HEADER OXIDOREDUCTASE 29-APR-09 3H8L
TITLE THE FIRST X-RAY STRUCTURE OF A SULFIDE:QUINONE
TITLE 2 OXIDOREDUCTASE: INSIGHTS INTO SULFIDE OXIDATION MECHANISM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NADH OXIDASE;
COMPND 3 CHAIN: A, B;
COMPND 4 EC: 1.6.99.3
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACIDIANUS AMBIVALENS;
SOURCE 3 ORGANISM_COMMON: DESULFUROLOBUS AMBIVALENS;
SOURCE 4 ORGANISM_TAXID: 2283
KEYWDS MEMBRANE PROTEIN, COMPLETE FORM, ROSSMAN-LIKE FOLD,
KEYWDS 2 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.BRITO,F.L.SOUSA,M.STELTER,T.M.BANDEIRAS,C.VONRHEIN,
AUTHOR 2 M.TEIXEIRA,M.M.PEREIRA,M.ARCHER
REVDAT 2 23-JUN-09 3H8L 1 JRNL
REVDAT 1 02-JUN-09 3H8L 0
JRNL AUTH J.A.BRITO,F.L.SOUSA,M.STELTER,T.M.BANDEIRAS,
JRNL AUTH 2 C.VONRHEIN,M.TEIXEIRA,M.M.PEREIRA,M.ARCHER
JRNL TITL STRUCTURAL AND FUNCTIONAL INSIGHTS INTO
JRNL TITL 2 SULFIDE:QUINONE OXIDOREDUCTASE.
JRNL REF BIOCHEMISTRY V. 48 5613 2009
JRNL REFN ISSN 0006-2960
JRNL PMID 19438211
JRNL DOI 10.1021/BI9003827
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.57 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT 2.7.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SMART,VONRHEIN,WOMACK,
REMARK 3 : MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.57
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 49437
REMARK 3
REMARK 3 USING DATA ABOVE SIGMA CUTOFF.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.195
REMARK 3 R VALUE (WORKING SET) : 0.194
REMARK 3 FREE R VALUE : 0.222
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080
REMARK 3 FREE R VALUE TEST SET COUNT : 2509
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.57
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.64
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.17
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3264
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2363
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3106
REMARK 3 BIN R VALUE (WORKING SET) : 0.2351
REMARK 3 BIN FREE R VALUE : 0.2586
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.84
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 158
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5590
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 157
REMARK 3 SOLVENT ATOMS : 267
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 67.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.49
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.65360
REMARK 3 B22 (A**2) : -0.65360
REMARK 3 B33 (A**2) : 1.30720
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES RMS WEIGHT COUNT
REMARK 3 BOND LENGTHS (A) : 0.006 ; 2.000 ; 5890
REMARK 3 BOND ANGLES (DEGREES) : 0.892 ; 2.000 ; 7980
REMARK 3 TORSION ANGLES (DEGREES) : 16.089 ; 2.000 ; 1196
REMARK 3 PSEUDOROTATION ANGLES (DEGREES) : NULL ; NULL ; NULL
REMARK 3 TRIGONAL CARBON PLANES (A) : 0.005 ; 2.000 ; 158
REMARK 3 GENERAL PLANES (A) : 0.012 ; 5.000 ; 880
REMARK 3 ISOTROPIC THERMAL FACTORS (A**2) : 0.898 ; 20.000; 5890
REMARK 3 NON-BONDED CONTACTS (A) : 0.000 ; 5.000 ; 93
REMARK 3
REMARK 3 INCORRECT CHIRAL-CENTERS (COUNT) : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3H8L COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-09.
REMARK 100 THE RCSB ID CODE IS RCSB052828.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-APR-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.5; 4.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.943
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49511
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.570
REMARK 200 RESOLUTION RANGE LOW (A) : 51.440
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.600
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 20.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.57
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.71
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.30
REMARK 200 R MERGE FOR SHELL (I) : 0.51000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.80
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.2 M NH4H2PO4, 100 MM TRIS-HCL PH
REMARK 280 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K. 2.2 M
REMARK 280 NH4H2PO4/K2HPO4, PH 4.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 108.93133
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 54.46567
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 81.69850
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 27.23283
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 136.16417
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 108.93133
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 54.46567
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 27.23283
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 81.69850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 136.16417
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7640 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29020 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 1
REMARK 465 GLY A 358
REMARK 465 TYR A 359
REMARK 465 ALA A 360
REMARK 465 VAL A 361
REMARK 465 SER A 362
REMARK 465 VAL A 363
REMARK 465 LYS A 364
REMARK 465 ASP A 365
REMARK 465 ASP A 366
REMARK 465 THR A 367
REMARK 465 TRP A 368
REMARK 465 TYR A 369
REMARK 465 GLY A 370
REMARK 465 GLY A 371
REMARK 465 THR A 372
REMARK 465 VAL A 373
REMARK 465 SER A 374
REMARK 465 ILE A 375
REMARK 465 ALA A 376
REMARK 465 ASP A 377
REMARK 465 PRO A 378
REMARK 465 ALA A 379
REMARK 465 ALA A 380
REMARK 465 VAL A 381
REMARK 465 ASN A 382
REMARK 465 HIS A 383
REMARK 465 LEU A 384
REMARK 465 LYS A 385
REMARK 465 LYS A 386
REMARK 465 GLU A 387
REMARK 465 LEU A 388
REMARK 465 PHE A 389
REMARK 465 THR A 390
REMARK 465 LYS A 391
REMARK 465 TYR A 392
REMARK 465 TYR A 393
REMARK 465 MET A 394
REMARK 465 TRP A 395
REMARK 465 THR A 396
REMARK 465 LYS A 397
REMARK 465 GLY A 398
REMARK 465 ASP A 399
REMARK 465 MET A 400
REMARK 465 ALA A 401
REMARK 465 LEU A 402
REMARK 465 GLU A 403
REMARK 465 LYS A 404
REMARK 465 PHE A 405
REMARK 465 LEU A 406
REMARK 465 ALA A 407
REMARK 465 SER A 408
REMARK 465 TRP A 409
REMARK 465 MET B 1
REMARK 465 GLY B 358
REMARK 465 TYR B 359
REMARK 465 ALA B 360
REMARK 465 VAL B 361
REMARK 465 SER B 362
REMARK 465 VAL B 363
REMARK 465 LYS B 364
REMARK 465 ASP B 365
REMARK 465 ASP B 366
REMARK 465 THR B 367
REMARK 465 TRP B 368
REMARK 465 TYR B 369
REMARK 465 GLY B 370
REMARK 465 GLY B 371
REMARK 465 THR B 372
REMARK 465 VAL B 373
REMARK 465 SER B 374
REMARK 465 ILE B 375
REMARK 465 ALA B 376
REMARK 465 ASP B 377
REMARK 465 PRO B 378
REMARK 465 ALA B 379
REMARK 465 ALA B 380
REMARK 465 VAL B 381
REMARK 465 ASN B 382
REMARK 465 HIS B 383
REMARK 465 LEU B 384
REMARK 465 LYS B 385
REMARK 465 LYS B 386
REMARK 465 GLU B 387
REMARK 465 LEU B 388
REMARK 465 PHE B 389
REMARK 465 THR B 390
REMARK 465 LYS B 391
REMARK 465 TYR B 392
REMARK 465 TYR B 393
REMARK 465 MET B 394
REMARK 465 TRP B 395
REMARK 465 THR B 396
REMARK 465 LYS B 397
REMARK 465 GLY B 398
REMARK 465 ASP B 399
REMARK 465 MET B 400
REMARK 465 ALA B 401
REMARK 465 LEU B 402
REMARK 465 GLU B 403
REMARK 465 LYS B 404
REMARK 465 PHE B 405
REMARK 465 LEU B 406
REMARK 465 ALA B 407
REMARK 465 SER B 408
REMARK 465 TRP B 409
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 GLU A 211 O HOH A 556 1.83
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 PRO A 131 C - N - CD ANGL. DEV. = -22.1 DEGREES
REMARK 500 GLU A 211 N - CA - C ANGL. DEV. = 21.5 DEGREES
REMARK 500 TYR A 212 N - CA - CB ANGL. DEV. = 21.2 DEGREES
REMARK 500 PRO B 131 C - N - CD ANGL. DEV. = -22.0 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 ARG A 10 -139.34 -130.55
REMARK 500 ARG A 42 -169.30 -108.38
REMARK 500 PRO A 46 173.44 -58.09
REMARK 500 ASP A 56 92.71 -166.49
REMARK 500 ALA A 111 -148.53 -108.09
REMARK 500 PRO A 131 -84.69 -18.20
REMARK 500 TYR A 212 107.89 93.93
REMARK 500 ILE A 348 -58.78 76.35
REMARK 500 ARG B 10 -139.55 -128.77
REMARK 500 ARG B 42 -168.51 -109.15
REMARK 500 PRO B 46 173.56 -58.93
REMARK 500 ASP B 56 94.32 -166.10
REMARK 500 ALA B 111 -148.69 -107.54
REMARK 500 PRO B 131 -84.40 -17.88
REMARK 500 THR B 278 109.80 -42.97
REMARK 500 ILE B 348 -58.71 76.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 GLU A 211 13.4 L L OUTSIDE RANGE
REMARK 500 TYR A 212 16.9 L L OUTSIDE RANGE
REMARK 500 SER A 214 24.6 L L OUTSIDE RANGE
REMARK 500 ASP B 300 24.9 L L OUTSIDE RANGE
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 1001
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S3H A 1002
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 2001
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 2002
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 2003
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 410
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 2003
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1001
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S3H B 1002
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 2001
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 2002
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 410
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 411
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3H8I RELATED DB: PDB
REMARK 900 TRUNCATED VERSION OF THE SAME PROTEIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 ACCORDING TO THE AUTHORS THE UNP DATABASE SEQUENCE IS
REMARK 999 IN ERROR AT THIS POSITION
DBREF 3H8L A 1 409 UNP Q7ZAG8 Q7ZAG8_ACIAM 1 409
DBREF 3H8L B 1 409 UNP Q7ZAG8 Q7ZAG8_ACIAM 1 409
SEQADV 3H8L VAL A 349 UNP Q7ZAG8 MET 349 SEE REMARK 999
SEQADV 3H8L VAL B 349 UNP Q7ZAG8 MET 349 SEE REMARK 999
SEQRES 1 A 409 MET THR LYS VAL LEU VAL LEU GLY GLY ARG PHE GLY ALA
SEQRES 2 A 409 LEU THR ALA ALA TYR THR LEU LYS ARG LEU VAL GLY SER
SEQRES 3 A 409 LYS ALA ASP VAL LYS VAL ILE ASN LYS SER ARG PHE SER
SEQRES 4 A 409 TYR PHE ARG PRO ALA LEU PRO HIS VAL ALA ILE GLY VAL
SEQRES 5 A 409 ARG ASP VAL ASP GLU LEU LYS VAL ASP LEU SER GLU ALA
SEQRES 6 A 409 LEU PRO GLU LYS GLY ILE GLN PHE GLN GLU GLY THR VAL
SEQRES 7 A 409 GLU LYS ILE ASP ALA LYS SER SER MET VAL TYR TYR THR
SEQRES 8 A 409 LYS PRO ASP GLY SER MET ALA GLU GLU GLU TYR ASP TYR
SEQRES 9 A 409 VAL ILE VAL GLY ILE GLY ALA HIS LEU ALA THR GLU LEU
SEQRES 10 A 409 VAL LYS GLY TRP ASP LYS TYR GLY TYR SER VAL CYS GLU
SEQRES 11 A 409 PRO GLU PHE ALA THR LYS LEU ARG GLU LYS LEU GLU SER
SEQRES 12 A 409 PHE GLN GLY GLY ASN ILE ALA ILE GLY SER GLY PRO PHE
SEQRES 13 A 409 TYR GLN GLY HIS ASN PRO LYS PRO LYS VAL PRO GLU ASN
SEQRES 14 A 409 PHE VAL PRO ASN ALA ASP SER ALA CYS GLU GLY PRO VAL
SEQRES 15 A 409 PHE GLU MET SER LEU MET LEU HIS GLY TYR PHE LYS LYS
SEQRES 16 A 409 LYS GLY MET LEU ASP LYS VAL HIS VAL THR VAL PHE SER
SEQRES 17 A 409 PRO GLY GLU TYR LEU SER ASP LEU SER PRO ASN SER ARG
SEQRES 18 A 409 LYS ALA VAL ALA SER ILE TYR ASN GLN LEU GLY ILE LYS
SEQRES 19 A 409 LEU VAL HIS ASN PHE LYS ILE LYS GLU ILE ARG GLU HIS
SEQRES 20 A 409 GLU ILE VAL ASP GLU LYS GLY ASN THR ILE PRO ALA ASP
SEQRES 21 A 409 ILE THR ILE LEU LEU PRO PRO TYR THR GLY ASN PRO ALA
SEQRES 22 A 409 LEU LYS ASN SER THR PRO ASP LEU VAL ASP ASP GLY GLY
SEQRES 23 A 409 PHE ILE PRO THR ASP LEU ASN MET VAL SER ILE LYS TYR
SEQRES 24 A 409 ASP ASN VAL TYR ALA VAL GLY ASP ALA ASN SER MET THR
SEQRES 25 A 409 VAL PRO LYS LEU GLY TYR LEU ALA VAL MET THR GLY ARG
SEQRES 26 A 409 ILE ALA ALA GLN HIS LEU ALA ASN ARG LEU GLY VAL PRO
SEQRES 27 A 409 THR LYS VAL ASP LYS TYR TYR PRO THR ILE VAL CYS VAL
SEQRES 28 A 409 ALA ASP ASN PRO TYR GLU GLY TYR ALA VAL SER VAL LYS
SEQRES 29 A 409 ASP ASP THR TRP TYR GLY GLY THR VAL SER ILE ALA ASP
SEQRES 30 A 409 PRO ALA ALA VAL ASN HIS LEU LYS LYS GLU LEU PHE THR
SEQRES 31 A 409 LYS TYR TYR MET TRP THR LYS GLY ASP MET ALA LEU GLU
SEQRES 32 A 409 LYS PHE LEU ALA SER TRP
SEQRES 1 B 409 MET THR LYS VAL LEU VAL LEU GLY GLY ARG PHE GLY ALA
SEQRES 2 B 409 LEU THR ALA ALA TYR THR LEU LYS ARG LEU VAL GLY SER
SEQRES 3 B 409 LYS ALA ASP VAL LYS VAL ILE ASN LYS SER ARG PHE SER
SEQRES 4 B 409 TYR PHE ARG PRO ALA LEU PRO HIS VAL ALA ILE GLY VAL
SEQRES 5 B 409 ARG ASP VAL ASP GLU LEU LYS VAL ASP LEU SER GLU ALA
SEQRES 6 B 409 LEU PRO GLU LYS GLY ILE GLN PHE GLN GLU GLY THR VAL
SEQRES 7 B 409 GLU LYS ILE ASP ALA LYS SER SER MET VAL TYR TYR THR
SEQRES 8 B 409 LYS PRO ASP GLY SER MET ALA GLU GLU GLU TYR ASP TYR
SEQRES 9 B 409 VAL ILE VAL GLY ILE GLY ALA HIS LEU ALA THR GLU LEU
SEQRES 10 B 409 VAL LYS GLY TRP ASP LYS TYR GLY TYR SER VAL CYS GLU
SEQRES 11 B 409 PRO GLU PHE ALA THR LYS LEU ARG GLU LYS LEU GLU SER
SEQRES 12 B 409 PHE GLN GLY GLY ASN ILE ALA ILE GLY SER GLY PRO PHE
SEQRES 13 B 409 TYR GLN GLY HIS ASN PRO LYS PRO LYS VAL PRO GLU ASN
SEQRES 14 B 409 PHE VAL PRO ASN ALA ASP SER ALA CYS GLU GLY PRO VAL
SEQRES 15 B 409 PHE GLU MET SER LEU MET LEU HIS GLY TYR PHE LYS LYS
SEQRES 16 B 409 LYS GLY MET LEU ASP LYS VAL HIS VAL THR VAL PHE SER
SEQRES 17 B 409 PRO GLY GLU TYR LEU SER ASP LEU SER PRO ASN SER ARG
SEQRES 18 B 409 LYS ALA VAL ALA SER ILE TYR ASN GLN LEU GLY ILE LYS
SEQRES 19 B 409 LEU VAL HIS ASN PHE LYS ILE LYS GLU ILE ARG GLU HIS
SEQRES 20 B 409 GLU ILE VAL ASP GLU LYS GLY ASN THR ILE PRO ALA ASP
SEQRES 21 B 409 ILE THR ILE LEU LEU PRO PRO TYR THR GLY ASN PRO ALA
SEQRES 22 B 409 LEU LYS ASN SER THR PRO ASP LEU VAL ASP ASP GLY GLY
SEQRES 23 B 409 PHE ILE PRO THR ASP LEU ASN MET VAL SER ILE LYS TYR
SEQRES 24 B 409 ASP ASN VAL TYR ALA VAL GLY ASP ALA ASN SER MET THR
SEQRES 25 B 409 VAL PRO LYS LEU GLY TYR LEU ALA VAL MET THR GLY ARG
SEQRES 26 B 409 ILE ALA ALA GLN HIS LEU ALA ASN ARG LEU GLY VAL PRO
SEQRES 27 B 409 THR LYS VAL ASP LYS TYR TYR PRO THR ILE VAL CYS VAL
SEQRES 28 B 409 ALA ASP ASN PRO TYR GLU GLY TYR ALA VAL SER VAL LYS
SEQRES 29 B 409 ASP ASP THR TRP TYR GLY GLY THR VAL SER ILE ALA ASP
SEQRES 30 B 409 PRO ALA ALA VAL ASN HIS LEU LYS LYS GLU LEU PHE THR
SEQRES 31 B 409 LYS TYR TYR MET TRP THR LYS GLY ASP MET ALA LEU GLU
SEQRES 32 B 409 LYS PHE LEU ALA SER TRP
HET FAD A1001 53
HET S3H A1002 3
HET PO4 A2001 5
HET PO4 A2002 5
HET PO4 A2003 5
HET PO4 A 410 5
HET PO4 B2003 5
HET FAD B1001 53
HET S3H B1002 3
HET PO4 B2001 5
HET PO4 B2002 5
HET PO4 B 410 5
HET PO4 B 411 5
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM S3H TRISULFANE
HETNAM PO4 PHOSPHATE ION
FORMUL 3 FAD 2(C27 H33 N9 O15 P2)
FORMUL 4 S3H 2(H2 S3)
FORMUL 5 PO4 9(O4 P 3-)
FORMUL 16 HOH *267(H2 O)
HELIX 1 1 ARG A 10 GLY A 25 1 16
HELIX 2 2 SER A 26 ALA A 28 5 3
HELIX 3 3 LEU A 62 LEU A 66 1 5
HELIX 4 4 PRO A 67 GLY A 70 5 4
HELIX 5 5 THR A 115 VAL A 118 5 4
HELIX 6 6 GLY A 120 GLY A 125 1 6
HELIX 7 7 GLU A 132 PHE A 144 1 13
HELIX 8 8 GLU A 179 LYS A 195 1 17
HELIX 9 9 SER A 217 GLY A 232 1 16
HELIX 10 10 ASN A 271 ASN A 276 1 6
HELIX 11 11 THR A 278 VAL A 282 5 5
HELIX 12 12 GLY A 306 ASN A 309 5 4
HELIX 13 13 LEU A 316 LEU A 335 1 20
HELIX 14 14 CYS A 350 ASN A 354 5 5
HELIX 15 15 ARG B 10 GLY B 25 1 16
HELIX 16 16 SER B 26 ALA B 28 5 3
HELIX 17 17 LEU B 62 LEU B 66 1 5
HELIX 18 18 PRO B 67 GLY B 70 5 4
HELIX 19 19 THR B 115 VAL B 118 5 4
HELIX 20 20 GLY B 120 GLY B 125 1 6
HELIX 21 21 GLU B 132 PHE B 144 1 13
HELIX 22 22 GLU B 179 LYS B 196 1 18
HELIX 23 23 SER B 217 GLY B 232 1 16
HELIX 24 24 ASN B 271 ASN B 276 1 6
HELIX 25 25 GLY B 306 ASN B 309 5 4
HELIX 26 26 LEU B 316 LEU B 335 1 20
HELIX 27 27 CYS B 350 ASN B 354 5 5
SHEET 1 A 5 GLN A 72 GLU A 75 0
SHEET 2 A 5 ASP A 29 ASN A 34 1 N VAL A 32 O GLN A 74
SHEET 3 A 5 LYS A 3 LEU A 7 1 N VAL A 4 O ASP A 29
SHEET 4 A 5 TYR A 104 VAL A 107 1 O ILE A 106 N LEU A 7
SHEET 5 A 5 VAL A 302 ALA A 304 1 O TYR A 303 N VAL A 107
SHEET 1 B 2 PHE A 38 PHE A 41 0
SHEET 2 B 2 LEU A 58 ASP A 61 -1 O VAL A 60 N SER A 39
SHEET 1 C 3 THR A 77 ASP A 82 0
SHEET 2 C 3 MET A 87 THR A 91 -1 O MET A 87 N ASP A 82
SHEET 3 C 3 MET A 97 GLU A 101 -1 O ALA A 98 N TYR A 90
SHEET 1 D 2 HIS A 112 LEU A 113 0
SHEET 2 D 2 TYR A 268 THR A 269 -1 O THR A 269 N HIS A 112
SHEET 1 E 5 TYR A 126 SER A 127 0
SHEET 2 E 5 ILE A 261 LEU A 265 1 O LEU A 264 N TYR A 126
SHEET 3 E 5 GLY A 147 SER A 153 1 N ALA A 150 O ILE A 263
SHEET 4 E 5 VAL A 202 PHE A 207 1 O HIS A 203 N GLY A 147
SHEET 5 E 5 LYS A 234 VAL A 236 1 O LYS A 234 N VAL A 206
SHEET 1 F 3 ILE A 241 ILE A 244 0
SHEET 2 F 3 GLU A 248 ASP A 251 -1 O VAL A 250 N LYS A 242
SHEET 3 F 3 THR A 256 PRO A 258 -1 O ILE A 257 N ILE A 249
SHEET 1 G 5 GLN B 72 GLU B 75 0
SHEET 2 G 5 ASP B 29 ASN B 34 1 N VAL B 32 O GLN B 74
SHEET 3 G 5 LYS B 3 LEU B 7 1 N VAL B 4 O ASP B 29
SHEET 4 G 5 TYR B 104 VAL B 107 1 O ILE B 106 N LEU B 7
SHEET 5 G 5 VAL B 302 ALA B 304 1 O TYR B 303 N VAL B 107
SHEET 1 H 2 PHE B 38 PHE B 41 0
SHEET 2 H 2 LEU B 58 ASP B 61 -1 O VAL B 60 N SER B 39
SHEET 1 I 3 THR B 77 ASP B 82 0
SHEET 2 I 3 MET B 87 THR B 91 -1 O MET B 87 N ASP B 82
SHEET 3 I 3 MET B 97 GLU B 101 -1 O GLU B 100 N VAL B 88
SHEET 1 J 2 HIS B 112 LEU B 113 0
SHEET 2 J 2 TYR B 268 THR B 269 -1 O THR B 269 N HIS B 112
SHEET 1 K 5 TYR B 126 SER B 127 0
SHEET 2 K 5 ILE B 261 LEU B 265 1 O LEU B 264 N TYR B 126
SHEET 3 K 5 GLY B 147 SER B 153 1 N ALA B 150 O ILE B 263
SHEET 4 K 5 VAL B 202 PHE B 207 1 O HIS B 203 N ILE B 149
SHEET 5 K 5 LYS B 234 VAL B 236 1 O LYS B 234 N VAL B 206
SHEET 1 L 3 ILE B 241 ILE B 244 0
SHEET 2 L 3 GLU B 248 ASP B 251 -1 O VAL B 250 N LYS B 242
SHEET 3 L 3 THR B 256 PRO B 258 -1 O ILE B 257 N ILE B 249
LINK SG CYS A 129 C8M FAD A1001 1555 1555 1.53
LINK SG CYS B 129 C8M FAD B1001 1555 1555 1.54
LINK SG CYS A 178 S1 S3H A1002 1555 1555 1.95
LINK SG CYS B 178 S1 S3H B1002 1555 1555 1.96
LINK SG BCYS A 350 S3 S3H A1002 1555 1555 2.09
LINK SG BCYS B 350 S3 S3H B1002 1555 1555 2.11
CISPEP 1 ASN A 161 PRO A 162 0 -2.34
CISPEP 2 VAL A 313 PRO A 314 0 1.17
CISPEP 3 ASN B 161 PRO B 162 0 -1.90
CISPEP 4 VAL B 313 PRO B 314 0 -0.70
SITE 1 AC1 28 GLY A 8 GLY A 9 ARG A 10 PHE A 11
SITE 2 AC1 28 GLY A 12 ASN A 34 LYS A 35 ALA A 44
SITE 3 AC1 28 GLY A 76 THR A 77 VAL A 78 GLY A 108
SITE 4 AC1 28 ILE A 109 CYS A 129 PRO A 181 ASN A 271
SITE 5 AC1 28 GLY A 306 ASP A 307 LYS A 315 LEU A 316
SITE 6 AC1 28 GLY A 317 TYR A 318 HOH A 411 HOH A 412
SITE 7 AC1 28 HOH A 419 HOH A 426 HOH A 469 PO4 A2003
SITE 1 AC2 5 CYS A 178 LYS A 315 LEU A 316 CYS A 350
SITE 2 AC2 5 HOH A 550
SITE 1 AC3 5 SER A 36 ARG A 37 GLU A 75 HOH A 521
SITE 2 AC3 5 HOH A 535
SITE 1 AC4 5 HIS A 190 LYS A 194 HOH A 525 LYS B 343
SITE 2 AC4 5 HOH B 476
SITE 1 AC5 10 LYS A 35 ALA A 111 HIS A 112 ASN A 271
SITE 2 AC5 10 PRO A 272 HOH A 426 HOH A 467 HOH A 488
SITE 3 AC5 10 HOH A 531 FAD A1001
SITE 1 AC6 5 PRO A 155 TYR A 157 LYS A 240 HOH A 477
SITE 2 AC6 5 HOH A 482
SITE 1 AC7 8 ALA B 111 HIS B 112 PRO B 272 HOH B 425
SITE 2 AC7 8 HOH B 465 HOH B 488 HOH B 501 FAD B1001
SITE 1 AC8 29 GLY B 8 GLY B 9 ARG B 10 PHE B 11
SITE 2 AC8 29 GLY B 12 ASN B 34 LYS B 35 ALA B 44
SITE 3 AC8 29 GLY B 76 THR B 77 VAL B 78 GLY B 108
SITE 4 AC8 29 ILE B 109 CYS B 129 PRO B 181 ASN B 271
SITE 5 AC8 29 GLY B 306 ASP B 307 LYS B 315 LEU B 316
SITE 6 AC8 29 GLY B 317 TYR B 318 HOH B 412 HOH B 413
SITE 7 AC8 29 HOH B 422 HOH B 436 HOH B 441 HOH B 465
SITE 8 AC8 29 PO4 B2003
SITE 1 AC9 4 CYS B 178 LYS B 315 LEU B 316 CYS B 350
SITE 1 BC1 4 SER B 36 ARG B 37 GLU B 75 HOH B 460
SITE 1 BC2 4 HIS B 190 LYS B 194 HOH B 487 HOH B 510
SITE 1 BC3 5 LYS A 3 GLN A 72 GLU B 99 HOH B 444
SITE 2 BC3 5 HOH B 489
SITE 1 BC4 6 TYR A 89 GLU A 99 LYS B 92 ASP B 94
SITE 2 BC4 6 SER B 96 HOH B 477
CRYST1 179.657 179.657 163.397 90.00 90.00 120.00 P 65 2 2 24
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 0.005566 0.003214 0.000000 0.00000
SCALE2 0.000000 0.006427 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006120 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
