HEADER OXIDOREDUCTASE 30-MAY-12 4FEH
TITLE MYCOBACTERIUM TUBERCULOSIS DPRE1 - HEXAGONAL CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: OXIDOREDUCTASE DPRE1;
COMPND 3 CHAIN: A;
COMPND 4 EC: 1.-.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 STRAIN: H37RV;
SOURCE 5 GENE: DPRE1, MT3898, RV3790;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A
KEYWDS ALPHA+BETA, OXIDOREDUCTASE, DECAPRENYLPHOSPHORYL-BETA-D-RIBOSE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.M.BATT,G.S.BESRA,K.FUTTERER
REVDAT 4 03-APR-24 4FEH 1 REMARK
REVDAT 3 28-FEB-24 4FEH 1 REMARK SEQADV
REVDAT 2 31-OCT-12 4FEH 1 JRNL
REVDAT 1 04-JUL-12 4FEH 0
JRNL AUTH S.M.BATT,T.JABEEN,V.BHOWRUTH,L.QUILL,P.A.LUND,L.EGGELING,
JRNL AUTH 2 L.J.ALDERWICK,K.FUTTERER,G.S.BESRA
JRNL TITL STRUCTURAL BASIS OF INHIBITION OF MYCOBACTERIUM TUBERCULOSIS
JRNL TITL 2 DPRE1 BY BENZOTHIAZINONE INHIBITORS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 11354 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22733761
JRNL DOI 10.1073/PNAS.1205735109
REMARK 2
REMARK 2 RESOLUTION. 2.04 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
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) : 2.04
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.34
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 38539
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) : 0.191
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1929
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 45.3504 - 4.9017 1.00 2720 124 0.1778 0.1878
REMARK 3 2 4.9017 - 3.8913 1.00 2634 153 0.1537 0.1698
REMARK 3 3 3.8913 - 3.3996 1.00 2619 141 0.1854 0.1935
REMARK 3 4 3.3996 - 3.0888 1.00 2632 133 0.1871 0.2278
REMARK 3 5 3.0888 - 2.8675 1.00 2597 159 0.1926 0.2463
REMARK 3 6 2.8675 - 2.6984 1.00 2615 138 0.1954 0.2442
REMARK 3 7 2.6984 - 2.5633 1.00 2597 127 0.1960 0.2158
REMARK 3 8 2.5633 - 2.4517 1.00 2633 141 0.2070 0.2471
REMARK 3 9 2.4517 - 2.3574 1.00 2591 138 0.1959 0.2605
REMARK 3 10 2.3574 - 2.2760 1.00 2612 130 0.2091 0.2516
REMARK 3 11 2.2760 - 2.2049 0.98 2542 141 0.2827 0.3333
REMARK 3 12 2.2049 - 2.1418 1.00 2611 140 0.2222 0.2808
REMARK 3 13 2.1418 - 2.0854 1.00 2622 116 0.2354 0.2934
REMARK 3 14 2.0854 - 2.0346 0.99 2585 148 0.2941 0.2930
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.40
REMARK 3 SHRINKAGE RADIUS : 1.24
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 37.66
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.300
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.890
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) : -1.31660
REMARK 3 B22 (A**2) : -1.31660
REMARK 3 B33 (A**2) : 2.63320
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 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 : 0.008 3265
REMARK 3 ANGLE : 1.125 4450
REMARK 3 CHIRALITY : 0.077 503
REMARK 3 PLANARITY : 0.005 571
REMARK 3 DIHEDRAL : 13.472 1151
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 4FEH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000072799.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I04-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9173
REMARK 200 MONOCHROMATOR : TOROIDAL MIRRORS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38562
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.030
REMARK 200 RESOLUTION RANGE LOW (A) : 64.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.05100
REMARK 200 R SYM (I) : 0.05100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 21.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.03
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.09
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : 0.76400
REMARK 200 R SYM FOR SHELL (I) : 0.76400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
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: DPRE1 - MONOCLINIC CRYSTAL FORM
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE, 35% ETHYLENE
REMARK 280 GLYCOL, PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 288K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+1/3
REMARK 290 6555 X-Y,X,Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 21.43333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 42.86667
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 21.43333
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 42.86667
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 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 MET A -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 LEU A 2
REMARK 465 SER A 3
REMARK 465 VAL A 4
REMARK 465 GLY A 5
REMARK 465 ALA A 6
REMARK 465 ALA A 269
REMARK 465 PRO A 270
REMARK 465 GLN A 271
REMARK 465 LEU A 272
REMARK 465 LEU A 273
REMARK 465 THR A 274
REMARK 465 LEU A 275
REMARK 465 PRO A 276
REMARK 465 ASP A 277
REMARK 465 VAL A 278
REMARK 465 PHE A 279
REMARK 465 PRO A 280
REMARK 465 ASN A 281
REMARK 465 GLY A 282
REMARK 465 LEU A 283
REMARK 465 ALA A 284
REMARK 465 ASN A 285
REMARK 465 LYS A 286
REMARK 465 TYR A 287
REMARK 465 THR A 288
REMARK 465 PHE A 289
REMARK 465 GLY A 290
REMARK 465 PRO A 291
REMARK 465 ILE A 292
REMARK 465 GLY A 293
REMARK 465 GLU A 294
REMARK 465 LEU A 295
REMARK 465 TRP A 296
REMARK 465 TYR A 297
REMARK 465 PRO A 316
REMARK 465 LEU A 317
REMARK 465 ASP A 318
REMARK 465 MET A 319
REMARK 465 PHE A 320
REMARK 465 GLY A 321
REMARK 465 GLU A 322
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 7 OG1 CG2
REMARK 470 LYS A 37 CE NZ
REMARK 470 ARG A 41 NE CZ NH1 NH2
REMARK 470 GLU A 44 CG CD OE1 OE2
REMARK 470 GLU A 157 CG CD OE1 OE2
REMARK 470 GLU A 166 CG CD OE1 OE2
REMARK 470 ASP A 167 CG OD1 OD2
REMARK 470 TRP A 230 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 230 CZ3 CH2
REMARK 470 GLU A 254 CG CD OE1 OE2
REMARK 470 LYS A 259 CG CD CE NZ
REMARK 470 GLU A 263 CG CD OE1 OE2
REMARK 470 LYS A 266 CG CD CE NZ
REMARK 470 ARG A 298 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 299 CG CD CE NZ
REMARK 470 TRP A 323 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 323 CZ3 CH2
REMARK 470 GLU A 342 CG CD OE1 OE2
REMARK 470 LYS A 349 CE NZ
REMARK 470 LYS A 398 CE NZ
REMARK 470 ARG A 405 NE CZ NH1 NH2
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 1183 O HOH A 1235 1.81
REMARK 500 OD1 ASP A 155 O HOH A 1204 1.87
REMARK 500 O HOH A 1187 O HOH A 1225 1.92
REMARK 500 NH2 ARG A 325 O HOH A 1232 1.95
REMARK 500 O HOH A 1074 O HOH A 1199 2.04
REMARK 500 O HOH A 1202 O HOH A 1227 2.05
REMARK 500 O HOH A 1177 O HOH A 1217 2.05
REMARK 500 O THR A 7 O HOH A 1152 2.05
REMARK 500 O HOH A 1199 O HOH A 1210 2.06
REMARK 500 OE2 GLU A 211 O HOH A 1223 2.07
REMARK 500 O HOH A 1168 O HOH A 1226 2.08
REMARK 500 O HOH A 1161 O HOH A 1237 2.09
REMARK 500 O HOH A 1161 O HOH A 1192 2.15
REMARK 500 O HOH A 1013 O HOH A 1243 2.16
REMARK 500 O HOH A 1240 O HOH A 1257 2.17
REMARK 500 O HOH A 1013 O HOH A 1014 2.18
REMARK 500 NH2 ARG A 159 O HOH A 1204 2.19
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 1231 O HOH A 1234 6554 2.02
REMARK 500 O HOH A 1086 O HOH A 1167 4655 2.13
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 ASN A 66 85.62 -156.70
REMARK 500 LYS A 299 -30.15 -146.50
REMARK 500 ALA A 343 42.86 -92.67
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 900
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FDP RELATED DB: PDB
REMARK 900 RELATED ID: 4FDN RELATED DB: PDB
REMARK 900 RELATED ID: 4FDO RELATED DB: PDB
REMARK 900 RELATED ID: 4FF6 RELATED DB: PDB
DBREF 4FEH A 1 461 UNP P72056 DPRE1_MYCTU 1 461
SEQADV 4FEH MET A -19 UNP P72056 EXPRESSION TAG
SEQADV 4FEH GLY A -18 UNP P72056 EXPRESSION TAG
SEQADV 4FEH SER A -17 UNP P72056 EXPRESSION TAG
SEQADV 4FEH SER A -16 UNP P72056 EXPRESSION TAG
SEQADV 4FEH HIS A -15 UNP P72056 EXPRESSION TAG
SEQADV 4FEH HIS A -14 UNP P72056 EXPRESSION TAG
SEQADV 4FEH HIS A -13 UNP P72056 EXPRESSION TAG
SEQADV 4FEH HIS A -12 UNP P72056 EXPRESSION TAG
SEQADV 4FEH HIS A -11 UNP P72056 EXPRESSION TAG
SEQADV 4FEH HIS A -10 UNP P72056 EXPRESSION TAG
SEQADV 4FEH SER A -9 UNP P72056 EXPRESSION TAG
SEQADV 4FEH SER A -8 UNP P72056 EXPRESSION TAG
SEQADV 4FEH GLY A -7 UNP P72056 EXPRESSION TAG
SEQADV 4FEH LEU A -6 UNP P72056 EXPRESSION TAG
SEQADV 4FEH VAL A -5 UNP P72056 EXPRESSION TAG
SEQADV 4FEH PRO A -4 UNP P72056 EXPRESSION TAG
SEQADV 4FEH ARG A -3 UNP P72056 EXPRESSION TAG
SEQADV 4FEH GLY A -2 UNP P72056 EXPRESSION TAG
SEQADV 4FEH SER A -1 UNP P72056 EXPRESSION TAG
SEQADV 4FEH HIS A 0 UNP P72056 EXPRESSION TAG
SEQRES 1 A 481 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 481 LEU VAL PRO ARG GLY SER HIS MET LEU SER VAL GLY ALA
SEQRES 3 A 481 THR THR THR ALA THR ARG LEU THR GLY TRP GLY ARG THR
SEQRES 4 A 481 ALA PRO SER VAL ALA ASN VAL LEU ARG THR PRO ASP ALA
SEQRES 5 A 481 GLU MET ILE VAL LYS ALA VAL ALA ARG VAL ALA GLU SER
SEQRES 6 A 481 GLY GLY GLY ARG GLY ALA ILE ALA ARG GLY LEU GLY ARG
SEQRES 7 A 481 SER TYR GLY ASP ASN ALA GLN ASN GLY GLY GLY LEU VAL
SEQRES 8 A 481 ILE ASP MET THR PRO LEU ASN THR ILE HIS SER ILE ASP
SEQRES 9 A 481 ALA ASP THR LYS LEU VAL ASP ILE ASP ALA GLY VAL ASN
SEQRES 10 A 481 LEU ASP GLN LEU MET LYS ALA ALA LEU PRO PHE GLY LEU
SEQRES 11 A 481 TRP VAL PRO VAL LEU PRO GLY THR ARG GLN VAL THR VAL
SEQRES 12 A 481 GLY GLY ALA ILE ALA CYS ASP ILE HIS GLY LYS ASN HIS
SEQRES 13 A 481 HIS SER ALA GLY SER PHE GLY ASN HIS VAL ARG SER MET
SEQRES 14 A 481 ASP LEU LEU THR ALA ASP GLY GLU ILE ARG HIS LEU THR
SEQRES 15 A 481 PRO THR GLY GLU ASP ALA GLU LEU PHE TRP ALA THR VAL
SEQRES 16 A 481 GLY GLY ASN GLY LEU THR GLY ILE ILE MET ARG ALA THR
SEQRES 17 A 481 ILE GLU MET THR PRO THR SER THR ALA TYR PHE ILE ALA
SEQRES 18 A 481 ASP GLY ASP VAL THR ALA SER LEU ASP GLU THR ILE ALA
SEQRES 19 A 481 LEU HIS SER ASP GLY SER GLU ALA ARG TYR THR TYR SER
SEQRES 20 A 481 SER ALA TRP PHE ASP ALA ILE SER ALA PRO PRO LYS LEU
SEQRES 21 A 481 GLY ARG ALA ALA VAL SER ARG GLY ARG LEU ALA THR VAL
SEQRES 22 A 481 GLU GLN LEU PRO ALA LYS LEU ARG SER GLU PRO LEU LYS
SEQRES 23 A 481 PHE ASP ALA PRO GLN LEU LEU THR LEU PRO ASP VAL PHE
SEQRES 24 A 481 PRO ASN GLY LEU ALA ASN LYS TYR THR PHE GLY PRO ILE
SEQRES 25 A 481 GLY GLU LEU TRP TYR ARG LYS SER GLY THR TYR ARG GLY
SEQRES 26 A 481 LYS VAL GLN ASN LEU THR GLN PHE TYR HIS PRO LEU ASP
SEQRES 27 A 481 MET PHE GLY GLU TRP ASN ARG ALA TYR GLY PRO ALA GLY
SEQRES 28 A 481 PHE LEU GLN TYR GLN PHE VAL ILE PRO THR GLU ALA VAL
SEQRES 29 A 481 ASP GLU PHE LYS LYS ILE ILE GLY VAL ILE GLN ALA SER
SEQRES 30 A 481 GLY HIS TYR SER PHE LEU ASN VAL PHE LYS LEU PHE GLY
SEQRES 31 A 481 PRO ARG ASN GLN ALA PRO LEU SER PHE PRO ILE PRO GLY
SEQRES 32 A 481 TRP ASN ILE CYS VAL ASP PHE PRO ILE LYS ASP GLY LEU
SEQRES 33 A 481 GLY LYS PHE VAL SER GLU LEU ASP ARG ARG VAL LEU GLU
SEQRES 34 A 481 PHE GLY GLY ARG LEU TYR THR ALA LYS ASP SER ARG THR
SEQRES 35 A 481 THR ALA GLU THR PHE HIS ALA MET TYR PRO ARG VAL ASP
SEQRES 36 A 481 GLU TRP ILE SER VAL ARG ARG LYS VAL ASP PRO LEU ARG
SEQRES 37 A 481 VAL PHE ALA SER ASP MET ALA ARG ARG LEU GLU LEU LEU
HET FAD A 900 53
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 HOH *257(H2 O)
HELIX 1 1 ASP A 31 GLU A 44 1 14
HELIX 2 2 ASN A 97 LEU A 106 1 10
HELIX 3 3 THR A 122 CYS A 129 1 8
HELIX 4 4 ASN A 135 GLY A 140 1 6
HELIX 5 5 SER A 141 ASN A 144 5 4
HELIX 6 6 ASP A 167 VAL A 175 1 9
HELIX 7 7 SER A 208 SER A 217 1 10
HELIX 8 8 GLY A 219 TYR A 224 5 6
HELIX 9 9 THR A 252 LEU A 256 5 5
HELIX 10 10 PRO A 257 GLU A 263 5 7
HELIX 11 11 LEU A 310 HIS A 315 1 6
HELIX 12 12 ASN A 324 GLY A 328 1 5
HELIX 13 13 ALA A 343 SER A 357 1 15
HELIX 14 14 GLY A 395 PHE A 410 1 16
HELIX 15 15 THR A 416 ASP A 419 5 4
HELIX 16 16 THR A 423 TYR A 431 1 9
HELIX 17 17 ARG A 433 ASP A 445 1 13
HELIX 18 18 SER A 452 LEU A 458 1 7
SHEET 1 A 4 THR A 8 LEU A 13 0
SHEET 2 A 4 SER A 22 ARG A 28 -1 O SER A 22 N LEU A 13
SHEET 3 A 4 LEU A 70 ASP A 73 1 O VAL A 71 N LEU A 27
SHEET 4 A 4 ALA A 51 ARG A 54 1 N ARG A 54 O ILE A 72
SHEET 1 B 5 ILE A 80 ASP A 84 0
SHEET 2 B 5 LEU A 89 ASP A 93 -1 O ASP A 91 N SER A 82
SHEET 3 B 5 ILE A 183 GLU A 190 -1 O ALA A 187 N ILE A 92
SHEET 4 B 5 VAL A 146 LEU A 152 -1 N LEU A 152 O ILE A 183
SHEET 5 B 5 ILE A 158 LEU A 161 -1 O LEU A 161 N MET A 149
SHEET 1 C 2 LEU A 110 TRP A 111 0
SHEET 2 C 2 THR A 192 PRO A 193 -1 O THR A 192 N TRP A 111
SHEET 1 D 8 TYR A 303 ASN A 309 0
SHEET 2 D 8 TYR A 198 VAL A 205 -1 N PHE A 199 O GLN A 308
SHEET 3 D 8 ALA A 243 LEU A 250 -1 O ARG A 247 N ASP A 202
SHEET 4 D 8 TYR A 226 PHE A 231 -1 N SER A 228 O SER A 246
SHEET 5 D 8 VAL A 365 PHE A 369 -1 O PHE A 366 N ALA A 229
SHEET 6 D 8 GLY A 383 PRO A 391 -1 O ASN A 385 N LYS A 367
SHEET 7 D 8 PHE A 332 PRO A 340 -1 N TYR A 335 O VAL A 388
SHEET 8 D 8 ARG A 413 LEU A 414 -1 O ARG A 413 N VAL A 338
CISPEP 1 PRO A 237 PRO A 238 0 2.55
CISPEP 2 GLY A 328 PRO A 329 0 -2.72
SITE 1 AC1 34 TRP A 16 ILE A 52 ALA A 53 ARG A 54
SITE 2 AC1 34 GLY A 55 LEU A 56 GLY A 57 ARG A 58
SITE 3 AC1 34 SER A 59 TYR A 60 ASN A 63 ALA A 64
SITE 4 AC1 34 MET A 74 ALA A 94 PRO A 116 GLY A 117
SITE 5 AC1 34 THR A 118 VAL A 121 THR A 122 GLY A 124
SITE 6 AC1 34 GLY A 125 ALA A 128 CYS A 129 ILE A 131
SITE 7 AC1 34 HIS A 132 ASN A 178 GLY A 179 GLY A 182
SITE 8 AC1 34 ILE A 184 TYR A 415 ALA A 417 HOH A1002
SITE 9 AC1 34 HOH A1009 HOH A1197
CRYST1 127.880 127.880 64.300 90.00 90.00 120.00 P 64 6
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 0.007820 0.004515 0.000000 0.00000
SCALE2 0.000000 0.009030 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015552 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
