HEADER OXIDOREDUCTASE 14-JUL-11 3SX6
TITLE CRYSTAL STRUCTURE OF SULFIDE:QUINONE OXIDOREDUCTASE CYS356ALA VARIANT
TITLE 2 FROM ACIDITHIOBACILLUS FERROOXIDANS COMPLEXED WITH DECYLUBIQUINONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SULFIDE-QUINONE REDUCTASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SQR,SULFIDE:QUINONE OXIDOREDUCTASE;
COMPND 5 EC: 1.8.5.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACIDITHIOBACILLUS FERROOXIDANS ATCC 23270;
SOURCE 3 ORGANISM_TAXID: 243159;
SOURCE 4 STRAIN: ATCC 23270 / DSM 14882 / NCIB 8455;
SOURCE 5 GENE: AFE_1792;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SULFIDE:QUINONE OXIDOREDUCTASE, CYS356ALA VARIANT, INTEGRAL MONOTOPIC
KEYWDS 2 MEMBRANE PROTEIN, COMPLEX WITH SULFIDE AND DECYLUBIQUINONE,
KEYWDS 3 OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.M.CHERNEY,Y.ZHANG,M.N.G.JAMES,J.H.WEINER
REVDAT 3 27-MAR-24 3SX6 1 COMPND SOURCE REMARK DBREF
REVDAT 3 2 1 SEQADV SEQRES HET HETNAM
REVDAT 3 3 1 FORMUL LINK SITE ATOM
REVDAT 2 13-JUN-12 3SX6 1 JRNL
REVDAT 1 16-MAY-12 3SX6 0
JRNL AUTH M.M.CHERNEY,Y.ZHANG,M.N.JAMES,J.H.WEINER
JRNL TITL STRUCTURE-ACTIVITY CHARACTERIZATION OF SULFIDE:QUINONE
JRNL TITL 2 OXIDOREDUCTASE VARIANTS.
JRNL REF J.STRUCT.BIOL. V. 178 319 2012
JRNL REFN ISSN 1047-8477
JRNL PMID 22542586
JRNL DOI 10.1016/J.JSB.2012.04.007
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7_650)
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.14
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 46540
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.179
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.110
REMARK 3 FREE R VALUE TEST SET COUNT : 2376
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 30.1440 - 4.6116 0.97 2999 143 0.1618 0.1823
REMARK 3 2 4.6116 - 3.6624 0.98 2842 170 0.1347 0.1554
REMARK 3 3 3.6624 - 3.2001 0.99 2823 160 0.1682 0.2254
REMARK 3 4 3.2001 - 2.9077 0.99 2825 146 0.1971 0.2407
REMARK 3 5 2.9077 - 2.6995 0.99 2803 144 0.2058 0.2352
REMARK 3 6 2.6995 - 2.5404 0.99 2817 131 0.2009 0.2505
REMARK 3 7 2.5404 - 2.4132 1.00 2803 164 0.1957 0.2731
REMARK 3 8 2.4132 - 2.3082 1.00 2804 144 0.1879 0.2698
REMARK 3 9 2.3082 - 2.2194 0.99 2766 171 0.1909 0.2370
REMARK 3 10 2.2194 - 2.1428 0.99 2748 140 0.1899 0.2707
REMARK 3 11 2.1428 - 2.0758 0.97 2700 147 0.1911 0.2696
REMARK 3 12 2.0758 - 2.0165 0.94 2615 144 0.1990 0.2149
REMARK 3 13 2.0165 - 1.9634 0.90 2505 142 0.1988 0.2352
REMARK 3 14 1.9634 - 1.9156 0.85 2384 114 0.2139 0.2460
REMARK 3 15 1.9156 - 1.8720 0.78 2186 101 0.2446 0.3276
REMARK 3 16 1.8720 - 1.8322 0.69 1917 114 0.2864 0.3727
REMARK 3 17 1.8322 - 1.7955 0.59 1627 101 0.3247 0.3518
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 44.24
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.600
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) : -6.12120
REMARK 3 B22 (A**2) : -6.12120
REMARK 3 B33 (A**2) : 12.24230
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 : 0.006 3456
REMARK 3 ANGLE : 1.078 4688
REMARK 3 CHIRALITY : 0.076 504
REMARK 3 PLANARITY : 0.008 589
REMARK 3 DIHEDRAL : 20.593 1313
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 1:161)
REMARK 3 ORIGIN FOR THE GROUP (A): 40.5840 -26.7760 12.1828
REMARK 3 T TENSOR
REMARK 3 T11: 0.2346 T22: 0.3047
REMARK 3 T33: 0.1836 T12: -0.0660
REMARK 3 T13: 0.0349 T23: 0.0274
REMARK 3 L TENSOR
REMARK 3 L11: 0.5461 L22: 1.6119
REMARK 3 L33: 0.2914 L12: 0.6045
REMARK 3 L13: -0.2041 L23: -0.3266
REMARK 3 S TENSOR
REMARK 3 S11: 0.0624 S12: -0.1325 S13: -0.0857
REMARK 3 S21: 0.3068 S22: -0.0556 S23: 0.1755
REMARK 3 S31: 0.0303 S32: -0.1562 S33: -0.0115
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 162:232)
REMARK 3 ORIGIN FOR THE GROUP (A): 64.4777 -17.1586 6.2074
REMARK 3 T TENSOR
REMARK 3 T11: 0.1998 T22: 0.2161
REMARK 3 T33: 0.3858 T12: -0.0339
REMARK 3 T13: -0.0479 T23: 0.0480
REMARK 3 L TENSOR
REMARK 3 L11: 0.7048 L22: 1.1121
REMARK 3 L33: 0.2051 L12: 0.3109
REMARK 3 L13: -0.2808 L23: -0.1383
REMARK 3 S TENSOR
REMARK 3 S11: 0.0976 S12: -0.0595 S13: -0.0464
REMARK 3 S21: 0.0161 S22: -0.2009 S23: -0.6700
REMARK 3 S31: -0.0479 S32: 0.1390 S33: 0.0261
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 233:341)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.5926 -25.8538 -2.5480
REMARK 3 T TENSOR
REMARK 3 T11: 0.2167 T22: 0.2830
REMARK 3 T33: 0.1657 T12: -0.0493
REMARK 3 T13: -0.0033 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 0.5055 L22: 1.4912
REMARK 3 L33: 0.4488 L12: 0.7270
REMARK 3 L13: -0.3655 L23: -0.5138
REMARK 3 S TENSOR
REMARK 3 S11: -0.0517 S12: 0.1739 S13: -0.0660
REMARK 3 S21: -0.2062 S22: 0.0719 S23: -0.0612
REMARK 3 S31: 0.1874 S32: -0.1583 S33: 0.0042
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 342:377)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.4886 -10.2781 -1.9944
REMARK 3 T TENSOR
REMARK 3 T11: 0.2475 T22: 0.3165
REMARK 3 T33: 0.2512 T12: -0.0192
REMARK 3 T13: -0.0160 T23: 0.0311
REMARK 3 L TENSOR
REMARK 3 L11: 0.6349 L22: 1.6406
REMARK 3 L33: 0.3510 L12: 0.6005
REMARK 3 L13: -0.0587 L23: -0.4376
REMARK 3 S TENSOR
REMARK 3 S11: 0.0217 S12: -0.0911 S13: 0.0962
REMARK 3 S21: -0.1004 S22: 0.1678 S23: 0.2228
REMARK 3 S31: 0.0039 S32: -0.3123 S33: -0.0297
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 378:410)
REMARK 3 ORIGIN FOR THE GROUP (A): 42.1319 -7.2394 11.6927
REMARK 3 T TENSOR
REMARK 3 T11: 0.3226 T22: 0.3057
REMARK 3 T33: 0.3026 T12: 0.0011
REMARK 3 T13: 0.0867 T23: -0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.7355 L22: 1.0252
REMARK 3 L33: 0.5379 L12: 0.6578
REMARK 3 L13: -0.6106 L23: -0.5731
REMARK 3 S TENSOR
REMARK 3 S11: 0.0774 S12: -0.0773 S13: 0.2586
REMARK 3 S21: 0.3862 S22: 0.0148 S23: 0.2096
REMARK 3 S31: -0.0837 S32: -0.0857 S33: -0.0711
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 3SX6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1000066763.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949
REMARK 200 MONOCHROMATOR : DCM, SI(111) CRYO-COOLED FIRST
REMARK 200 CRYSTAL AND SAGITTALLY BENT
REMARK 200 SECOND
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : XDS, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 46610
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.796
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.2
REMARK 200 DATA REDUNDANCY : 11.80
REMARK 200 R MERGE (I) : 0.06700
REMARK 200 R SYM (I) : 0.06700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.86
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.5
REMARK 200 DATA REDUNDANCY IN SHELL : 8.60
REMARK 200 R MERGE FOR SHELL (I) : 0.74900
REMARK 200 R SYM FOR SHELL (I) : 0.74900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.830
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX 1.7_650
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 600, 0.1 M BIS-TRIS BUFFER,0.1
REMARK 280 M MGSO4, 0.05% DDM, 2 MM DECYLUBIQUINONE, PH 5.5, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 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
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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+2/3
REMARK 290 11555 -X+Y,Y,-Z
REMARK 290 12555 X,X-Y,-Z+1/3
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 54.34200
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 27.17100
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 54.34200
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 27.17100
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 54.34200
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 27.17100
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 54.34200
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 0.00000
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 27.17100
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: 8590 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -114.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 567 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 629 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 632 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 671 LIES ON A SPECIAL POSITION.
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 419
REMARK 465 GLY A 420
REMARK 465 ILE A 421
REMARK 465 THR A 422
REMARK 465 ARG A 423
REMARK 465 LEU A 424
REMARK 465 LYS A 425
REMARK 465 GLU A 426
REMARK 465 GLU A 427
REMARK 465 ASP A 428
REMARK 465 THR A 429
REMARK 465 HIS A 430
REMARK 465 ARG A 431
REMARK 465 LYS A 432
REMARK 465 ALA A 433
REMARK 465 SER A 434
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 SER A 1 56.68 -148.65
REMARK 500 ALA A 9 65.45 -111.35
REMARK 500 ASP A 206 43.66 -99.45
REMARK 500 PRO A 371 -153.82 -79.24
REMARK 500 SER A 407 -56.43 -163.17
REMARK 500 GLU A 408 164.30 -47.36
REMARK 500 PHE A 410 -26.91 126.28
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 646 DISTANCE = 8.13 ANGSTROMS
REMARK 525 HOH A 712 DISTANCE = 5.88 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 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DCQ A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S A 508
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3KPG RELATED DB: PDB
REMARK 900 RELATED ID: 3KPI RELATED DB: PDB
REMARK 900 RELATED ID: 3KPK RELATED DB: PDB
REMARK 900 RELATED ID: 3SXI RELATED DB: PDB
REMARK 900 RELATED ID: 3SY4 RELATED DB: PDB
REMARK 900 RELATED ID: 3SYI RELATED DB: PDB
REMARK 900 RELATED ID: 3SZ0 RELATED DB: PDB
REMARK 900 RELATED ID: 3SZC RELATED DB: PDB
REMARK 900 RELATED ID: 3SZF RELATED DB: PDB
DBREF 3SX6 A 2 434 UNP B7JBP8 SQRD_ACIF2 2 434
SEQADV 3SX6 MET A -2 UNP B7JBP8 INITIATING METHIONINE
SEQADV 3SX6 ARG A -1 UNP B7JBP8 EXPRESSION TAG
SEQADV 3SX6 GLY A 0 UNP B7JBP8 EXPRESSION TAG
SEQADV 3SX6 SER A 1 UNP B7JBP8 EXPRESSION TAG
SEQADV 3SX6 ALA A 356 UNP B7JBP8 CYS 356 ENGINEERED MUTATION
SEQRES 1 A 437 MET ARG GLY SER ALA HIS VAL VAL ILE LEU GLY ALA GLY
SEQRES 2 A 437 THR GLY GLY MET PRO ALA ALA TYR GLU MET LYS GLU ALA
SEQRES 3 A 437 LEU GLY SER GLY HIS GLU VAL THR LEU ILE SER ALA ASN
SEQRES 4 A 437 ASP TYR PHE GLN PHE VAL PRO SER ASN PRO TRP VAL GLY
SEQRES 5 A 437 VAL GLY TRP LYS GLU ARG ASP ASP ILE ALA PHE PRO ILE
SEQRES 6 A 437 ARG HIS TYR VAL GLU ARG LYS GLY ILE HIS PHE ILE ALA
SEQRES 7 A 437 GLN SER ALA GLU GLN ILE ASP ALA GLU ALA GLN ASN ILE
SEQRES 8 A 437 THR LEU ALA ASP GLY ASN THR VAL HIS TYR ASP TYR LEU
SEQRES 9 A 437 MET ILE ALA THR GLY PRO LYS LEU ALA PHE GLU ASN VAL
SEQRES 10 A 437 PRO GLY SER ASP PRO HIS GLU GLY PRO VAL GLN SER ILE
SEQRES 11 A 437 CYS THR VAL ASP HIS ALA GLU ARG ALA PHE ALA GLU TYR
SEQRES 12 A 437 GLN ALA LEU LEU ARG GLU PRO GLY PRO ILE VAL ILE GLY
SEQRES 13 A 437 ALA MET ALA GLY ALA SER TSY PHE GLY PRO ALA TYR GLU
SEQRES 14 A 437 TYR ALA MET ILE VAL ALA SER ASP LEU LYS LYS ARG GLY
SEQRES 15 A 437 MET ARG ASP LYS ILE PRO SER PHE THR PHE ILE THR SER
SEQRES 16 A 437 GLU PRO TYR ILE GLY HIS LEU GLY ILE GLN GLY VAL GLY
SEQRES 17 A 437 ASP SER LYS GLY ILE LEU THR LYS GLY LEU LYS GLU GLU
SEQRES 18 A 437 GLY ILE GLU ALA TYR THR ASN CYS LYS VAL THR LYS VAL
SEQRES 19 A 437 GLU ASP ASN LYS MET TYR VAL THR GLN VAL ASP GLU LYS
SEQRES 20 A 437 GLY GLU THR ILE LYS GLU MET VAL LEU PRO VAL LYS PHE
SEQRES 21 A 437 GLY MET MET ILE PRO ALA PHE LYS GLY VAL PRO ALA VAL
SEQRES 22 A 437 ALA GLY VAL GLU GLY LEU CYS ASN PRO GLY GLY PHE VAL
SEQRES 23 A 437 LEU VAL ASP GLU HIS GLN ARG SER LYS LYS TYR ALA ASN
SEQRES 24 A 437 ILE PHE ALA ALA GLY ILE ALA ILE ALA ILE PRO PRO VAL
SEQRES 25 A 437 GLU THR THR PRO VAL PRO THR GLY ALA PRO LYS THR GLY
SEQRES 26 A 437 TYR MET ILE GLU SER MET VAL SER ALA ALA VAL HIS ASN
SEQRES 27 A 437 ILE LYS ALA ASP LEU GLU GLY ARG LYS GLY GLU GLN THR
SEQRES 28 A 437 MET GLY THR TRP ASN ALA VAL ALA PHE ALA ASP MET GLY
SEQRES 29 A 437 ASP ARG GLY ALA ALA PHE ILE ALA LEU PRO GLN LEU LYS
SEQRES 30 A 437 PRO ARG LYS VAL ASP VAL PHE ALA TYR GLY ARG TRP VAL
SEQRES 31 A 437 HIS LEU ALA LYS VAL ALA PHE GLU LYS TYR PHE ILE ARG
SEQRES 32 A 437 LYS MET LYS MET GLY VAL SER GLU PRO PHE TYR GLU LYS
SEQRES 33 A 437 VAL LEU PHE LYS MET MET GLY ILE THR ARG LEU LYS GLU
SEQRES 34 A 437 GLU ASP THR HIS ARG LYS ALA SER
MODRES 3SX6 TSY A 160 CYS MODIFIED RESIDUE
HET TSY A 160 8
HET FAD A 500 53
HET LMT A 501 35
HET DCQ A 502 23
HET SO4 A 503 5
HET SO4 A 504 5
HET H2S A 505 1
HET H2S A 508 1
HETNAM TSY (2S)-2-AMINO-3-TRISULFANYLPROPANOIC ACID
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM LMT DODECYL-BETA-D-MALTOSIDE
HETNAM DCQ 2-DECYL-5,6-DIMETHOXY-3-METHYLCYCLOHEXA-2,5-DIENE-1,4-
HETNAM 2 DCQ DIONE
HETNAM SO4 SULFATE ION
HETNAM H2S HYDROSULFURIC ACID
HETSYN DCQ DECYLUBIQUINONE
HETSYN H2S HYDROGEN SULFIDE
FORMUL 1 TSY C3 H7 N O2 S3
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 LMT C24 H46 O11
FORMUL 4 DCQ C19 H30 O4
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 H2S 2(H2 S)
FORMUL 9 HOH *341(H2 O)
HELIX 1 1 GLY A 12 GLY A 25 1 14
HELIX 2 2 SER A 26 HIS A 28 5 3
HELIX 3 3 SER A 44 VAL A 50 1 7
HELIX 4 4 GLU A 54 ILE A 58 1 5
HELIX 5 5 ILE A 62 ARG A 68 1 7
HELIX 6 6 PHE A 111 VAL A 114 5 4
HELIX 7 7 THR A 129 GLU A 146 1 18
HELIX 8 8 PHE A 161 ARG A 178 1 18
HELIX 9 9 MET A 180 ILE A 184 5 5
HELIX 10 10 ASP A 206 GLU A 218 1 13
HELIX 11 11 VAL A 267 GLY A 272 1 6
HELIX 12 12 GLY A 301 ILE A 304 5 4
HELIX 13 13 THR A 321 LEU A 340 1 20
HELIX 14 14 ARG A 385 GLY A 405 1 21
HELIX 15 15 GLU A 412 LYS A 417 1 6
SHEET 1 A 5 HIS A 72 ILE A 74 0
SHEET 2 A 5 GLU A 29 ILE A 33 1 N LEU A 32 O HIS A 72
SHEET 3 A 5 HIS A 3 LEU A 7 1 N ILE A 6 O THR A 31
SHEET 4 A 5 TYR A 100 ILE A 103 1 O MET A 102 N VAL A 5
SHEET 5 A 5 ILE A 297 ALA A 299 1 O PHE A 298 N LEU A 101
SHEET 1 B 2 TYR A 38 GLN A 40 0
SHEET 2 B 2 ALA A 59 PRO A 61 -1 O PHE A 60 N PHE A 39
SHEET 1 C 3 ALA A 78 ASP A 82 0
SHEET 2 C 3 ASN A 87 LEU A 90 -1 O THR A 89 N GLU A 79
SHEET 3 C 3 THR A 95 HIS A 97 -1 O VAL A 96 N ILE A 88
SHEET 1 D 2 LYS A 108 LEU A 109 0
SHEET 2 D 2 PHE A 264 LYS A 265 -1 O LYS A 265 N LYS A 108
SHEET 1 E 5 VAL A 124 GLN A 125 0
SHEET 2 E 5 PHE A 257 ILE A 261 1 O GLY A 258 N GLN A 125
SHEET 3 E 5 ILE A 150 ALA A 154 1 N GLY A 153 O ILE A 261
SHEET 4 E 5 PHE A 187 THR A 191 1 O THR A 188 N ILE A 152
SHEET 5 E 5 GLU A 221 TYR A 223 1 O GLU A 221 N PHE A 189
SHEET 1 F 3 CYS A 226 GLU A 232 0
SHEET 2 F 3 LYS A 235 VAL A 241 -1 O THR A 239 N LYS A 227
SHEET 3 F 3 THR A 247 PRO A 254 -1 O LYS A 249 N GLN A 240
SHEET 1 G 3 ALA A 354 ASP A 359 0
SHEET 2 G 3 GLY A 364 LEU A 370 -1 O ALA A 365 N ALA A 358
SHEET 3 G 3 VAL A 378 GLY A 384 -1 O ALA A 382 N ALA A 366
LINK C SER A 159 N TSY A 160 1555 1555 1.33
LINK C TSY A 160 N PHE A 161 1555 1555 1.33
CISPEP 1 LEU A 370 PRO A 371 0 -5.70
CISPEP 2 LYS A 374 PRO A 375 0 -0.41
SITE 1 AC1 36 LEU A 7 GLY A 8 ALA A 9 GLY A 10
SITE 2 AC1 36 THR A 11 GLY A 12 SER A 34 ALA A 35
SITE 3 AC1 36 VAL A 42 SER A 77 ALA A 78 ALA A 104
SITE 4 AC1 36 THR A 105 GLY A 106 PRO A 107 PRO A 163
SITE 5 AC1 36 GLY A 301 ILE A 302 LYS A 320 THR A 321
SITE 6 AC1 36 GLY A 322 ILE A 325 VAL A 355 PHE A 357
SITE 7 AC1 36 HOH A 435 HOH A 436 HOH A 461 HOH A 489
SITE 8 AC1 36 DCQ A 502 HOH A 510 HOH A 546 HOH A 625
SITE 9 AC1 36 HOH A 645 HOH A 651 HOH A 764 HOH A 783
SITE 1 AC2 15 GLY A 205 ASP A 206 ILE A 210 ALA A 356
SITE 2 AC2 15 ALA A 358 ALA A 365 TYR A 383 HOH A 460
SITE 3 AC2 15 HOH A 462 HOH A 466 HOH A 468 HOH A 469
SITE 4 AC2 15 HOH A 473 SO4 A 504 HOH A 703
SITE 1 AC3 10 PRO A 43 GLY A 322 TYR A 323 PHE A 357
SITE 2 AC3 10 ILE A 368 PHE A 394 PHE A 398 TYR A 411
SITE 3 AC3 10 FAD A 500 HOH A 651
SITE 1 AC4 6 MET A -2 HIS A 3 HIS A 97 ASP A 99
SITE 2 AC4 6 HOH A 637 HOH A 774
SITE 1 AC5 7 ARG A 363 GLY A 384 ARG A 385 HOH A 462
SITE 2 AC5 7 LMT A 501 HOH A 542 HOH A 706
SITE 1 AC6 3 GLY A 162 HOH A 485 HOH A 527
SITE 1 AC8 2 H2S A 505 HOH A 783
SITE 1 AC9 5 LEU A 109 SER A 126 CYS A 128 THR A 129
SITE 2 AC9 5 HIS A 132
CRYST1 149.828 149.828 81.513 90.00 90.00 120.00 P 62 2 2 12
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 0.006674 0.003853 0.000000 0.00000
SCALE2 0.000000 0.007707 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012268 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
