.7533 0.89 2620 139 0.1410 0.1767
REMARK 3 16 1.7533 - 1.7160 0.90 2603 136 0.1494 0.2100
REMARK 3 17 1.7160 - 1.6817 0.88 2584 137 0.1682 0.1763
REMARK 3 18 1.6817 - 1.6499 0.89 2637 138 0.1913 0.1987
REMARK 3 19 1.6499 - 1.6205 0.89 2602 137 0.2143 0.2242
REMARK 3 20 1.6205 - 1.5930 0.88 2578 136 0.2552 0.2419
REMARK 3 21 1.5930 - 1.5673 0.88 2569 135 0.3134 0.2728
REMARK 3 22 1.5673 - 1.5432 0.86 2537 133 0.3986 0.4205
REMARK 3 23 1.5432 - 1.5205 0.86 2506 132 0.5062 0.4268
REMARK 3 24 1.5205 - 1.4991 0.84 2477 131 0.5779 0.5266
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 12.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.22
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 : 0.016 8825
REMARK 3 ANGLE : 1.459 15612
REMARK 3 CHIRALITY : 0.134 585
REMARK 3 PLANARITY : 0.036 1788
REMARK 3 DIHEDRAL : 23.110 2427
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 3 NEUTRON DATA.
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.21
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.59
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 76.2
REMARK 3 NUMBER OF REFLECTIONS : 17713
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.285
REMARK 3 R VALUE (WORKING SET) : 0.284
REMARK 3 FREE R VALUE : 0.312
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 886
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 61.6169 - 4.0222 0.94 3511 185 0.2705 0.3207
REMARK 3 2 4.0222 - 3.1925 0.89 3285 172 0.2405 0.2780
REMARK 3 3 3.1925 - 2.7890 0.78 2883 153 0.2627 0.2609
REMARK 3 4 2.7890 - 2.5340 0.70 2566 135 0.3123 0.3288
REMARK 3 5 2.5340 - 2.3523 0.65 2374 125 0.3309 0.3696
REMARK 3 6 2.3523 - 2.2137 0.60 2208 116 0.3531 0.3558
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.560
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
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 5KWF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-16.
REMARK 100 THE DEPOSITION ID IS D_1000222060.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 293
REMARK 200 PH : NULL
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 : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : OSMIC VARIMAX
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67641
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.499
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.1000
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 230
REMARK 230 EXPERIMENTAL DETAILS
REMARK 230 EXPERIMENT TYPE : NEUTRON DIFFRACTION
REMARK 230 DATE OF DATA COLLECTION : 01-JUN-13
REMARK 230 TEMPERATURE (KELVIN) : 293.0
REMARK 230 PH : NULL
REMARK 230 NUMBER OF CRYSTALS USED : 1
REMARK 230
REMARK 230 NEUTRON SOURCE : NUCLEAR REACTOR
REMARK 230 BEAMLINE : CG4D
REMARK 230 WAVELENGTH OR RANGE (A) : 2.8-4.3
REMARK 230 MONOCHROMATOR : NULL
REMARK 230 OPTICS : NULL
REMARK 230
REMARK 230 DETECTOR TYPE : IMAGE PLATE
REMARK 230 DETECTOR MANUFACTURER : MAATEL IMAGINE
REMARK 230 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 230 DATA SCALING SOFTWARE : SCALA
REMARK 230
REMARK 230 NUMBER OF UNIQUE REFLECTIONS : 17714
REMARK 230 RESOLUTION RANGE HIGH (A) : 2.192
REMARK 230 RESOLUTION RANGE LOW (A) : 61.593
REMARK 230 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 230
REMARK 230 OVERALL.
REMARK 230 COMPLETENESS FOR RANGE (%) : 76.7
REMARK 230 DATA REDUNDANCY : 4.000
REMARK 230 R MERGE (I) : 0.25800
REMARK 230 R SYM (I) : 0.25800
REMARK 230 <I/SIGMA(I)> FOR THE DATA SET : 4.0000
REMARK 230
REMARK 230 IN THE HIGHEST RESOLUTION SHELL.
REMARK 230 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20
REMARK 230 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 230 COMPLETENESS FOR SHELL (%) : 61.1
REMARK 230 DATA REDUNDANCY IN SHELL : 3.30
REMARK 230 R MERGE FOR SHELL (I) : 0.34900
REMARK 230 R SYM FOR SHELL (I) : NULL
REMARK 230 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 230
REMARK 230 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 230 SOFTWARE USED : PHASER
REMARK 230 STARTING MODEL: NULL
REMARK 230
REMARK 230 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 42.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 8000, 100MM MNSO4, 100MM
REMARK 280 CACODYLIC ACID PH 5.2, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 37.04200
REMARK 290 SMTRY3 2 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 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 ASP A 6
REMARK 465 ASN A 7
REMARK 465 GLY A 8
REMARK 465 ALA A 508
REMARK 465 SER A 509
REMARK 465 HIS A 510
REMARK 465 HIS A 511
REMARK 465 HIS A 512
REMARK 465 HIS A 513
REMARK 465 HIS A 514
REMARK 465 HIS A 515
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 THR A 507 CA C O CB OG1 CG2
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 DH12 ARG A 500 OE1 GLN A 504 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR A 284 CE1 TYR A 284 CZ -0.081
REMARK 500 CYS A 445 CB CYS A 445 SG -0.105
REMARK 500 GLU A 499 CD GLU A 499 OE2 -0.075
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 ARG A 137 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 MET A 154 CG - SD - CE ANGL. DEV. = 10.9 DEGREES
REMARK 500 ASP A 196 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 TYR A 232 CB - CG - CD2 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 254 NE - CZ - NH2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG A 328 NE - CZ - NH1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 ARG A 463 NE - CZ - NH2 ANGL. DEV. = -3.4 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 THR A 18 28.12 -141.28
REMARK 500 ASN A 46 17.13 -141.73
REMARK 500 ASP A 62 -159.89 -143.71
REMARK 500 ARG A 146 -50.59 -125.88
REMARK 500 SER A 211 -73.53 -139.62
REMARK 500 VAL A 217 -48.98 -170.30
REMARK 500 THR A 231 -98.44 -112.83
REMARK 500 ASN A 353 -6.12 76.52
REMARK 500 CYS A 452 57.75 -145.22
REMARK 500 ASP A 474 -162.78 -118.71
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 601
DBREF 5KWF A 6 509 UNP P12676 CHOD_STRS0 43 546
SEQADV 5KWF HIS A 510 UNP P12676 EXPRESSION TAG
SEQADV 5KWF HIS A 511 UNP P12676 EXPRESSION TAG
SEQADV 5KWF HIS A 512 UNP P12676 EXPRESSION TAG
SEQADV 5KWF HIS A 513 UNP P12676 EXPRESSION TAG
SEQADV 5KWF HIS A 514 UNP P12676 EXPRESSION TAG
SEQADV 5KWF HIS A 515 UNP P12676 EXPRESSION TAG
SEQRES 1 A 510 ASP ASN GLY GLY TYR VAL PRO ALA VAL VAL ILE GLY THR
SEQRES 2 A 510 GLY TYR GLY ALA ALA VAL SER ALA LEU ARG LEU GLY GLU
SEQRES 3 A 510 ALA GLY VAL GLN THR LEU MET LEU GLU MET GLY GLN LEU
SEQRES 4 A 510 TRP ASN GLN PRO GLY PRO ASP GLY ASN ILE PHE CYS GLY
SEQRES 5 A 510 MET LEU ASN PRO ASP LYS ARG SER SER TRP PHE LYS ASN
SEQRES 6 A 510 ARG THR GLU ALA PRO LEU GLY SER PHE LEU TRP LEU ASP
SEQRES 7 A 510 VAL VAL ASN ARG ASN ILE ASP PRO TYR ALA GLY VAL LEU
SEQRES 8 A 510 ASP ARG VAL ASN TYR ASP GLN MET SER VAL TYR VAL GLY
SEQRES 9 A 510 ARG GLY VAL GLY GLY GLY SER LEU VAL ASN GLY GLY MET
SEQRES 10 A 510 ALA VAL GLU PRO LYS ARG SER TYR PHE GLU GLU ILE LEU
SEQRES 11 A 510 PRO ARG VAL ASP SER SER GLU MET TYR ASP ARG TYR PHE
SEQRES 12 A 510 PRO ARG ALA ASN SER MET LEU ARG VAL ASN HIS ILE ASP
SEQRES 13 A 510 THR LYS TRP PHE GLU ASP THR GLU TRP TYR LYS PHE ALA
SEQRES 14 A 510 ARG VAL SER ARG GLU GLN ALA GLY LYS ALA GLY LEU GLY
SEQRES 15 A 510 THR VAL PHE VAL PRO ASN VAL TYR ASP PHE GLY TYR MET
SEQRES 16 A 510 GLN ARG GLU ALA ALA GLY GLU VAL PRO LYS SER ALA LEU
SEQRES 17 A 510 ALA THR GLU VAL ILE TYR GLY ASN ASN HIS GLY LYS GLN
SEQRES 18 A 510 SER LEU ASP LYS THR TYR LEU ALA ALA ALA LEU GLY THR
SEQRES 19 A 510 GLY LYS VAL THR ILE GLN THR LEU HIS GLN VAL LYS THR
SEQRES 20 A 510 ILE ARG GLN THR LYS ASP GLY GLY TYR ALA LEU THR VAL
SEQRES 21 A 510 GLU GLN LYS ASP THR ASP GLY LYS LEU LEU ALA THR LYS
SEQRES 22 A 510 GLU ILE SER CYS ARG TYR LEU PHE LEU GLY ALA GLY SER
SEQRES 23 A 510 LEU GLY SER THR GLU LEU LEU VAL ARG ALA ARG ASP THR
SEQRES 24 A 510 GLY THR LEU PRO ASN LEU ASN SER GLU VAL GLY ALA GLY
SEQRES 25 A 510 TRP GLY PRO ASN GLY ASN ILE MET THR ALA ARG ALA ASN
SEQRES 26 A 510 HIS MET TRP ASN PRO THR GLY ALA HIS GLN SER SER ILE
SEQRES 27 A 510 PRO ALA LEU GLY ILE ASP ALA TRP ASP ASN SER ASP SER
SEQRES 28 A 510 SER VAL PHE ALA GLU ILE ALA PRO MET PRO ALA GLY LEU
SEQRES 29 A 510 GLU THR TRP VAL SER LEU TYR LEU ALA ILE THR LYS ASN
SEQRES 30 A 510 PRO GLN ARG GLY THR PHE VAL TYR ASP ALA ALA THR ASP
SEQRES 31 A 510 ARG ALA LYS LEU ASN TRP THR ARG ASP GLN ASN ALA PRO
SEQRES 32 A 510 ALA VAL ASN ALA ALA LYS ALA LEU PHE ASP ARG ILE ASN
SEQRES 33 A 510 LYS ALA ASN GLY THR ILE TYR ARG TYR ASP LEU PHE GLY
SEQRES 34 A 510 THR GLN LEU LYS ALA PHE ALA ASP ASP PHE CYS TYR HIS
SEQRES 35 A 510 PRO LEU GLY GLY CYS VAL LEU GLY LYS ALA THR ASP ASP
SEQRES 36 A 510 TYR GLY ARG VAL ALA GLY TYR LYS ASN LEU TYR VAL THR
SEQRES 37 A 510 ASP GLY SER LEU ILE PRO GLY SER VAL GLY VAL ASN PRO
SEQRES 38 A 510 PHE VAL THR ILE THR ALA LEU ALA GLU ARG ASN VAL GLU
SEQRES 39 A 510 ARG ILE ILE LYS GLN ASP VAL THR ALA SER HIS HIS HIS
SEQRES 40 A 510 HIS HIS HIS
HET FAD A 601 92
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 DOD *258(D2 O)
HELIX 1 AA1 GLY A 19 ALA A 32 1 14
HELIX 2 AA2 ASP A 62 SER A 66 5 5
HELIX 3 AA3 SER A 78 ASP A 83 1 6
HELIX 4 AA4 VAL A 84 ASN A 86 5 3
HELIX 5 AA5 GLY A 113 VAL A 118 5 6
HELIX 6 AA6 LYS A 127 LEU A 135 1 9
HELIX 7 AA7 ASP A 139 ARG A 146 1 8
HELIX 8 AA8 ARG A 146 ARG A 156 1 11
HELIX 9 AA9 ASP A 161 THR A 168 1 8
HELIX 10 AB1 TYR A 171 ALA A 184 1 14
HELIX 11 AB2 ASP A 196 ALA A 205 1 10
HELIX 12 AB3 SER A 211 THR A 215 5 5
HELIX 13 AB4 THR A 231 THR A 239 1 9
HELIX 14 AB5 ALA A 289 THR A 304 1 16
HELIX 15 AB6 THR A 402 GLN A 405 5 4
HELIX 16 AB7 ASN A 406 GLY A 425 1 20
HELIX 17 AB8 ASP A 474 ILE A 478 5 5
HELIX 18 AB9 PRO A 486 VAL A 506 1 21
SHEET 1 AA1 6 VAL A 242 GLN A 245 0
SHEET 2 AA1 6 THR A 36 LEU A 39 1 N MET A 38 O GLN A 245
SHEET 3 AA1 6 TYR A 10 ILE A 16 1 N VAL A 15 O LEU A 37
SHEET 4 AA1 6 LEU A 274 LEU A 287 1 O PHE A 286 N VAL A 14
SHEET 5 AA1 6 TYR A 261 LYS A 268 -1 N GLN A 267 O LEU A 275
SHEET 6 AA1 6 HIS A 248 GLN A 255 -1 N LYS A 251 O THR A 264
SHEET 1 AA2 5 VAL A 242 GLN A 245 0
SHEET 2 AA2 5 THR A 36 LEU A 39 1 N MET A 38 O GLN A 245
SHEET 3 AA2 5 TYR A 10 ILE A 16 1 N VAL A 15 O LEU A 37
SHEET 4 AA2 5 LEU A 274 LEU A 287 1 O PHE A 286 N VAL A 14
SHEET 5 AA2 5 LEU A 470 VAL A 472 1 O TYR A 471 N LEU A 287
SHEET 1 AA3 3 LEU A 96 ASN A 100 0
SHEET 2 AA3 3 SER A 105 GLY A 109 -1 O VAL A 108 N ASP A 97
SHEET 3 AA3 3 PHE A 444 CYS A 445 1 O CYS A 445 N TYR A 107
SHEET 1 AA4 6 THR A 188 PHE A 190 0
SHEET 2 AA4 6 LEU A 346 ALA A 350 -1 O GLY A 347 N VAL A 189
SHEET 3 AA4 6 VAL A 358 ALA A 363 -1 O ALA A 360 N ILE A 348
SHEET 4 AA4 6 VAL A 373 THR A 380 -1 O LEU A 377 N GLU A 361
SHEET 5 AA4 6 ASN A 323 ALA A 329 -1 N ILE A 324 O ALA A 378
SHEET 6 AA4 6 ILE A 427 TYR A 428 -1 O ILE A 427 N ALA A 329
SHEET 1 AA5 6 THR A 188 PHE A 190 0
SHEET 2 AA5 6 LEU A 346 ALA A 350 -1 O GLY A 347 N VAL A 189
SHEET 3 AA5 6 VAL A 358 ALA A 363 -1 O ALA A 360 N ILE A 348
SHEET 4 AA5 6 VAL A 373 THR A 380 -1 O LEU A 377 N GLU A 361
SHEET 5 AA5 6 ASN A 323 ALA A 329 -1 N ILE A 324 O ALA A 378
SHEET 6 AA5 6 PHE A 440 ALA A 441 -1 O ALA A 441 N MET A 325
SHEET 1 AA6 2 THR A 387 ASP A 391 0
SHEET 2 AA6 2 ARG A 396 ASN A 400 -1 O LYS A 398 N VAL A 389
SITE 1 AC1 41 GLY A 17 GLY A 19 TYR A 20 GLY A 21
SITE 2 AC1 41 LEU A 39 GLU A 40 MET A 41 TYR A 107
SITE 3 AC1 41 GLY A 109 ARG A 110 GLY A 111 GLY A 114
SITE 4 AC1 41 GLY A 115 ASN A 119 GLY A 120 GLY A 121
SITE 5 AC1 41 MET A 122 ILE A 218 HIS A 248 VAL A 250
SITE 6 AC1 41 GLY A 288 ALA A 289 GLY A 290 TYR A 446
SITE 7 AC1 41 HIS A 447 ASP A 474 GLY A 475 ASN A 485
SITE 8 AC1 41 PRO A 486 PHE A 487 ILE A 490 HOH A 746
SITE 9 AC1 41 DOD A 765 DOD A 766 HOH A 775 HOH A 801
SITE 10 AC1 41 DOD A 833 DOD A 836 DOD A 873 DOD A 887
SITE 11 AC1 41 DOD A 922
CRYST1 51.605 74.084 63.828 90.00 105.21 90.00 P 1 21 1 2
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 0.019378 0.000000 0.005267 0.00000
SCALE2 0.000000 0.013498 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016236 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
