HEADER OXIDOREDUCTASE 21-AUG-18 6HFV
TITLE MYCOBACTERIUM TUBERCULOSIS DPRE1 IN COMPLEX WITH CMP2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DECAPRENYLPHOSPHORYL-BETA-D-RIBOSE OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: DECAPRENYLPHOSPHO-BETA-D-RIBOFURANOSE 2-DEHYDROGENASE,
COMPND 5 DECAPRENYLPHOSPHORYL-BETA-D-RIBOFURANOSE 2'-EPIMERASE SUBUNIT DPRE1,
COMPND 6 DECAPRENYL-PHOSPHORIBOSE 2'-EPIMERASE SUBUNIT 1,DECAPRENYLPHOSPHORYL-
COMPND 7 BETA-D-RIBOFURANOSE 2'-OXIDASE,DECAPRENYLPHOSPHORYL-BETA-D-RIBOSE 2-
COMPND 8 EPIMERASE FLAVOPROTEIN SUBUNIT,FAD-DEPENDENT DECAPRENYLPHOSPHORYL-
COMPND 9 BETA-D-RIBOFURANOSE 2-OXIDASE;
COMPND 10 EC: 1.1.98.3;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS (STRAIN ATCC 25618 /
SOURCE 3 H37RV);
SOURCE 4 ORGANISM_TAXID: 83332;
SOURCE 5 STRAIN: ATCC 25618 / H37RV;
SOURCE 6 GENE: DPRE1, RV3790;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS OXIDOREDUCTASE, OXIDOREDUCTASE INHIBITOR
EXPDTA X-RAY DIFFRACTION
AUTHOR C.CHUNG
REVDAT 2 21-AUG-19 6HFV 1 REMARK HET LINK SITE
REVDAT 2 2 1 ATOM
REVDAT 1 19-SEP-18 6HFV 0
JRNL AUTH A.RICHTER,I.RUDOLPH,U.MOLLMANN,K.VOIGT,C.W.CHUNG,
JRNL AUTH 2 O.M.P.SINGH,M.REES,A.MENDOZA-LOSANA,R.BATES,L.BALLELL,
JRNL AUTH 3 S.BATT,N.VEERAPEN,K.FUTTERER,G.BESRA,P.IMMING,A.ARGYROU
JRNL TITL NOVEL INSIGHT INTO THE REACTION OF NITRO, NITROSO AND
JRNL TITL 2 HYDROXYLAMINO BENZOTHIAZINONES AND OF BENZOXACINONES WITH
JRNL TITL 3 MYCOBACTERIUM TUBERCULOSIS DPRE1.
JRNL REF SCI REP V. 8 13473 2018
JRNL REFN ESSN 2045-2322
JRNL PMID 30194385
JRNL DOI 10.1038/S41598-018-31316-6
REMARK 2
REMARK 2 RESOLUTION. 2.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 2.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 57.40
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 3 NUMBER OF REFLECTIONS : 59902
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) : 0.178
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3190
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) : 2.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.10
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4400
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.41
REMARK 3 BIN R VALUE (WORKING SET) : 0.3100
REMARK 3 BIN FREE R VALUE SET COUNT : 236
REMARK 3 BIN FREE R VALUE : 0.3190
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6468
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 162
REMARK 3 SOLVENT ATOMS : 389
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.97
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.60000
REMARK 3 B22 (A**2) : 3.77000
REMARK 3 B33 (A**2) : -2.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -4.37000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.173
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.149
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.142
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.877
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 6791 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 6370 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9247 ; 1.152 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 14586 ; 0.782 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 835 ; 5.582 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 287 ;29.564 ;22.613
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1036 ;12.116 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 58 ;11.806 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1026 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 7615 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 1597 ; 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): 3364 ; 3.843 ; 7.666
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3363 ; 3.843 ; 7.665
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4191 ; 5.549 ;17.192
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4192 ; 5.548 ;17.194
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3427 ; 4.687 ; 8.289
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3428 ; 4.686 ; 8.291
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5057 ; 7.165 ;18.251
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 8119 ; 9.355 ;35.104
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 8120 ; 9.354 ;35.108
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 : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 7 A 679
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6678 -12.0807 36.4072
REMARK 3 T TENSOR
REMARK 3 T11: 0.0245 T22: 0.0226
REMARK 3 T33: 0.1578 T12: 0.0078
REMARK 3 T13: 0.0128 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 0.5600 L22: 0.3679
REMARK 3 L33: 0.6928 L12: -0.0699
REMARK 3 L13: 0.5523 L23: 0.1478
REMARK 3 S TENSOR
REMARK 3 S11: 0.0511 S12: -0.0501 S13: -0.0241
REMARK 3 S21: -0.0098 S22: 0.0392 S23: -0.0249
REMARK 3 S31: 0.0386 S32: -0.0293 S33: -0.0903
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 7 B 643
REMARK 3 ORIGIN FOR THE GROUP (A): -21.3261 -18.6578 0.6484
REMARK 3 T TENSOR
REMARK 3 T11: 0.0896 T22: 0.0840
REMARK 3 T33: 0.1571 T12: 0.0429
REMARK 3 T13: -0.0340 T23: -0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 1.6606 L22: 0.2220
REMARK 3 L33: 1.0842 L12: 0.5741
REMARK 3 L13: 0.8826 L23: 0.2224
REMARK 3 S TENSOR
REMARK 3 S11: 0.2091 S12: 0.2966 S13: -0.1357
REMARK 3 S21: 0.0878 S22: 0.0956 S23: -0.0018
REMARK 3 S31: 0.1864 S32: 0.2191 S33: -0.3047
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 6HFV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1200011586.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 25-SEP-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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) : 1.0725
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 63093
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050
REMARK 200 RESOLUTION RANGE LOW (A) : 57.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 3.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM IN 30% PPG, 100MM IMIDAZOLE, PH
REMARK 280 7.4, BATCH MODE, TEMPERATURE 298K
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 42.21500
REMARK 290 SMTRY3 2 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 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 APPLY THE FOLLOWING TO CHAINS: B
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 -13
REMARK 465 GLY A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 HIS A -9
REMARK 465 HIS A -8
REMARK 465 HIS A -7
REMARK 465 HIS A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 SER A -3
REMARK 465 GLN A -2
REMARK 465 ASP A -1
REMARK 465 PRO 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 GLY A 46
REMARK 465 GLY A 47
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 PHE A 320
REMARK 465 GLY A 321
REMARK 465 GLU A 322
REMARK 465 TRP A 323
REMARK 465 ASN A 324
REMARK 465 ARG A 325
REMARK 465 ALA A 326
REMARK 465 TYR A 327
REMARK 465 GLY A 328
REMARK 465 PRO A 329
REMARK 465 ALA A 330
REMARK 465 MET B -13
REMARK 465 GLY B -12
REMARK 465 SER B -11
REMARK 465 SER B -10
REMARK 465 HIS B -9
REMARK 465 HIS B -8
REMARK 465 HIS B -7
REMARK 465 HIS B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 SER B -3
REMARK 465 GLN B -2
REMARK 465 ASP B -1
REMARK 465 PRO B 0
REMARK 465 MET B 1
REMARK 465 LEU B 2
REMARK 465 SER B 3
REMARK 465 VAL B 4
REMARK 465 GLY B 5
REMARK 465 ALA B 6
REMARK 465 GLY B 46
REMARK 465 GLY B 47
REMARK 465 ALA B 269
REMARK 465 PRO B 270
REMARK 465 GLN B 271
REMARK 465 LEU B 272
REMARK 465 LEU B 273
REMARK 465 THR B 274
REMARK 465 LEU B 275
REMARK 465 PRO B 276
REMARK 465 ASP B 277
REMARK 465 VAL B 278
REMARK 465 PHE B 279
REMARK 465 PRO B 280
REMARK 465 ASN B 281
REMARK 465 GLY B 282
REMARK 465 LEU B 283
REMARK 465 ALA B 284
REMARK 465 ASN B 285
REMARK 465 LYS B 286
REMARK 465 TYR B 287
REMARK 465 THR B 288
REMARK 465 PHE B 289
REMARK 465 GLY B 290
REMARK 465 PRO B 291
REMARK 465 ILE B 292
REMARK 465 ASP B 318
REMARK 465 MET B 319
REMARK 465 PHE B 320
REMARK 465 GLY B 321
REMARK 465 GLU B 322
REMARK 465 TRP B 323
REMARK 465 ASN B 324
REMARK 465 ARG B 325
REMARK 465 ALA B 326
REMARK 465 TYR B 327
REMARK 465 GLY B 328
REMARK 465 PRO B 329
REMARK 465 ALA B 330
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 37 CE NZ
REMARK 470 LYS A 259 CG CD CE NZ
REMARK 470 LYS A 266 CG CD CE NZ
REMARK 470 ASP A 268 CG OD1 OD2
REMARK 470 LYS A 299 CE NZ
REMARK 470 MET A 319 CG SD CE
REMARK 470 LYS B 259 CG CD CE NZ
REMARK 470 LYS B 266 CG CD CE NZ
REMARK 470 LYS B 299 CG CD CE NZ
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 OD2 ASP B 268 ND2 ASN B 309 2.06
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 ALA B 20 70.49 56.34
REMARK 500 ASP B 130 61.83 39.88
REMARK 500 ALA B 258 -39.59 -38.71
REMARK 500 ALA B 343 39.79 -86.51
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 A 835 DISTANCE = 6.07 ANGSTROMS
REMARK 525 HOH A 836 DISTANCE = 6.34 ANGSTROMS
REMARK 525 HOH A 837 DISTANCE = 6.63 ANGSTROMS
REMARK 525 HOH A 838 DISTANCE = 6.91 ANGSTROMS
REMARK 525 HOH A 839 DISTANCE = 6.97 ANGSTROMS
REMARK 525 HOH A 840 DISTANCE = 6.99 ANGSTROMS
REMARK 525 HOH A 841 DISTANCE = 7.18 ANGSTROMS
REMARK 525 HOH A 842 DISTANCE = 8.14 ANGSTROMS
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue G1T A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide G1T B 502 and CYS B
REMARK 800 387
DBREF 6HFV A 1 461 UNP P9WJF1 DPRE1_MYCTU 1 461
DBREF 6HFV B 1 461 UNP P9WJF1 DPRE1_MYCTU 1 461
SEQADV 6HFV MET A -13 UNP P9WJF1 INITIATING METHIONINE
SEQADV 6HFV GLY A -12 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV SER A -11 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV SER A -10 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV HIS A -9 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV HIS A -8 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV HIS A -7 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV HIS A -6 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV HIS A -5 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV HIS A -4 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV SER A -3 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV GLN A -2 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV ASP A -1 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV PRO A 0 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV MET B -13 UNP P9WJF1 INITIATING METHIONINE
SEQADV 6HFV GLY B -12 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV SER B -11 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV SER B -10 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV HIS B -9 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV HIS B -8 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV HIS B -7 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV HIS B -6 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV HIS B -5 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV HIS B -4 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV SER B -3 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV GLN B -2 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV ASP B -1 UNP P9WJF1 EXPRESSION TAG
SEQADV 6HFV PRO B 0 UNP P9WJF1 EXPRESSION TAG
SEQRES 1 A 475 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 A 475 PRO MET LEU SER VAL GLY ALA THR THR THR ALA THR ARG
SEQRES 3 A 475 LEU THR GLY TRP GLY ARG THR ALA PRO SER VAL ALA ASN
SEQRES 4 A 475 VAL LEU ARG THR PRO ASP ALA GLU MET ILE VAL LYS ALA
SEQRES 5 A 475 VAL ALA ARG VAL ALA GLU SER GLY GLY GLY ARG GLY ALA
SEQRES 6 A 475 ILE ALA ARG GLY LEU GLY ARG SER TYR GLY ASP ASN ALA
SEQRES 7 A 475 GLN ASN GLY GLY GLY LEU VAL ILE ASP MET THR PRO LEU
SEQRES 8 A 475 ASN THR ILE HIS SER ILE ASP ALA ASP THR LYS LEU VAL
SEQRES 9 A 475 ASP ILE ASP ALA GLY VAL ASN LEU ASP GLN LEU MET LYS
SEQRES 10 A 475 ALA ALA LEU PRO PHE GLY LEU TRP VAL PRO VAL LEU PRO
SEQRES 11 A 475 GLY THR ARG GLN VAL THR VAL GLY GLY ALA ILE ALA CYS
SEQRES 12 A 475 ASP ILE HIS GLY LYS ASN HIS HIS SER ALA GLY SER PHE
SEQRES 13 A 475 GLY ASN HIS VAL ARG SER MET ASP LEU LEU THR ALA ASP
SEQRES 14 A 475 GLY GLU ILE ARG HIS LEU THR PRO THR GLY GLU ASP ALA
SEQRES 15 A 475 GLU LEU PHE TRP ALA THR VAL GLY GLY ASN GLY LEU THR
SEQRES 16 A 475 GLY ILE ILE MET ARG ALA THR ILE GLU MET THR PRO THR
SEQRES 17 A 475 SER THR ALA TYR PHE ILE ALA ASP GLY ASP VAL THR ALA
SEQRES 18 A 475 SER LEU ASP GLU THR ILE ALA LEU HIS SER ASP GLY SER
SEQRES 19 A 475 GLU ALA ARG TYR THR TYR SER SER ALA TRP PHE ASP ALA
SEQRES 20 A 475 ILE SER ALA PRO PRO LYS LEU GLY ARG ALA ALA VAL SER
SEQRES 21 A 475 ARG GLY ARG LEU ALA THR VAL GLU GLN LEU PRO ALA LYS
SEQRES 22 A 475 LEU ARG SER GLU PRO LEU LYS PHE ASP ALA PRO GLN LEU
SEQRES 23 A 475 LEU THR LEU PRO ASP VAL PHE PRO ASN GLY LEU ALA ASN
SEQRES 24 A 475 LYS TYR THR PHE GLY PRO ILE GLY GLU LEU TRP TYR ARG
SEQRES 25 A 475 LYS SER GLY THR TYR ARG GLY LYS VAL GLN ASN LEU THR
SEQRES 26 A 475 GLN PHE TYR HIS PRO LEU ASP MET PHE GLY GLU TRP ASN
SEQRES 27 A 475 ARG ALA TYR GLY PRO ALA GLY PHE LEU GLN TYR GLN PHE
SEQRES 28 A 475 VAL ILE PRO THR GLU ALA VAL ASP GLU PHE LYS LYS ILE
SEQRES 29 A 475 ILE GLY VAL ILE GLN ALA SER GLY HIS TYR SER PHE LEU
SEQRES 30 A 475 ASN VAL PHE LYS LEU PHE GLY PRO ARG ASN GLN ALA PRO
SEQRES 31 A 475 LEU SER PHE PRO ILE PRO GLY TRP ASN ILE CYS VAL ASP
SEQRES 32 A 475 PHE PRO ILE LYS ASP GLY LEU GLY LYS PHE VAL SER GLU
SEQRES 33 A 475 LEU ASP ARG ARG VAL LEU GLU PHE GLY GLY ARG LEU TYR
SEQRES 34 A 475 THR ALA LYS ASP SER ARG THR THR ALA GLU THR PHE HIS
SEQRES 35 A 475 ALA MET TYR PRO ARG VAL ASP GLU TRP ILE SER VAL ARG
SEQRES 36 A 475 ARG LYS VAL ASP PRO LEU ARG VAL PHE ALA SER ASP MET
SEQRES 37 A 475 ALA ARG ARG LEU GLU LEU LEU
SEQRES 1 B 475 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP
SEQRES 2 B 475 PRO MET LEU SER VAL GLY ALA THR THR THR ALA THR ARG
SEQRES 3 B 475 LEU THR GLY TRP GLY ARG THR ALA PRO SER VAL ALA ASN
SEQRES 4 B 475 VAL LEU ARG THR PRO ASP ALA GLU MET ILE VAL LYS ALA
SEQRES 5 B 475 VAL ALA ARG VAL ALA GLU SER GLY GLY GLY ARG GLY ALA
SEQRES 6 B 475 ILE ALA ARG GLY LEU GLY ARG SER TYR GLY ASP ASN ALA
SEQRES 7 B 475 GLN ASN GLY GLY GLY LEU VAL ILE ASP MET THR PRO LEU
SEQRES 8 B 475 ASN THR ILE HIS SER ILE ASP ALA ASP THR LYS LEU VAL
SEQRES 9 B 475 ASP ILE ASP ALA GLY VAL ASN LEU ASP GLN LEU MET LYS
SEQRES 10 B 475 ALA ALA LEU PRO PHE GLY LEU TRP VAL PRO VAL LEU PRO
SEQRES 11 B 475 GLY THR ARG GLN VAL THR VAL GLY GLY ALA ILE ALA CYS
SEQRES 12 B 475 ASP ILE HIS GLY LYS ASN HIS HIS SER ALA GLY SER PHE
SEQRES 13 B 475 GLY ASN HIS VAL ARG SER MET ASP LEU LEU THR ALA ASP
SEQRES 14 B 475 GLY GLU ILE ARG HIS LEU THR PRO THR GLY GLU ASP ALA
SEQRES 15 B 475 GLU LEU PHE TRP ALA THR VAL GLY GLY ASN GLY LEU THR
SEQRES 16 B 475 GLY ILE ILE MET ARG ALA THR ILE GLU MET THR PRO THR
SEQRES 17 B 475 SER THR ALA TYR PHE ILE ALA ASP GLY ASP VAL THR ALA
SEQRES 18 B 475 SER LEU ASP GLU THR ILE ALA LEU HIS SER ASP GLY SER
SEQRES 19 B 475 GLU ALA ARG TYR THR TYR SER SER ALA TRP PHE ASP ALA
SEQRES 20 B 475 ILE SER ALA PRO PRO LYS LEU GLY ARG ALA ALA VAL SER
SEQRES 21 B 475 ARG GLY ARG LEU ALA THR VAL GLU GLN LEU PRO ALA LYS
SEQRES 22 B 475 LEU ARG SER GLU PRO LEU LYS PHE ASP ALA PRO GLN LEU
SEQRES 23 B 475 LEU THR LEU PRO ASP VAL PHE PRO ASN GLY LEU ALA ASN
SEQRES 24 B 475 LYS TYR THR PHE GLY PRO ILE GLY GLU LEU TRP TYR ARG
SEQRES 25 B 475 LYS SER GLY THR TYR ARG GLY LYS VAL GLN ASN LEU THR
SEQRES 26 B 475 GLN PHE TYR HIS PRO LEU ASP MET PHE GLY GLU TRP ASN
SEQRES 27 B 475 ARG ALA TYR GLY PRO ALA GLY PHE LEU GLN TYR GLN PHE
SEQRES 28 B 475 VAL ILE PRO THR GLU ALA VAL ASP GLU PHE LYS LYS ILE
SEQRES 29 B 475 ILE GLY VAL ILE GLN ALA SER GLY HIS TYR SER PHE LEU
SEQRES 30 B 475 ASN VAL PHE LYS LEU PHE GLY PRO ARG ASN GLN ALA PRO
SEQRES 31 B 475 LEU SER PHE PRO ILE PRO GLY TRP ASN ILE CYS VAL ASP
SEQRES 32 B 475 PHE PRO ILE LYS ASP GLY LEU GLY LYS PHE VAL SER GLU
SEQRES 33 B 475 LEU ASP ARG ARG VAL LEU GLU PHE GLY GLY ARG LEU TYR
SEQRES 34 B 475 THR ALA LYS ASP SER ARG THR THR ALA GLU THR PHE HIS
SEQRES 35 B 475 ALA MET TYR PRO ARG VAL ASP GLU TRP ILE SER VAL ARG
SEQRES 36 B 475 ARG LYS VAL ASP PRO LEU ARG VAL PHE ALA SER ASP MET
SEQRES 37 B 475 ALA ARG ARG LEU GLU LEU LEU
HET FAD A 501 53
HET IMD A 502 5
HET G1T A 503 23
HET FAD B 501 53
HET G1T B 502 23
HET IMD B 503 5
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM IMD IMIDAZOLE
HETNAM G1T 8-(OXIDANYLAMINO)-2-PIPERIDIN-1-YL-6-(TRIFLUOROMETHYL)-
HETNAM 2 G1T 1,3-BENZOTHIAZIN-4-ONE
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 IMD 2(C3 H5 N2 1+)
FORMUL 5 G1T 2(C14 H14 F3 N3 O2 S)
FORMUL 9 HOH *389(H2 O)
HELIX 1 AA1 ASP A 31 ALA A 43 1 13
HELIX 2 AA2 ASN A 97 LEU A 106 1 10
HELIX 3 AA3 THR A 122 CYS A 129 1 8
HELIX 4 AA4 ASN A 135 GLY A 140 1 6
HELIX 5 AA5 SER A 141 ASN A 144 5 4
HELIX 6 AA6 ASP A 167 VAL A 175 1 9
HELIX 7 AA7 SER A 208 ASP A 218 1 11
HELIX 8 AA8 GLY A 219 TYR A 224 5 6
HELIX 9 AA9 THR A 252 LEU A 256 5 5
HELIX 10 AB1 PRO A 257 SER A 262 1 6
HELIX 11 AB2 GLY A 290 GLY A 301 1 12
HELIX 12 AB3 ASN A 309 HIS A 315 1 7
HELIX 13 AB4 ALA A 343 ALA A 356 1 14
HELIX 14 AB5 GLY A 395 PHE A 410 1 16
HELIX 15 AB6 THR A 416 ASP A 419 5 4
HELIX 16 AB7 THR A 423 TYR A 431 1 9
HELIX 17 AB8 ARG A 433 ASP A 445 1 13
HELIX 18 AB9 SER A 452 LEU A 458 1 7
HELIX 19 AC1 ASP B 31 SER B 45 1 15
HELIX 20 AC2 ASN B 97 LEU B 106 1 10
HELIX 21 AC3 THR B 122 CYS B 129 1 8
HELIX 22 AC4 ASN B 135 GLY B 140 1 6
HELIX 23 AC5 SER B 141 ASN B 144 5 4
HELIX 24 AC6 ASP B 167 VAL B 175 1 9
HELIX 25 AC7 SER B 208 ASP B 218 1 11
HELIX 26 AC8 GLY B 219 TYR B 224 5 6
HELIX 27 AC9 THR B 252 LEU B 256 5 5
HELIX 28 AD1 PRO B 257 SER B 262 1 6
HELIX 29 AD2 GLU B 294 THR B 302 1 9
HELIX 30 AD3 ASN B 309 HIS B 315 1 7
HELIX 31 AD4 ALA B 343 SER B 357 1 15
HELIX 32 AD5 GLY B 395 PHE B 410 1 16
HELIX 33 AD6 THR B 423 TYR B 431 1 9
HELIX 34 AD7 ARG B 433 ASP B 445 1 13
HELIX 35 AD8 SER B 452 LEU B 458 1 7
SHEET 1 AA1 4 THR A 8 LEU A 13 0
SHEET 2 AA1 4 SER A 22 ARG A 28 -1 O ALA A 24 N THR A 11
SHEET 3 AA1 4 LEU A 70 ASP A 73 1 O ASP A 73 N LEU A 27
SHEET 4 AA1 4 ALA A 51 ARG A 54 1 N ARG A 54 O ILE A 72
SHEET 1 AA210 ILE A 158 LEU A 161 0
SHEET 2 AA210 VAL A 146 LEU A 152 -1 N MET A 149 O LEU A 161
SHEET 3 AA210 ILE A 183 GLU A 190 -1 O MET A 185 N ASP A 150
SHEET 4 AA210 LEU A 89 ASP A 93 -1 N ILE A 92 O ALA A 187
SHEET 5 AA210 ILE A 80 ASP A 84 -1 N SER A 82 O ASP A 91
SHEET 6 AA210 ILE B 80 ASP B 84 -1 O ILE B 83 N ILE A 83
SHEET 7 AA210 LEU B 89 ASP B 93 -1 O ASP B 91 N SER B 82
SHEET 8 AA210 ILE B 183 GLU B 190 -1 O ALA B 187 N ILE B 92
SHEET 9 AA210 VAL B 146 LEU B 152 -1 N ASP B 150 O MET B 185
SHEET 10 AA210 ILE B 158 LEU B 161 -1 O LEU B 161 N MET B 149
SHEET 1 AA3 2 LEU A 110 TRP A 111 0
SHEET 2 AA3 2 THR A 192 PRO A 193 -1 O THR A 192 N TRP A 111
SHEET 1 AA4 8 TYR A 303 GLN A 308 0
SHEET 2 AA4 8 PHE A 199 VAL A 205 -1 N PHE A 199 O GLN A 308
SHEET 3 AA4 8 ALA A 243 LEU A 250 -1 O VAL A 245 N ASP A 204
SHEET 4 AA4 8 TYR A 226 PHE A 231 -1 N SER A 228 O SER A 246
SHEET 5 AA4 8 VAL A 365 PHE A 369 -1 O PHE A 366 N ALA A 229
SHEET 6 AA4 8 GLY A 383 PRO A 391 -1 O ASN A 385 N LYS A 367
SHEET 7 AA4 8 PHE A 332 PRO A 340 -1 N TYR A 335 O VAL A 388
SHEET 8 AA4 8 ARG A 413 LEU A 414 -1 O ARG A 413 N VAL A 338
SHEET 1 AA5 4 THR B 9 LEU B 13 0
SHEET 2 AA5 4 SER B 22 ARG B 28 -1 O VAL B 26 N THR B 9
SHEET 3 AA5 4 LEU B 70 ASP B 73 1 O VAL B 71 N ASN B 25
SHEET 4 AA5 4 ALA B 51 ARG B 54 1 N ARG B 54 O ILE B 72
SHEET 1 AA6 2 LEU B 110 TRP B 111 0
SHEET 2 AA6 2 THR B 192 PRO B 193 -1 O THR B 192 N TRP B 111
SHEET 1 AA7 8 TYR B 303 GLN B 308 0
SHEET 2 AA7 8 PHE B 199 VAL B 205 -1 N PHE B 199 O GLN B 308
SHEET 3 AA7 8 ALA B 243 LEU B 250 -1 O ARG B 247 N ASP B 202
SHEET 4 AA7 8 TYR B 226 PHE B 231 -1 N SER B 228 O SER B 246
SHEET 5 AA7 8 VAL B 365 PHE B 369 -1 O PHE B 366 N ALA B 229
SHEET 6 AA7 8 GLY B 383 PRO B 391 -1 O ASN B 385 N LYS B 367
SHEET 7 AA7 8 PHE B 332 PRO B 340 -1 N TYR B 335 O VAL B 388
SHEET 8 AA7 8 ARG B 413 LEU B 414 -1 O ARG B 413 N VAL B 338
LINK SG CYS A 387 N3 G1T A 503 1555 1555 1.69
LINK SG CYS B 387 N3 G1T B 502 1555 1555 1.69
CISPEP 1 PRO A 237 PRO A 238 0 12.60
CISPEP 2 PRO B 237 PRO B 238 0 1.69
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 G1T A 503
SITE 9 AC1 34 HOH A 678 HOH A 742
SITE 1 AC2 4 SER A 82 ASP A 84 SER B 82 ASP B 84
SITE 1 AC3 13 GLY A 117 HIS A 132 GLY A 133 LYS A 134
SITE 2 AC3 13 LEU A 317 GLN A 336 LYS A 367 ASN A 385
SITE 3 AC3 13 CYS A 387 LYS A 418 FAD A 501 HOH A 623
SITE 4 AC3 13 HOH A 729
SITE 1 AC4 32 TRP B 16 ILE B 52 ALA B 53 GLY B 55
SITE 2 AC4 32 LEU B 56 GLY B 57 ARG B 58 SER B 59
SITE 3 AC4 32 TYR B 60 ASN B 63 ALA B 64 MET B 74
SITE 4 AC4 32 ALA B 94 PRO B 116 GLY B 117 THR B 118
SITE 5 AC4 32 VAL B 121 THR B 122 GLY B 124 GLY B 125
SITE 6 AC4 32 ALA B 128 CYS B 129 ILE B 131 HIS B 132
SITE 7 AC4 32 ASN B 178 GLY B 179 GLY B 182 ILE B 184
SITE 8 AC4 32 TYR B 415 ALA B 417 G1T B 502 HOH B 681
SITE 1 AC5 3 SER B 228 TRP B 230 PRO B 316
SITE 1 AC6 16 GLY B 117 HIS B 132 GLY B 133 LYS B 134
SITE 2 AC6 16 LEU B 317 TYR B 335 GLN B 336 ASN B 364
SITE 3 AC6 16 VAL B 365 LYS B 367 ASN B 385 ILE B 386
SITE 4 AC6 16 VAL B 388 LYS B 418 FAD B 501 HOH B 604
CRYST1 78.080 84.430 80.450 90.00 103.00 90.00 P 1 21 1 4
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 0.012807 0.000000 0.002957 0.00000
SCALE2 0.000000 0.011844 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012757 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
