HEADER OXIDOREDUCTASE 19-SEP-12 4H6Q
TITLE STRUCTURE OF OXIDIZED DEINOCOCCUS RADIODURANS PROLINE DEHYDROGENASE
TITLE 2 COMPLEXED WITH L-TETRAHYDROFUROIC ACID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROLINE DEHYDROGENASE;
COMPND 3 CHAIN: A, C;
COMPND 4 EC: 1.5.99.8;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 243230;
SOURCE 4 STRAIN: R1;
SOURCE 5 GENE: DR_0814, PROLINE DEHYDROGENASE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PKA8H
KEYWDS BETA8-ALPHA8-BARREL, FLAVOENZYME, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR L.MIN,J.J.TANNER
REVDAT 3 20-SEP-23 4H6Q 1 REMARK SEQADV
REVDAT 2 02-JAN-13 4H6Q 1 JRNL
REVDAT 1 28-NOV-12 4H6Q 0
JRNL AUTH M.LUO,B.W.ARENTSON,D.SRIVASTAVA,D.F.BECKER,J.J.TANNER
JRNL TITL CRYSTAL STRUCTURES AND KINETICS OF MONOFUNCTIONAL PROLINE
JRNL TITL 2 DEHYDROGENASE PROVIDE INSIGHT INTO SUBSTRATE RECOGNITION AND
JRNL TITL 3 CONFORMATIONAL CHANGES ASSOCIATED WITH FLAVIN REDUCTION AND
JRNL TITL 4 PRODUCT RELEASE.
JRNL REF BIOCHEMISTRY V. 51 10099 2012
JRNL REFN ISSN 0006-2960
JRNL PMID 23151026
JRNL DOI 10.1021/BI301312F
REMARK 2
REMARK 2 RESOLUTION. 1.36 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8_1069
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) : 1.36
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 78.21
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.150
REMARK 3 COMPLETENESS FOR RANGE (%) : 95.6
REMARK 3 NUMBER OF REFLECTIONS : 124194
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.150
REMARK 3 R VALUE (WORKING SET) : 0.148
REMARK 3 FREE R VALUE : 0.181
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 11592
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 78.2090 - 4.2219 0.88 6805 314 0.1657 0.1603
REMARK 3 2 4.2219 - 3.3510 0.93 7050 416 0.1451 0.1642
REMARK 3 3 3.3510 - 2.9274 0.94 7197 368 0.1611 0.1940
REMARK 3 4 2.9274 - 2.6597 0.88 6697 411 0.1554 0.1830
REMARK 3 5 2.6597 - 2.4691 0.94 7149 406 0.1488 0.1740
REMARK 3 6 2.4691 - 2.3235 0.96 7331 367 0.1375 0.1859
REMARK 3 7 2.3235 - 2.2071 0.96 7357 382 0.1281 0.1732
REMARK 3 8 2.2071 - 2.1110 0.97 7417 352 0.1264 0.1648
REMARK 3 9 2.1110 - 2.0298 0.98 7489 397 0.1272 0.1671
REMARK 3 10 2.0298 - 1.9597 0.93 7122 389 0.1231 0.1780
REMARK 3 11 1.9597 - 1.8984 0.94 7203 370 0.1217 0.1735
REMARK 3 12 1.8984 - 1.8442 0.96 7353 385 0.1177 0.1758
REMARK 3 13 1.8442 - 1.7956 0.97 7366 462 0.1197 0.1707
REMARK 3 14 1.7956 - 1.7518 0.98 7433 429 0.1303 0.1752
REMARK 3 15 1.7518 - 1.7120 0.98 7480 398 0.1301 0.1714
REMARK 3 16 1.7120 - 1.6755 0.98 7568 369 0.1327 0.1783
REMARK 3 17 1.6755 - 1.6420 0.98 7530 350 0.1292 0.1729
REMARK 3 18 1.6420 - 1.6110 0.98 7653 366 0.1298 0.1643
REMARK 3 19 1.6110 - 1.5823 0.96 7317 421 0.1354 0.1889
REMARK 3 20 1.5823 - 1.5554 0.91 7006 367 0.1541 0.1875
REMARK 3 21 1.5554 - 1.5303 0.95 7234 385 0.1598 0.2000
REMARK 3 22 1.5303 - 1.5068 0.97 7512 322 0.1677 0.2208
REMARK 3 23 1.5068 - 1.4846 0.97 7343 369 0.1836 0.2398
REMARK 3 24 1.4846 - 1.4637 0.97 7500 405 0.1934 0.2280
REMARK 3 25 1.4637 - 1.4439 0.97 7456 393 0.1924 0.2412
REMARK 3 26 1.4439 - 1.4252 0.98 7508 381 0.2072 0.2447
REMARK 3 27 1.4252 - 1.4074 0.98 7485 412 0.2199 0.2657
REMARK 3 28 1.4074 - 1.3904 0.98 7405 407 0.2294 0.2534
REMARK 3 29 1.3904 - 1.3742 0.98 7619 409 0.2499 0.3083
REMARK 3 30 1.3742 - 1.3590 0.91 6897 390 0.2590 0.2882
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.140
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.240
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 22.21
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 : 0.015 4726
REMARK 3 ANGLE : 1.754 6451
REMARK 3 CHIRALITY : 0.102 712
REMARK 3 PLANARITY : 0.008 822
REMARK 3 DIHEDRAL : 18.953 1856
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 4H6Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000075088.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 200
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97920
REMARK 200 MONOCHROMATOR : BEAMLINE OPTICS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 124194
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.359
REMARK 200 RESOLUTION RANGE LOW (A) : 78.209
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.03200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.36
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.43100
REMARK 200 R SYM FOR SHELL (I) : 0.43100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2G37
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.23
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 25% (W/V)
REMARK 280 PEG3350, 0.1 MM BIS-TRIS, 400 MM TETRAHYDROFURAN-2-CARBOXYLIC
REMARK 280 ACID, PH 5.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 22.23450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.19650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 47.73100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.19650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.23450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 47.73100
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
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: 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 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 GLY A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ILE A 2
REMARK 465 ASP A 3
REMARK 465 GLN A 4
REMARK 465 LEU A 5
REMARK 465 TYR A 6
REMARK 465 ARG A 7
REMARK 465 LYS A 8
REMARK 465 ALA A 9
REMARK 465 VAL A 10
REMARK 465 LEU A 11
REMARK 465 THR A 12
REMARK 465 VAL A 13
REMARK 465 ALA A 14
REMARK 465 GLU A 15
REMARK 465 ARG A 16
REMARK 465 ARG A 298
REMARK 465 ASN A 299
REMARK 465 ALA A 300
REMARK 465 ALA A 301
REMARK 465 PHE A 302
REMARK 465 VAL A 303
REMARK 465 VAL A 304
REMARK 465 GLN A 305
REMARK 465 GLY A 306
REMARK 465 MET A 307
REMARK 465 LEU A 308
REMARK 465 LYS A 309
REMARK 465 GLY A 310
REMARK 465 GLY C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 ILE C 2
REMARK 465 ASP C 3
REMARK 465 GLN C 4
REMARK 465 LEU C 5
REMARK 465 TYR C 6
REMARK 465 ARG C 7
REMARK 465 LYS C 8
REMARK 465 ALA C 9
REMARK 465 VAL C 10
REMARK 465 LEU C 11
REMARK 465 THR C 12
REMARK 465 VAL C 13
REMARK 465 ALA C 14
REMARK 465 GLU C 15
REMARK 465 ARG C 16
REMARK 465 ARG C 298
REMARK 465 ASN C 299
REMARK 465 ALA C 300
REMARK 465 ALA C 301
REMARK 465 PHE C 302
REMARK 465 VAL C 303
REMARK 465 VAL C 304
REMARK 465 GLN C 305
REMARK 465 GLY C 306
REMARK 465 MET C 307
REMARK 465 LEU C 308
REMARK 465 LYS C 309
REMARK 465 GLY C 310
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 PRO A 17 CG CD
REMARK 470 GLN A 18 CG CD OE1 NE2
REMARK 470 VAL A 19 CG1 CG2
REMARK 470 GLU A 20 CG CD OE1 OE2
REMARK 470 GLN A 21 CG CD OE1 NE2
REMARK 470 ARG A 24 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 41 CG CD OE1 OE2
REMARK 470 GLU A 147 CG CD OE1 OE2
REMARK 470 LYS A 204 CG CD CE NZ
REMARK 470 ARG A 233 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 262 NE CZ NH1 NH2
REMARK 470 ARG A 283 CD NE CZ NH1 NH2
REMARK 470 PRO C 17 CG CD
REMARK 470 GLN C 18 CG CD OE1 NE2
REMARK 470 VAL C 19 CG1 CG2
REMARK 470 GLU C 20 CG CD OE1 OE2
REMARK 470 GLN C 21 CG CD OE1 NE2
REMARK 470 ARG C 24 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 41 CG CD OE1 OE2
REMARK 470 ARG C 52 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 67 CG OD1 OD2
REMARK 470 LYS C 71 NZ
REMARK 470 LYS C 81 CD CE NZ
REMARK 470 LYS C 92 CE NZ
REMARK 470 LYS C 106 CE NZ
REMARK 470 GLU C 108 CG CD OE1 OE2
REMARK 470 ASN C 109 CG OD1 ND2
REMARK 470 GLU C 111 OE1 OE2
REMARK 470 GLU C 147 CG CD OE1 OE2
REMARK 470 GLU C 159 CG CD OE1 OE2
REMARK 470 ARG C 183 NE CZ NH1 NH2
REMARK 470 LYS C 204 CG CD CE NZ
REMARK 470 ARG C 213 NE CZ NH1 NH2
REMARK 470 ARG C 233 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 262 CZ NH1 NH2
REMARK 470 ARG C 283 NE CZ NH1 NH2
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 ASP C 250 CB - CG - OD1 ANGL. DEV. = 5.5 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 GLU A 137 -150.12 -94.20
REMARK 500 GLU C 137 -148.45 -92.65
REMARK 500 ARG C 183 60.69 34.57
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 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TFB A 2002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 2001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TFB C 2002
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4H6R RELATED DB: PDB
DBREF 4H6Q A 1 310 UNP Q9RW55 Q9RW55_DEIRA 1 310
DBREF 4H6Q C 1 310 UNP Q9RW55 Q9RW55_DEIRA 1 310
SEQADV 4H6Q GLY A -1 UNP Q9RW55 EXPRESSION TAG
SEQADV 4H6Q HIS A 0 UNP Q9RW55 EXPRESSION TAG
SEQADV 4H6Q GLY C -1 UNP Q9RW55 EXPRESSION TAG
SEQADV 4H6Q HIS C 0 UNP Q9RW55 EXPRESSION TAG
SEQRES 1 A 312 GLY HIS MET ILE ASP GLN LEU TYR ARG LYS ALA VAL LEU
SEQRES 2 A 312 THR VAL ALA GLU ARG PRO GLN VAL GLU GLN LEU ALA ARG
SEQRES 3 A 312 GLN LYS MET TRP ASN LEU ALA GLU ARG PHE VAL ALA GLY
SEQRES 4 A 312 GLU SER ILE GLU SER ALA ILE GLN ALA VAL GLN ALA LEU
SEQRES 5 A 312 GLU ARG ASP GLY ILE ALA GLY ASN LEU ASP LEU LEU GLY
SEQRES 6 A 312 GLU PHE ILE ASP SER PRO ALA LYS CYS THR GLU PHE ALA
SEQRES 7 A 312 ASP ASP VAL ILE LYS LEU ILE GLU ALA ALA HIS ALA ALA
SEQRES 8 A 312 GLY ILE LYS PRO TYR VAL SER ILE LYS LEU SER SER VAL
SEQRES 9 A 312 GLY GLN GLY LYS ASP GLU ASN GLY GLU ASP LEU GLY LEU
SEQRES 10 A 312 THR ASN ALA ARG ARG ILE ILE ALA LYS ALA LYS GLU TYR
SEQRES 11 A 312 GLY GLY PHE ILE CYS LEU ASP MET GLU ASP HIS THR ARG
SEQRES 12 A 312 VAL ASP VAL THR LEU GLU GLN PHE ARG THR LEU VAL GLY
SEQRES 13 A 312 GLU PHE GLY ALA GLU HIS VAL GLY THR VAL LEU GLN SER
SEQRES 14 A 312 TYR LEU TYR ARG SER LEU GLY ASP ARG ALA SER LEU ASP
SEQRES 15 A 312 ASP LEU ARG PRO ASN ILE ARG MET VAL LYS GLY ALA TYR
SEQRES 16 A 312 LEU GLU PRO ALA THR VAL ALA TYR PRO ASP LYS ALA ASP
SEQRES 17 A 312 VAL ASP GLN ASN TYR ARG ARG LEU VAL PHE GLN HIS LEU
SEQRES 18 A 312 LYS ALA GLY ASN TYR THR ASN VAL ALA THR HIS ASP GLU
SEQRES 19 A 312 ARG ILE ILE ASP ASP VAL LYS ARG PHE VAL LEU ALA HIS
SEQRES 20 A 312 GLY ILE GLY LYS ASP ALA PHE GLU PHE GLN MET LEU TYR
SEQRES 21 A 312 GLY ILE ARG ARG ASP LEU GLN LYS GLN LEU ALA ALA GLU
SEQRES 22 A 312 GLY TYR ARG VAL ARG VAL TYR LEU PRO TYR GLY ARG ASP
SEQRES 23 A 312 TRP TYR ALA TYR PHE SER ARG ARG ILE ALA GLU THR PRO
SEQRES 24 A 312 ARG ASN ALA ALA PHE VAL VAL GLN GLY MET LEU LYS GLY
SEQRES 1 C 312 GLY HIS MET ILE ASP GLN LEU TYR ARG LYS ALA VAL LEU
SEQRES 2 C 312 THR VAL ALA GLU ARG PRO GLN VAL GLU GLN LEU ALA ARG
SEQRES 3 C 312 GLN LYS MET TRP ASN LEU ALA GLU ARG PHE VAL ALA GLY
SEQRES 4 C 312 GLU SER ILE GLU SER ALA ILE GLN ALA VAL GLN ALA LEU
SEQRES 5 C 312 GLU ARG ASP GLY ILE ALA GLY ASN LEU ASP LEU LEU GLY
SEQRES 6 C 312 GLU PHE ILE ASP SER PRO ALA LYS CYS THR GLU PHE ALA
SEQRES 7 C 312 ASP ASP VAL ILE LYS LEU ILE GLU ALA ALA HIS ALA ALA
SEQRES 8 C 312 GLY ILE LYS PRO TYR VAL SER ILE LYS LEU SER SER VAL
SEQRES 9 C 312 GLY GLN GLY LYS ASP GLU ASN GLY GLU ASP LEU GLY LEU
SEQRES 10 C 312 THR ASN ALA ARG ARG ILE ILE ALA LYS ALA LYS GLU TYR
SEQRES 11 C 312 GLY GLY PHE ILE CYS LEU ASP MET GLU ASP HIS THR ARG
SEQRES 12 C 312 VAL ASP VAL THR LEU GLU GLN PHE ARG THR LEU VAL GLY
SEQRES 13 C 312 GLU PHE GLY ALA GLU HIS VAL GLY THR VAL LEU GLN SER
SEQRES 14 C 312 TYR LEU TYR ARG SER LEU GLY ASP ARG ALA SER LEU ASP
SEQRES 15 C 312 ASP LEU ARG PRO ASN ILE ARG MET VAL LYS GLY ALA TYR
SEQRES 16 C 312 LEU GLU PRO ALA THR VAL ALA TYR PRO ASP LYS ALA ASP
SEQRES 17 C 312 VAL ASP GLN ASN TYR ARG ARG LEU VAL PHE GLN HIS LEU
SEQRES 18 C 312 LYS ALA GLY ASN TYR THR ASN VAL ALA THR HIS ASP GLU
SEQRES 19 C 312 ARG ILE ILE ASP ASP VAL LYS ARG PHE VAL LEU ALA HIS
SEQRES 20 C 312 GLY ILE GLY LYS ASP ALA PHE GLU PHE GLN MET LEU TYR
SEQRES 21 C 312 GLY ILE ARG ARG ASP LEU GLN LYS GLN LEU ALA ALA GLU
SEQRES 22 C 312 GLY TYR ARG VAL ARG VAL TYR LEU PRO TYR GLY ARG ASP
SEQRES 23 C 312 TRP TYR ALA TYR PHE SER ARG ARG ILE ALA GLU THR PRO
SEQRES 24 C 312 ARG ASN ALA ALA PHE VAL VAL GLN GLY MET LEU LYS GLY
HET FAD A2001 106
HET TFB A2002 8
HET GOL A2003 6
HET FAD C2001 106
HET TFB C2002 8
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM TFB TETRAHYDROFURAN-2-CARBOXYLIC ACID
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 TFB 2(C5 H8 O3)
FORMUL 5 GOL C3 H8 O3
FORMUL 8 HOH *475(H2 O)
HELIX 1 1 PRO A 17 VAL A 19 5 3
HELIX 2 2 GLU A 20 GLU A 32 1 13
HELIX 3 3 SER A 39 ASP A 53 1 15
HELIX 4 4 SER A 68 ALA A 89 1 22
HELIX 5 5 LYS A 98 VAL A 102 5 5
HELIX 6 6 LEU A 113 TYR A 128 1 16
HELIX 7 7 ASP A 138 THR A 140 5 3
HELIX 8 8 ARG A 141 GLY A 157 1 17
HELIX 9 9 ARG A 171 LEU A 179 1 9
HELIX 10 10 ASP A 180 ARG A 183 5 4
HELIX 11 11 ASP A 203 ALA A 221 1 19
HELIX 12 12 ASP A 231 HIS A 245 1 15
HELIX 13 13 ARG A 261 GLU A 271 1 11
HELIX 14 14 TRP A 285 GLU A 295 1 11
HELIX 15 15 GLN C 18 GLU C 32 1 15
HELIX 16 16 SER C 39 ASP C 53 1 15
HELIX 17 17 SER C 68 ALA C 89 1 22
HELIX 18 18 LYS C 98 VAL C 102 5 5
HELIX 19 19 LEU C 113 TYR C 128 1 16
HELIX 20 20 ASP C 138 THR C 140 5 3
HELIX 21 21 ARG C 141 GLY C 157 1 17
HELIX 22 22 ARG C 171 SER C 178 1 8
HELIX 23 23 LEU C 179 ARG C 183 5 5
HELIX 24 24 ASP C 203 ALA C 221 1 19
HELIX 25 25 ASP C 231 HIS C 245 1 15
HELIX 26 26 ARG C 261 GLU C 271 1 11
HELIX 27 27 TRP C 285 GLU C 295 1 11
SHEET 1 A 9 ALA A 56 LEU A 61 0
SHEET 2 A 9 TYR A 94 ILE A 97 1 O SER A 96 N LEU A 59
SHEET 3 A 9 PHE A 131 LEU A 134 1 O CYS A 133 N ILE A 97
SHEET 4 A 9 VAL A 161 GLN A 166 1 O GLY A 162 N LEU A 134
SHEET 5 A 9 ILE A 186 VAL A 189 1 O ARG A 187 N THR A 163
SHEET 6 A 9 THR A 225 ALA A 228 1 O ASN A 226 N MET A 188
SHEET 7 A 9 PHE A 252 LEU A 257 1 O GLU A 253 N VAL A 227
SHEET 8 A 9 VAL A 275 TYR A 281 1 O TYR A 278 N MET A 256
SHEET 9 A 9 ALA A 56 LEU A 61 1 N ASN A 58 O LEU A 279
SHEET 1 B 2 ASP A 107 GLU A 108 0
SHEET 2 B 2 GLU A 111 ASP A 112 -1 O GLU A 111 N GLU A 108
SHEET 1 C 9 ALA C 56 LEU C 61 0
SHEET 2 C 9 TYR C 94 ILE C 97 1 O TYR C 94 N LEU C 59
SHEET 3 C 9 PHE C 131 LEU C 134 1 O CYS C 133 N ILE C 97
SHEET 4 C 9 VAL C 161 GLN C 166 1 O GLY C 162 N LEU C 134
SHEET 5 C 9 ILE C 186 VAL C 189 1 O ARG C 187 N THR C 163
SHEET 6 C 9 THR C 225 ALA C 228 1 O ASN C 226 N MET C 188
SHEET 7 C 9 PHE C 252 LEU C 257 1 O GLU C 253 N VAL C 227
SHEET 8 C 9 ARG C 274 TYR C 281 1 O TYR C 278 N MET C 256
SHEET 9 C 9 ALA C 56 LEU C 61 1 N ASN C 58 O LEU C 279
SHEET 1 D 2 ASP C 107 GLU C 108 0
SHEET 2 D 2 GLU C 111 ASP C 112 -1 O GLU C 111 N GLU C 108
SITE 1 AC1 32 ASP A 135 MET A 136 VAL A 164 GLN A 166
SITE 2 AC1 32 ARG A 187 VAL A 189 LYS A 190 GLY A 191
SITE 3 AC1 32 ALA A 192 TYR A 193 ALA A 228 THR A 229
SITE 4 AC1 32 HIS A 230 ASP A 231 GLN A 255 MET A 256
SITE 5 AC1 32 LEU A 257 ILE A 260 TYR A 278 ARG A 292
SITE 6 AC1 32 GLU A 295 PRO A 297 TFB A2002 HOH A2104
SITE 7 AC1 32 HOH A2115 HOH A2128 HOH A2136 HOH A2183
SITE 8 AC1 32 HOH A2210 HOH A2350 HOH A2377 HOH A2380
SITE 1 AC2 8 LYS A 98 ASP A 135 TYR A 278 TYR A 288
SITE 2 AC2 8 ARG A 291 ARG A 292 FAD A2001 HOH A2147
SITE 1 AC3 7 TYR A 94 TYR A 224 GLU A 253 ARG A 276
SITE 2 AC3 7 HOH A2295 HOH A2310 HOH A2362
SITE 1 AC4 30 ASP C 135 MET C 136 VAL C 164 GLN C 166
SITE 2 AC4 30 ARG C 187 VAL C 189 LYS C 190 GLY C 191
SITE 3 AC4 30 ALA C 192 TYR C 193 ALA C 228 THR C 229
SITE 4 AC4 30 HIS C 230 ASP C 231 GLN C 255 MET C 256
SITE 5 AC4 30 LEU C 257 ILE C 260 ARG C 292 GLU C 295
SITE 6 AC4 30 PRO C 297 TFB C2002 HOH C2106 HOH C2110
SITE 7 AC4 30 HOH C2116 HOH C2139 HOH C2190 HOH C2192
SITE 8 AC4 30 HOH C2228 HOH C2263
SITE 1 AC5 8 LYS C 98 ASP C 135 TYR C 278 TYR C 288
SITE 2 AC5 8 ARG C 291 ARG C 292 FAD C2001 HOH C2160
CRYST1 44.469 95.462 136.393 90.00 90.00 90.00 P 21 21 21 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 0.022488 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010475 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007332 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
