HEADER OXIDOREDUCTASE 15-JUL-11 3SY4
TITLE CRYSTAL STRUCTURE OF SULFIDE:QUINONE OXIDOREDUCTASE SER126ALA VARIANT
TITLE 2 FROM ACIDITHIOBACILLUS FERROOXIDANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SULFIDE-QUINONE REDUCTASE, PUTATIVE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ACIDITHIOBACILLUS FERROOXIDANS;
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, SER126ALA VARIANT, INTEGRAL MONOTOPIC
KEYWDS 2 MEMBRANE PROTEIN, COMPLEX WITH SULFIDE, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR M.M.CHERNEY,Y.ZHANG,M.N.G.JAMES,J.H.WEINER
REVDAT 2 13-JUN-12 3SY4 1 JRNL
REVDAT 1 16-MAY-12 3SY4 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. 1.91 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 69.15
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.370
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.0
REMARK 3 NUMBER OF REFLECTIONS : 38487
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.180
REMARK 3 FREE R VALUE TEST SET COUNT : 3753
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 69.1922 - 5.7290 1.00 2792 166 0.1718 0.1789
REMARK 3 2 5.7290 - 4.5476 1.00 2795 141 0.1300 0.1832
REMARK 3 3 4.5476 - 3.9728 1.00 2827 138 0.1248 0.1636
REMARK 3 4 3.9728 - 3.6096 1.00 2820 134 0.1472 0.1958
REMARK 3 5 3.6096 - 3.3509 1.00 2786 156 0.1705 0.2065
REMARK 3 6 3.3509 - 3.1533 1.00 2781 156 0.1826 0.1767
REMARK 3 7 3.1533 - 2.9954 1.00 2762 181 0.1761 0.2464
REMARK 3 8 2.9954 - 2.8650 1.00 2813 150 0.1825 0.2482
REMARK 3 9 2.8650 - 2.7547 1.00 2796 153 0.1886 0.1951
REMARK 3 10 2.7547 - 2.6596 1.00 2810 125 0.1886 0.2506
REMARK 3 11 2.6596 - 2.5765 1.00 2790 149 0.1811 0.2212
REMARK 3 12 2.5765 - 2.5028 1.00 2823 141 0.1898 0.2447
REMARK 3 13 2.5028 - 2.4369 1.00 2788 141 0.1869 0.3057
REMARK 3 14 2.4369 - 2.3775 1.00 2804 156 0.2014 0.2330
REMARK 3 15 2.3775 - 2.3234 1.00 2806 156 0.1902 0.2436
REMARK 3 16 2.3234 - 2.2740 1.00 2712 189 0.1841 0.2081
REMARK 3 17 2.2740 - 2.2285 0.99 2790 158 0.1871 0.2325
REMARK 3 18 2.2285 - 2.1864 0.94 2635 128 0.1843 0.2997
REMARK 3 19 2.1864 - 2.1474 0.91 2568 138 0.2106 0.2756
REMARK 3 20 2.1474 - 2.1110 0.85 2372 126 0.2014 0.2639
REMARK 3 21 2.1110 - 2.0769 0.83 2309 154 0.2094 0.2903
REMARK 3 22 2.0769 - 2.0450 0.79 2201 120 0.2374 0.2886
REMARK 3 23 2.0450 - 2.0149 0.76 2134 116 0.2508 0.2422
REMARK 3 24 2.0149 - 1.9865 0.72 1999 118 0.2715 0.3515
REMARK 3 25 1.9865 - 1.9597 0.66 1825 118 0.2839 0.3551
REMARK 3 26 1.9597 - 1.9342 0.59 1674 75 0.3168 0.3595
REMARK 3 27 1.9342 - 1.9100 0.53 1508 70 0.3651 0.3180
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 49.40
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.630
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.690
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) : -4.15150
REMARK 3 B22 (A**2) : -4.15150
REMARK 3 B33 (A**2) : 8.30300
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 3405
REMARK 3 ANGLE : 1.159 4617
REMARK 3 CHIRALITY : 0.076 500
REMARK 3 PLANARITY : 0.005 584
REMARK 3 DIHEDRAL : 15.506 1249
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): 40.5699 -26.7855 12.2183
REMARK 3 T TENSOR
REMARK 3 T11: 0.2843 T22: 0.3497
REMARK 3 T33: 0.2070 T12: -0.0632
REMARK 3 T13: 0.0267 T23: 0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 1.8942 L22: 1.5057
REMARK 3 L33: 0.3416 L12: 0.6402
REMARK 3 L13: -0.2489 L23: -0.3297
REMARK 3 S TENSOR
REMARK 3 S11: 0.0901 S12: -0.1888 S13: -0.1166
REMARK 3 S21: 0.2730 S22: -0.0666 S23: -0.0035
REMARK 3 S31: -0.0041 S32: -0.1466 S33: -0.0059
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 162:232)
REMARK 3 ORIGIN FOR THE GROUP (A): 64.4161 -17.1429 6.1123
REMARK 3 T TENSOR
REMARK 3 T11: 0.2301 T22: 0.2381
REMARK 3 T33: 0.4741 T12: -0.0551
REMARK 3 T13: -0.0563 T23: 0.0681
REMARK 3 L TENSOR
REMARK 3 L11: 1.4602 L22: 1.7189
REMARK 3 L33: 0.8809 L12: 0.2001
REMARK 3 L13: -0.2041 L23: -0.7183
REMARK 3 S TENSOR
REMARK 3 S11: 0.0863 S12: -0.1701 S13: -0.0353
REMARK 3 S21: 0.1652 S22: -0.2334 S23: -0.7617
REMARK 3 S31: -0.1097 S32: 0.1408 S33: 0.0754
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resseq 233:341)
REMARK 3 ORIGIN FOR THE GROUP (A): 45.7479 -25.8907 -2.5476
REMARK 3 T TENSOR
REMARK 3 T11: 0.2430 T22: 0.3196
REMARK 3 T33: 0.2132 T12: -0.0423
REMARK 3 T13: 0.0341 T23: 0.0204
REMARK 3 L TENSOR
REMARK 3 L11: 1.9617 L22: 1.5211
REMARK 3 L33: 0.4387 L12: 0.6502
REMARK 3 L13: 0.0808 L23: -0.3749
REMARK 3 S TENSOR
REMARK 3 S11: -0.0525 S12: 0.2522 S13: -0.0428
REMARK 3 S21: -0.1732 S22: 0.0509 S23: -0.1525
REMARK 3 S31: 0.1246 S32: -0.1419 S33: -0.0083
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resseq 342:377)
REMARK 3 ORIGIN FOR THE GROUP (A): 43.6038 -10.3178 -1.9325
REMARK 3 T TENSOR
REMARK 3 T11: 0.1958 T22: 0.2457
REMARK 3 T33: 0.1905 T12: -0.0178
REMARK 3 T13: 0.0272 T23: 0.0436
REMARK 3 L TENSOR
REMARK 3 L11: 1.4995 L22: 2.0129
REMARK 3 L33: 1.2902 L12: 0.2519
REMARK 3 L13: -0.4572 L23: -0.4933
REMARK 3 S TENSOR
REMARK 3 S11: 0.1632 S12: 0.0305 S13: 0.2030
REMARK 3 S21: -0.0111 S22: 0.0732 S23: 0.1960
REMARK 3 S31: 0.0361 S32: -0.3171 S33: -0.1577
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resseq 378:410)
REMARK 3 ORIGIN FOR THE GROUP (A): 41.9843 -7.3784 11.4960
REMARK 3 T TENSOR
REMARK 3 T11: 0.3601 T22: 0.2648
REMARK 3 T33: 0.3373 T12: 0.0597
REMARK 3 T13: 0.1039 T23: 0.0347
REMARK 3 L TENSOR
REMARK 3 L11: 1.7228 L22: 1.2068
REMARK 3 L33: 1.6640 L12: 1.2954
REMARK 3 L13: -1.7692 L23: -0.9350
REMARK 3 S TENSOR
REMARK 3 S11: 0.0793 S12: 0.1106 S13: 0.6108
REMARK 3 S21: 0.4530 S22: 0.1692 S23: 0.3346
REMARK 3 S31: -0.0347 S32: -0.2819 S33: -0.0081
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 3SY4 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 RCSB ID CODE IS RCSB066796.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-FEB-10
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) : 0.9795
REMARK 200 MONOCHROMATOR : ACCEL/BRUKER DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR (DCM), FEATURING
REMARK 200 INDIRECTLY CRYO-COOLED FIRST
REMARK 200 CRYSTAL AND SAGITTALLY FOCUSING
REMARK 200 SECOND CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38487
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.910
REMARK 200 RESOLUTION RANGE LOW (A) : 81.600
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 200 DATA REDUNDANCY : 32.300
REMARK 200 R MERGE (I) : 0.08800
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 31.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.01
REMARK 200 COMPLETENESS FOR SHELL (%) : 64.7
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : 0.99200
REMARK 200 R SYM FOR SHELL (I) : 0.99200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.61
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, PH 5.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 54.48667
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 27.24333
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 54.48667
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 27.24333
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 54.48667
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 27.24333
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 54.48667
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 27.24333
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: 6070 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 34800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 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 -0.500000 -0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 -0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 27.24333
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 613 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 737 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 752 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: 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 PRO A 307 O HOH A 762 2.08
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 A 9 67.38 -111.77
REMARK 500 LYS A 177 -5.76 -59.83
REMARK 500 ASP A 206 44.48 -101.92
REMARK 500 PRO A 371 -153.28 -80.68
REMARK 500 SER A 407 -133.10 -155.28
REMARK 500 GLU A 408 -129.96 18.15
REMARK 500 PRO A 409 -134.64 -90.06
REMARK 500 TYR A 411 -125.04 53.04
REMARK 500 VAL A 414 26.86 -78.75
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 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 H2S A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S 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: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE H2S A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 507
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: 3SX6 RELATED DB: PDB
REMARK 900 RELATED ID: 3SXI 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 3SY4 A 2 434 UNP B7JBP8 B7JBP8_ACIF2 2 434
SEQADV 3SY4 MET A -2 UNP B7JBP8 EXPRESSION TAG
SEQADV 3SY4 ARG A -1 UNP B7JBP8 EXPRESSION TAG
SEQADV 3SY4 GLY A 0 UNP B7JBP8 EXPRESSION TAG
SEQADV 3SY4 SER A 1 UNP B7JBP8 EXPRESSION TAG
SEQADV 3SY4 ALA A 126 UNP B7JBP8 SER 126 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 ALA 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 CYS 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 CYS 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
HET FAD A 500 53
HET LMT A 501 35
HET H2S A 502 1
HET H2S A 503 1
HET H2S A 504 1
HET H2S A 505 1
HET H2S A 506 1
HET SO4 A 507 5
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM LMT DODECYL-BETA-D-MALTOSIDE
HETNAM H2S HYDROSULFURIC ACID
HETNAM SO4 SULFATE ION
HETSYN H2S HYDROGEN SULFIDE
FORMUL 2 FAD C27 H33 N9 O15 P2
FORMUL 3 LMT C24 H46 O11
FORMUL 4 H2S 5(H2 S)
FORMUL 9 SO4 O4 S 2-
FORMUL 10 HOH *294(H2 O)
HELIX 1 1 GLY A 12 GLY A 25 1 14
HELIX 2 2 SER A 44 VAL A 50 1 7
HELIX 3 3 GLU A 54 ILE A 58 1 5
HELIX 4 4 ILE A 62 ARG A 68 1 7
HELIX 5 5 PHE A 111 VAL A 114 5 4
HELIX 6 6 THR A 129 GLU A 146 1 18
HELIX 7 7 PHE A 161 LYS A 177 1 17
HELIX 8 8 MET A 180 ILE A 184 5 5
HELIX 9 9 ASP A 206 GLU A 218 1 13
HELIX 10 10 VAL A 267 GLY A 272 1 6
HELIX 11 11 GLY A 301 ILE A 304 5 4
HELIX 12 12 THR A 321 GLU A 341 1 21
HELIX 13 13 ARG A 385 GLY A 405 1 21
HELIX 14 14 LYS A 413 LYS A 417 5 5
SHEET 1 A 5 HIS A 72 ILE A 74 0
SHEET 2 A 5 VAL A 30 ILE A 33 1 N LEU A 32 O HIS A 72
SHEET 3 A 5 VAL A 4 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 LEU A 7
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 TYR A 237 N LYS A 230
SHEET 3 F 3 THR A 247 PRO A 254 -1 O LEU A 253 N MET A 236
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 SG ACYS A 356 S H2S A 505 1555 1555 2.15
LINK SG BCYS A 356 S H2S A 505 1555 1555 2.15
LINK SG CYS A 160 S H2S A 504 1555 1555 2.27
CISPEP 1 LEU A 370 PRO A 371 0 -2.60
CISPEP 2 LYS A 374 PRO A 375 0 1.79
SITE 1 AC1 42 LEU A 7 GLY A 8 ALA A 9 GLY A 10
SITE 2 AC1 42 THR A 11 GLY A 12 SER A 34 ALA A 35
SITE 3 AC1 42 ASN A 36 VAL A 42 PRO A 43 SER A 77
SITE 4 AC1 42 ALA A 78 ALA A 104 THR A 105 GLY A 106
SITE 5 AC1 42 PRO A 107 CYS A 160 PRO A 163 VAL A 267
SITE 6 AC1 42 GLY A 301 ILE A 302 LYS A 320 THR A 321
SITE 7 AC1 42 GLY A 322 ILE A 325 VAL A 355 PHE A 357
SITE 8 AC1 42 LYS A 391 H2S A 505 HOH A 508 HOH A 509
SITE 9 AC1 42 HOH A 530 HOH A 543 HOH A 560 HOH A 567
SITE 10 AC1 42 HOH A 612 HOH A 645 HOH A 700 HOH A 701
SITE 11 AC1 42 HOH A 792 HOH A 801
SITE 1 AC2 17 GLY A 162 MET A 169 GLY A 205 ASP A 206
SITE 2 AC2 17 ILE A 210 LEU A 211 GLU A 217 CYS A 356
SITE 3 AC2 17 ALA A 358 ALA A 365 PHE A 367 TYR A 383
SITE 4 AC2 17 HOH A 518 HOH A 562 HOH A 620 HOH A 672
SITE 5 AC2 17 HOH A 738
SITE 1 AC3 5 GLY A 162 CYS A 356 H2S A 504 H2S A 505
SITE 2 AC3 5 HOH A 706
SITE 1 AC4 5 LEU A 109 ALA A 126 CYS A 128 THR A 129
SITE 2 AC4 5 HIS A 132
SITE 1 AC5 3 CYS A 160 H2S A 502 H2S A 505
SITE 1 AC6 4 CYS A 356 FAD A 500 H2S A 502 H2S A 504
SITE 1 AC7 3 LYS A 374 PRO A 375 ARG A 376
SITE 1 AC8 4 MET A -2 HIS A 3 HIS A 97 HOH A 676
CRYST1 149.766 149.766 81.730 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 0.006677 0.003855 0.000000 0.00000
SCALE2 0.000000 0.007710 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012235 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
