HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10 3AE7
TITLE CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE 2 2-IODO-N-(3-ISOPROPOXY-PHENYL)-BENZAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT,
COMPND 3 MITOCHONDRIAL;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: FLAVOPROTEIN SUBUNIT OF COMPLEX II, FP;
COMPND 6 EC: 1.3.5.1;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: SUCCINATE DEHYDROGENASE [UBIQUINONE] IRON-SULFUR SUBUNIT,
COMPND 9 MITOCHONDRIAL;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: IRON-SULFUR SUBUNIT OF COMPLEX II, IP;
COMPND 12 EC: 1.3.5.1;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: SUCCINATE DEHYDROGENASE CYTOCHROME B560 SUBUNIT,
COMPND 15 MITOCHONDRIAL;
COMPND 16 CHAIN: C;
COMPND 17 SYNONYM: SUCCINATE-UBIQUINONE OXIDOREDUCTASE CYTOCHROME B LARGE
COMPND 18 SUBUNIT, CYBL;
COMPND 19 MOL_ID: 4;
COMPND 20 MOLECULE: SUCCINATE DEHYDROGENASE [UBIQUINONE] CYTOCHROME B SMALL
COMPND 21 SUBUNIT, MITOCHONDRIAL;
COMPND 22 CHAIN: D;
COMPND 23 FRAGMENT: RESIDUES 57-159;
COMPND 24 SYNONYM: SUCCINATE-UBIQUINONE OXIDOREDUCTASE CYTOCHROME B SMALL
COMPND 25 SUBUNIT, CYBS, SUCCINATE-UBIQUINONE REDUCTASE MEMBRANE ANCHOR
COMPND 26 SUBUNIT, QPS3, CII-4, SUCCINATE DEHYDROGENASE COMPLEX SUBUNIT D
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 ORGAN: HEART;
SOURCE 6 TISSUE: MUSCLE;
SOURCE 7 MOL_ID: 2;
SOURCE 8 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 9 ORGANISM_COMMON: PIG;
SOURCE 10 ORGANISM_TAXID: 9823;
SOURCE 11 ORGAN: HEART;
SOURCE 12 TISSUE: MUSCLE;
SOURCE 13 MOL_ID: 3;
SOURCE 14 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 15 ORGANISM_COMMON: PIG;
SOURCE 16 ORGANISM_TAXID: 9823;
SOURCE 17 ORGAN: HEART;
SOURCE 18 TISSUE: MUSCLE;
SOURCE 19 MOL_ID: 4;
SOURCE 20 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 21 ORGANISM_COMMON: PIG;
SOURCE 22 ORGANISM_TAXID: 9823;
SOURCE 23 ORGAN: HEART;
SOURCE 24 TISSUE: MUSCLE
KEYWDS RESPIRATORY COMPLEX II, INHIBITORS, ELECTRON TRANSPORT, IRON, IRON-
KEYWDS 2 SULFUR, METAL-BINDING, MITOCHONDRION, MITOCHONDRION INNER MEMBRANE,
KEYWDS 3 OXIDOREDUCTASE, TRANSIT PEPTIDE, TRANSPORT, TRICARBOXYLIC ACID
KEYWDS 4 CYCLE, HEME, TRANSMEMBRANE, FAD-BINDING PROTEIN, OXIDOREDUCTASE-
KEYWDS 5 OXIDOREDUCTASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HARADA,T.SASAKI,M.SHINDO,Y.KIDO,D.K.INAOKA,J.OMORI,A.OSANAI,
AUTHOR 2 K.SAKAMOTO,J.MAO,S.MATSUOKA,M.INOUE,T.HONMA,A.TANAKA,K.KITA
REVDAT 4 01-NOV-23 3AE7 1 REMARK LINK
REVDAT 3 11-OCT-17 3AE7 1 REMARK
REVDAT 2 05-AUG-15 3AE7 1 JRNL VERSN
REVDAT 1 09-FEB-11 3AE7 0
JRNL AUTH D.K.INAOKA,T.SHIBA,D.SATO,E.O.BALOGUN,T.SASAKI,M.NAGAHAMA,
JRNL AUTH 2 M.ODA,S.MATSUOKA,J.OHMORI,T.HONMA,M.INOUE,K.KITA,S.HARADA
JRNL TITL STRUCTURAL INSIGHTS INTO THE MOLECULAR DESIGN OF FLUTOLANIL
JRNL TITL 2 DERIVATIVES TARGETED FOR FUMARATE RESPIRATION OF PARASITE
JRNL TITL 3 MITOCHONDRIA
JRNL REF INT J MOL SCI V. 16 15287 2015
JRNL REFN ESSN 1422-0067
JRNL PMID 26198225
JRNL DOI 10.3390/IJMS160715287
REMARK 2
REMARK 2 RESOLUTION. 3.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.13
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.0
REMARK 3 NUMBER OF REFLECTIONS : 20118
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) : 0.259
REMARK 3 R VALUE (WORKING SET) : 0.256
REMARK 3 FREE R VALUE : 0.305
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1046
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) : 3.62
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.71
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1077
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.3800
REMARK 3 BIN FREE R VALUE SET COUNT : 68
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8480
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 135
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 145.1
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.42000
REMARK 3 B22 (A**2) : 0.62000
REMARK 3 B33 (A**2) : -1.04000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.765
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.587
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 81.032
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.906
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.860
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8821 ; 0.005 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11970 ; 0.844 ; 1.988
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1088 ; 3.872 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 375 ;33.189 ;23.413
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1469 ;14.857 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;12.043 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1304 ; 0.052 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6644 ; 0.002 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 5410 ; 0.087 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8675 ; 0.156 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3411 ; 0.069 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3278 ; 0.120 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 15
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 10 A 191
REMARK 3 ORIGIN FOR THE GROUP (A): 19.8520 -17.8930 -17.4100
REMARK 3 T TENSOR
REMARK 3 T11: 0.5536 T22: 0.5629
REMARK 3 T33: 0.8826 T12: 0.0686
REMARK 3 T13: 0.0294 T23: -0.0039
REMARK 3 L TENSOR
REMARK 3 L11: 2.5878 L22: 1.2936
REMARK 3 L33: 3.9478 L12: -0.3418
REMARK 3 L13: -0.0784 L23: 0.7305
REMARK 3 S TENSOR
REMARK 3 S11: -0.0476 S12: 0.2716 S13: -0.0428
REMARK 3 S21: 0.0449 S22: 0.0739 S23: -0.0530
REMARK 3 S31: -0.2372 S32: 0.1387 S33: -0.0263
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 : A 192 A 261
REMARK 3 ORIGIN FOR THE GROUP (A): 3.5410 -16.1390 -20.1670
REMARK 3 T TENSOR
REMARK 3 T11: 0.4153 T22: 0.6593
REMARK 3 T33: 0.8981 T12: 0.1360
REMARK 3 T13: 0.0234 T23: -0.0251
REMARK 3 L TENSOR
REMARK 3 L11: 1.8395 L22: 4.4001
REMARK 3 L33: 4.2835 L12: 2.0674
REMARK 3 L13: 0.4171 L23: 1.0641
REMARK 3 S TENSOR
REMARK 3 S11: -0.1182 S12: 0.2205 S13: 0.1100
REMARK 3 S21: -0.7414 S22: -0.0124 S23: 0.2082
REMARK 3 S31: -0.6490 S32: -0.5811 S33: 0.1306
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 262 A 354
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4760 8.7620 -24.9950
REMARK 3 T TENSOR
REMARK 3 T11: 1.5298 T22: 0.4433
REMARK 3 T33: 1.1238 T12: 0.1249
REMARK 3 T13: 0.0968 T23: 0.1495
REMARK 3 L TENSOR
REMARK 3 L11: 1.9738 L22: 2.0643
REMARK 3 L33: -1.3816 L12: -0.8679
REMARK 3 L13: 0.9550 L23: 0.2038
REMARK 3 S TENSOR
REMARK 3 S11: -0.1262 S12: 0.2349 S13: 0.5710
REMARK 3 S21: -0.6227 S22: 0.0372 S23: -0.1259
REMARK 3 S31: -0.6720 S32: -0.1859 S33: 0.0890
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 355 A 429
REMARK 3 ORIGIN FOR THE GROUP (A): 12.3140 -13.9510 -11.3520
REMARK 3 T TENSOR
REMARK 3 T11: 0.6249 T22: 0.6276
REMARK 3 T33: 0.9548 T12: 0.1174
REMARK 3 T13: 0.0783 T23: -0.0377
REMARK 3 L TENSOR
REMARK 3 L11: 0.4396 L22: 3.9500
REMARK 3 L33: 0.5203 L12: 0.3434
REMARK 3 L13: 0.3414 L23: 2.0526
REMARK 3 S TENSOR
REMARK 3 S11: 0.0868 S12: -0.0438 S13: 0.2152
REMARK 3 S21: -0.0788 S22: -0.0167 S23: 0.0690
REMARK 3 S31: -0.2231 S32: -0.0421 S33: -0.0701
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 430 A 511
REMARK 3 ORIGIN FOR THE GROUP (A): -7.1770 -15.3110 -20.6290
REMARK 3 T TENSOR
REMARK 3 T11: 0.3655 T22: 1.0153
REMARK 3 T33: 0.7026 T12: 0.1964
REMARK 3 T13: 0.0824 T23: -0.0649
REMARK 3 L TENSOR
REMARK 3 L11: 2.7096 L22: 4.3838
REMARK 3 L33: 2.1424 L12: -0.2472
REMARK 3 L13: -0.1889 L23: -0.1875
REMARK 3 S TENSOR
REMARK 3 S11: -0.1705 S12: 0.3868 S13: -0.0234
REMARK 3 S21: 0.2461 S22: 0.1484 S23: 0.6902
REMARK 3 S31: -0.1944 S32: -0.9696 S33: 0.0221
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 512 A 622
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6490 -6.3540 -5.0150
REMARK 3 T TENSOR
REMARK 3 T11: 0.6680 T22: 0.5442
REMARK 3 T33: 0.9250 T12: 0.2352
REMARK 3 T13: 0.0688 T23: -0.0705
REMARK 3 L TENSOR
REMARK 3 L11: 1.5779 L22: 0.9866
REMARK 3 L33: 3.8372 L12: 0.5307
REMARK 3 L13: -0.4375 L23: 0.0305
REMARK 3 S TENSOR
REMARK 3 S11: 0.1232 S12: -0.2923 S13: 0.4466
REMARK 3 S21: 0.2976 S22: -0.2235 S23: 0.2948
REMARK 3 S31: -0.8342 S32: -0.6932 S33: 0.1003
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 9 B 106
REMARK 3 ORIGIN FOR THE GROUP (A): 2.0130 -11.8980 -46.1910
REMARK 3 T TENSOR
REMARK 3 T11: 0.5476 T22: 1.0473
REMARK 3 T33: 0.8052 T12: 0.1847
REMARK 3 T13: -0.0202 T23: 0.0715
REMARK 3 L TENSOR
REMARK 3 L11: 1.4018 L22: 2.7166
REMARK 3 L33: 5.0539 L12: -0.4363
REMARK 3 L13: 0.3336 L23: -1.2014
REMARK 3 S TENSOR
REMARK 3 S11: -0.0476 S12: 0.8534 S13: 0.4551
REMARK 3 S21: -0.1777 S22: -0.0195 S23: 0.0538
REMARK 3 S31: -0.3757 S32: -0.9494 S33: 0.0671
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 107 B 247
REMARK 3 ORIGIN FOR THE GROUP (A): 28.7730 -24.0980 -39.9600
REMARK 3 T TENSOR
REMARK 3 T11: 0.7469 T22: 0.4744
REMARK 3 T33: 0.9866 T12: 0.0034
REMARK 3 T13: -0.0038 T23: 0.0585
REMARK 3 L TENSOR
REMARK 3 L11: 2.7763 L22: -0.2102
REMARK 3 L33: 4.5813 L12: 0.5262
REMARK 3 L13: -2.3423 L23: 0.8352
REMARK 3 S TENSOR
REMARK 3 S11: -0.0467 S12: 0.1329 S13: 0.0367
REMARK 3 S21: 0.0685 S22: 0.0397 S23: -0.2211
REMARK 3 S31: 0.2741 S32: 0.3495 S33: 0.0070
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 6 C 35
REMARK 3 ORIGIN FOR THE GROUP (A): 11.1390 -30.9910 -47.2770
REMARK 3 T TENSOR
REMARK 3 T11: 0.6141 T22: 0.7872
REMARK 3 T33: 0.7978 T12: -0.0422
REMARK 3 T13: 0.1582 T23: -0.1557
REMARK 3 L TENSOR
REMARK 3 L11: 4.3714 L22: 13.5938
REMARK 3 L33: 4.8147 L12: -3.3705
REMARK 3 L13: 2.3456 L23: -1.0706
REMARK 3 S TENSOR
REMARK 3 S11: 0.1428 S12: 0.1136 S13: -0.2584
REMARK 3 S21: -0.7120 S22: -0.4924 S23: 0.0004
REMARK 3 S31: 0.3660 S32: -0.3752 S33: 0.3497
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 36 C 63
REMARK 3 ORIGIN FOR THE GROUP (A): 28.9350 -26.8860 -71.4100
REMARK 3 T TENSOR
REMARK 3 T11: 2.0502 T22: 0.1294
REMARK 3 T33: 1.0652 T12: 0.0307
REMARK 3 T13: 0.0171 T23: 0.1102
REMARK 3 L TENSOR
REMARK 3 L11: 5.1198 L22: -4.8800
REMARK 3 L33: 3.6552 L12: 1.3669
REMARK 3 L13: 4.2330 L23: -5.2146
REMARK 3 S TENSOR
REMARK 3 S11: -0.8696 S12: -0.5933 S13: -0.3434
REMARK 3 S21: -1.2228 S22: -0.0502 S23: 1.3902
REMARK 3 S31: -0.8537 S32: 0.2885 S33: 0.9198
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 64 C 89
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0240 -29.3570 -93.4750
REMARK 3 T TENSOR
REMARK 3 T11: 1.5560 T22: 1.0771
REMARK 3 T33: 0.9621 T12: 0.0737
REMARK 3 T13: 0.0115 T23: -0.1715
REMARK 3 L TENSOR
REMARK 3 L11: 0.1743 L22: -3.4725
REMARK 3 L33: 6.7318 L12: 2.3772
REMARK 3 L13: -2.8030 L23: -0.4683
REMARK 3 S TENSOR
REMARK 3 S11: -0.2827 S12: 0.4991 S13: 0.0395
REMARK 3 S21: -0.1557 S22: 0.0801 S23: 0.3104
REMARK 3 S31: -0.4200 S32: -0.2564 S33: 0.2026
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 90 C 120
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4620 -17.4290 -66.6090
REMARK 3 T TENSOR
REMARK 3 T11: 0.8575 T22: 0.4269
REMARK 3 T33: 0.8967 T12: -0.0317
REMARK 3 T13: 0.1512 T23: 0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 1.8447 L22: 5.2479
REMARK 3 L33: 10.6785 L12: -1.9245
REMARK 3 L13: -6.6734 L23: 3.1884
REMARK 3 S TENSOR
REMARK 3 S11: 0.1123 S12: -0.0495 S13: 0.1961
REMARK 3 S21: -0.5745 S22: -0.1417 S23: -0.5142
REMARK 3 S31: -0.6253 S32: -0.4705 S33: 0.0294
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 121 C 143
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0260 -10.8750 -71.7750
REMARK 3 T TENSOR
REMARK 3 T11: 1.6125 T22: 0.1332
REMARK 3 T33: 1.0925 T12: 0.1949
REMARK 3 T13: 0.3339 T23: 0.1375
REMARK 3 L TENSOR
REMARK 3 L11: 10.5624 L22: 3.6979
REMARK 3 L33: 30.8921 L12: 3.9017
REMARK 3 L13: -15.0950 L23: 3.3716
REMARK 3 S TENSOR
REMARK 3 S11: -0.5181 S12: -0.2884 S13: -0.7357
REMARK 3 S21: -0.1893 S22: -0.3277 S23: -0.5559
REMARK 3 S31: 1.7900 S32: -0.3386 S33: 0.8458
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 35 D 96
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5420 -31.9120 -65.4590
REMARK 3 T TENSOR
REMARK 3 T11: 0.8086 T22: 0.3792
REMARK 3 T33: 0.9045 T12: 0.0113
REMARK 3 T13: 0.1825 T23: -0.0388
REMARK 3 L TENSOR
REMARK 3 L11: 5.4905 L22: 3.6619
REMARK 3 L33: 4.4107 L12: -0.6657
REMARK 3 L13: -1.2704 L23: 0.2920
REMARK 3 S TENSOR
REMARK 3 S11: 0.0339 S12: -0.4669 S13: -0.4653
REMARK 3 S21: -0.5571 S22: -0.1697 S23: -0.2285
REMARK 3 S31: 0.0020 S32: 0.4546 S33: 0.1358
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 97 D 136
REMARK 3 ORIGIN FOR THE GROUP (A): 38.7710 -37.1020 -78.5720
REMARK 3 T TENSOR
REMARK 3 T11: 1.8150 T22: 0.5588
REMARK 3 T33: 0.9976 T12: -0.0218
REMARK 3 T13: 0.4684 T23: -0.1989
REMARK 3 L TENSOR
REMARK 3 L11: 4.3458 L22: 1.6110
REMARK 3 L33: 1.7755 L12: 0.0731
REMARK 3 L13: 2.1932 L23: -2.5706
REMARK 3 S TENSOR
REMARK 3 S11: 0.6388 S12: 0.2865 S13: 0.0952
REMARK 3 S21: 0.1437 S22: -0.7737 S23: -0.0650
REMARK 3 S31: -0.7291 S32: 0.3810 S33: 0.1349
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 U VALUES : RESIDUAL ONLY
REMARK 4
REMARK 4 3AE7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-FEB-10.
REMARK 100 THE DEPOSITION ID IS D_1000029141.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-NOV-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : BL-17A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20323
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.600
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.14900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.1430
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.40
REMARK 200 R MERGE FOR SHELL (I) : 0.55300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.220
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 1ZOY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.44
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM HEPES-NAOH, 6% PEG 4000, 200MM
REMARK 280 SUCROSE, 100MM NACL, 10MM CACL2, 0.5MM EDTA, 3% 1,6-HAXANEDIOL,
REMARK 280 0.5% N-DECYL-BETA-D-MALTOSIDE, PH 7.2, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 35.58750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 146.84550
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.99400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 146.84550
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.58750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.99400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 13010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 400
REMARK 400 COMPOUND
REMARK 400 THESE COMPLEX FORMS MITOCHONDRIAL RESPIRATORY COMPLEX II.
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 SER A 1
REMARK 465 SER A 2
REMARK 465 ALA A 3
REMARK 465 LYS A 4
REMARK 465 VAL A 5
REMARK 465 SER A 6
REMARK 465 ASP A 7
REMARK 465 ALA A 8
REMARK 465 ILE A 9
REMARK 465 ALA B 1
REMARK 465 GLN B 2
REMARK 465 THR B 3
REMARK 465 ALA B 4
REMARK 465 ALA B 5
REMARK 465 ALA B 6
REMARK 465 THR B 7
REMARK 465 ALA B 8
REMARK 465 LYS B 248
REMARK 465 LYS B 249
REMARK 465 ALA B 250
REMARK 465 SER B 251
REMARK 465 ALA B 252
REMARK 465 LEU C 4
REMARK 465 GLY C 5
REMARK 465 ALA D 34
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 THR A 11 -23.51 65.67
REMARK 500 PRO A 53 -39.19 -39.35
REMARK 500 THR A 121 -167.91 -113.00
REMARK 500 VAL A 150 56.69 -110.45
REMARK 500 ALA A 151 72.55 44.92
REMARK 500 ASP A 152 -4.60 66.85
REMARK 500 PRO A 290 -81.57 -65.89
REMARK 500 VAL A 291 52.07 -104.69
REMARK 500 ALA A 292 -36.95 -141.74
REMARK 500 LYS A 293 -145.25 59.48
REMARK 500 ARG A 313 32.81 -96.73
REMARK 500 HIS A 365 -57.41 -133.36
REMARK 500 ASN A 374 -177.10 -69.38
REMARK 500 CYS A 433 118.28 63.86
REMARK 500 PHE A 459 47.54 -100.06
REMARK 500 ALA A 482 -155.45 -85.19
REMARK 500 ARG A 512 56.43 -118.48
REMARK 500 TRP A 516 75.87 43.58
REMARK 500 LYS A 544 63.71 -112.57
REMARK 500 GLN A 569 -41.53 -164.50
REMARK 500 ILE B 55 -69.01 -91.44
REMARK 500 SER B 64 -84.21 -156.76
REMARK 500 CYS B 73 36.02 -77.37
REMARK 500 LYS B 109 120.67 -174.15
REMARK 500 ASP B 110 92.49 44.65
REMARK 500 LEU B 111 8.16 59.43
REMARK 500 GLU B 126 81.17 58.34
REMARK 500 LEU B 155 -43.70 -137.01
REMARK 500 GLN B 207 26.37 -78.82
REMARK 500 SER C 22 -169.18 -119.42
REMARK 500 HIS C 29 -60.27 -124.45
REMARK 500 LEU C 82 83.47 45.59
REMARK 500 ALA C 142 62.82 -100.45
REMARK 500 ASP D 123 -157.48 -109.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 302 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 65 SG
REMARK 620 2 FES B 302 S1 114.2
REMARK 620 3 FES B 302 S2 132.7 90.4
REMARK 620 4 CYS B 70 SG 100.1 115.0 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES B 302 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 73 SG
REMARK 620 2 FES B 302 S1 137.3
REMARK 620 3 FES B 302 S2 121.3 90.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 303 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 158 SG
REMARK 620 2 SF4 B 303 S1 106.7
REMARK 620 3 SF4 B 303 S2 124.2 105.0
REMARK 620 4 SF4 B 303 S3 109.0 105.6 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 303 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 161 SG
REMARK 620 2 SF4 B 303 S2 116.9
REMARK 620 3 SF4 B 303 S3 109.5 105.1
REMARK 620 4 SF4 B 303 S4 114.3 104.9 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 303 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 164 SG
REMARK 620 2 SF4 B 303 S1 111.7
REMARK 620 3 SF4 B 303 S3 116.2 105.6
REMARK 620 4 SF4 B 303 S4 112.3 105.1 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 304 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 221 SG
REMARK 620 2 F3S B 304 S1 136.2
REMARK 620 3 F3S B 304 S2 106.9 105.6
REMARK 620 4 F3S B 304 S3 100.5 101.4 100.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 B 303 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 225 SG
REMARK 620 2 SF4 B 303 S1 128.1
REMARK 620 3 SF4 B 303 S2 113.2 105.1
REMARK 620 4 SF4 B 303 S4 97.8 105.1 104.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C1305 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 101 NE2
REMARK 620 2 HEM C1305 NA 86.2
REMARK 620 3 HEM C1305 NB 99.9 88.7
REMARK 620 4 HEM C1305 NC 93.3 177.2 88.7
REMARK 620 5 HEM C1305 ND 84.0 91.3 176.0 91.4
REMARK 620 6 HIS D 79 NE2 166.1 87.9 92.4 93.2 83.6
REMARK 620 N 1 2 3 4 5
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 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 12J B 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3ABV RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AE1 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AE2 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AE3 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AE4 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AE5 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AE6 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AE8 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AE9 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AEA RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AEB RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AEC RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AED RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AEE RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 900 RELATED ID: 3AEF RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX WITH AN EMPTY QUINONE-BINDING POCKET
REMARK 900 RELATED ID: 3AEG RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEX BOUND WITH ANOTHER INHIBITOR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF CHAIN D IS REFERRED IN REF 2 IN A5GZW8, UNIPROT.
DBREF 3AE7 A 1 622 UNP Q0QF01 DHSA_PIG 43 664
DBREF 3AE7 B 1 252 UNP Q007T0 DHSB_PIG 29 280
DBREF 3AE7 C 4 143 UNP D0VWV4 C560_PIG 30 169
DBREF 3AE7 D 34 136 UNP A5GZW8 DHSD_PIG 57 159
SEQRES 1 A 622 SER SER ALA LYS VAL SER ASP ALA ILE SER THR GLN TYR
SEQRES 2 A 622 PRO VAL VAL ASP HIS GLU PHE ASP ALA VAL VAL VAL GLY
SEQRES 3 A 622 ALA GLY GLY ALA GLY LEU ARG ALA ALA PHE GLY LEU SER
SEQRES 4 A 622 GLU ALA GLY PHE ASN THR ALA CYS VAL THR LYS LEU PHE
SEQRES 5 A 622 PRO THR ARG SER HIS THR VAL ALA ALA GLN GLY GLY ILE
SEQRES 6 A 622 ASN ALA ALA LEU GLY ASN MET GLU GLU ASP ASN TRP ARG
SEQRES 7 A 622 TRP HIS PHE TYR ASP THR VAL LYS GLY SER ASP TRP LEU
SEQRES 8 A 622 GLY ASP GLN ASP ALA ILE HIS TYR MET THR GLU GLN ALA
SEQRES 9 A 622 PRO ALA SER VAL VAL GLU LEU GLU ASN TYR GLY MET PRO
SEQRES 10 A 622 PHE SER ARG THR GLU ASP GLY LYS ILE TYR GLN ARG ALA
SEQRES 11 A 622 PHE GLY GLY GLN SER LEU LYS PHE GLY LYS GLY GLY GLN
SEQRES 12 A 622 ALA HIS ARG CYS CYS CYS VAL ALA ASP ARG THR GLY HIS
SEQRES 13 A 622 SER LEU LEU HIS THR LEU TYR GLY ARG SER LEU ARG TYR
SEQRES 14 A 622 ASP THR SER TYR PHE VAL GLU TYR PHE ALA LEU ASP LEU
SEQRES 15 A 622 LEU MET GLU ASN GLY GLU CYS ARG GLY VAL ILE ALA LEU
SEQRES 16 A 622 CYS ILE GLU ASP GLY SER ILE HIS ARG ILE ARG ALA ARG
SEQRES 17 A 622 ASN THR VAL VAL ALA THR GLY GLY TYR GLY ARG THR TYR
SEQRES 18 A 622 PHE SER CYS THR SER ALA HIS THR SER THR GLY ASP GLY
SEQRES 19 A 622 THR ALA MET VAL THR ARG ALA GLY LEU PRO CYS GLN ASP
SEQRES 20 A 622 LEU GLU PHE VAL GLN PHE HIS PRO THR GLY ILE TYR GLY
SEQRES 21 A 622 ALA GLY CYS LEU ILE THR GLU GLY CYS ARG GLY GLU GLY
SEQRES 22 A 622 GLY ILE LEU ILE ASN SER GLN GLY GLU ARG PHE MET GLU
SEQRES 23 A 622 ARG TYR ALA PRO VAL ALA LYS ASP LEU ALA SER ARG ASP
SEQRES 24 A 622 VAL VAL SER ARG SER MET THR LEU GLU ILE ARG GLU GLY
SEQRES 25 A 622 ARG GLY CYS GLY PRO GLU LYS ASP HIS VAL TYR LEU GLN
SEQRES 26 A 622 LEU HIS HIS LEU PRO PRO GLU GLN LEU ALA VAL ARG LEU
SEQRES 27 A 622 PRO GLY ILE SER GLU THR ALA MET ILE PHE ALA GLY VAL
SEQRES 28 A 622 ASP VAL THR LYS GLU PRO ILE PRO VAL LEU PRO THR VAL
SEQRES 29 A 622 HIS TYR ASN MET GLY GLY ILE PRO THR ASN TYR LYS GLY
SEQRES 30 A 622 GLN VAL LEU ARG HIS VAL ASN GLY GLN ASP GLN VAL VAL
SEQRES 31 A 622 PRO GLY LEU TYR ALA CYS GLY GLU ALA ALA CYS ALA SER
SEQRES 32 A 622 VAL HIS GLY ALA ASN ARG LEU GLY ALA ASN SER LEU LEU
SEQRES 33 A 622 ASP LEU VAL VAL PHE GLY ARG ALA CYS ALA LEU SER ILE
SEQRES 34 A 622 ALA GLU SER CYS ARG PRO GLY ASP LYS VAL PRO SER ILE
SEQRES 35 A 622 LYS PRO ASN ALA GLY GLU GLU SER VAL MET ASN LEU ASP
SEQRES 36 A 622 LYS LEU ARG PHE ALA ASN GLY THR ILE ARG THR SER GLU
SEQRES 37 A 622 LEU ARG LEU SER MET GLN LYS SER MET GLN SER HIS ALA
SEQRES 38 A 622 ALA VAL PHE ARG VAL GLY SER VAL LEU GLN GLU GLY CYS
SEQRES 39 A 622 GLU LYS ILE LEU ARG LEU TYR GLY ASP LEU GLN HIS LEU
SEQRES 40 A 622 LYS THR PHE ASP ARG GLY MET VAL TRP ASN THR ASP LEU
SEQRES 41 A 622 VAL GLU THR LEU GLU LEU GLN ASN LEU MET LEU CYS ALA
SEQRES 42 A 622 LEU GLN THR ILE TYR GLY ALA GLU ALA ARG LYS GLU SER
SEQRES 43 A 622 ARG GLY ALA HIS ALA ARG GLU ASP PHE LYS GLU ARG VAL
SEQRES 44 A 622 ASP GLU TYR ASP TYR SER LYS PRO ILE GLN GLY GLN GLN
SEQRES 45 A 622 LYS LYS PRO PHE GLN GLU HIS TRP ARG LYS HIS THR LEU
SEQRES 46 A 622 SER TYR VAL ASP VAL LYS THR GLY LYS VAL SER LEU GLU
SEQRES 47 A 622 TYR ARG PRO VAL ILE ASP LYS THR LEU ASN GLU ALA ASP
SEQRES 48 A 622 CYS ALA THR VAL PRO PRO ALA ILE ARG SER TYR
SEQRES 1 B 252 ALA GLN THR ALA ALA ALA THR ALA PRO ARG ILE LYS LYS
SEQRES 2 B 252 PHE ALA ILE TYR ARG TRP ASP PRO ASP LYS THR GLY ASP
SEQRES 3 B 252 LYS PRO HIS MET GLN THR TYR GLU ILE ASP LEU ASN ASN
SEQRES 4 B 252 CYS GLY PRO MET VAL LEU ASP ALA LEU ILE LYS ILE LYS
SEQRES 5 B 252 ASN GLU ILE ASP SER THR LEU THR PHE ARG ARG SER CYS
SEQRES 6 B 252 ARG GLU GLY ILE CYS GLY SER CYS ALA MET ASN ILE ASN
SEQRES 7 B 252 GLY GLY ASN THR LEU ALA CYS THR ARG ARG ILE ASP THR
SEQRES 8 B 252 ASN LEU ASP LYS VAL SER LYS ILE TYR PRO LEU PRO HIS
SEQRES 9 B 252 MET TYR VAL ILE LYS ASP LEU VAL PRO ASP LEU SER ASN
SEQRES 10 B 252 PHE TYR ALA GLN TYR LYS SER ILE GLU PRO TYR LEU LYS
SEQRES 11 B 252 LYS LYS ASP GLU SER GLN GLU GLY LYS GLN GLN TYR LEU
SEQRES 12 B 252 GLN SER ILE GLU GLU ARG GLU LYS LEU ASP GLY LEU TYR
SEQRES 13 B 252 GLU CYS ILE LEU CYS ALA CYS CYS SER THR SER CYS PRO
SEQRES 14 B 252 SER TYR TRP TRP ASN GLY ASP LYS TYR LEU GLY PRO ALA
SEQRES 15 B 252 VAL LEU MET GLN ALA TYR ARG TRP MET ILE ASP SER ARG
SEQRES 16 B 252 ASP ASP PHE THR GLU GLU ARG LEU ALA LYS LEU GLN ASP
SEQRES 17 B 252 PRO PHE SER LEU TYR ARG CYS HIS THR ILE MET ASN CYS
SEQRES 18 B 252 THR GLY THR CYS PRO LYS GLY LEU ASN PRO GLY LYS ALA
SEQRES 19 B 252 ILE ALA GLU ILE LYS LYS MET MET ALA THR TYR LYS GLU
SEQRES 20 B 252 LYS LYS ALA SER ALA
SEQRES 1 C 140 LEU GLY THR THR ALA LYS GLU GLU MET GLU ARG PHE TRP
SEQRES 2 C 140 ASN LYS ASN LEU GLY SER ASN ARG PRO LEU SER PRO HIS
SEQRES 3 C 140 ILE THR ILE TYR ARG TRP SER LEU PRO MET ALA MET SER
SEQRES 4 C 140 ILE CYS HIS ARG GLY THR GLY ILE ALA LEU SER ALA GLY
SEQRES 5 C 140 VAL SER LEU PHE GLY LEU SER ALA LEU LEU LEU PRO GLY
SEQRES 6 C 140 ASN PHE GLU SER HIS LEU GLU LEU VAL LYS SER LEU CYS
SEQRES 7 C 140 LEU GLY PRO THR LEU ILE TYR THR ALA LYS PHE GLY ILE
SEQRES 8 C 140 VAL PHE PRO LEU MET TYR HIS THR TRP ASN GLY ILE ARG
SEQRES 9 C 140 HIS LEU ILE TRP ASP LEU GLY LYS GLY LEU THR ILE PRO
SEQRES 10 C 140 GLN LEU THR GLN SER GLY VAL VAL VAL LEU ILE LEU THR
SEQRES 11 C 140 VAL LEU SER SER VAL GLY LEU ALA ALA MET
SEQRES 1 D 103 ALA SER SER LYS ALA ALA SER LEU HIS TRP THR GLY GLU
SEQRES 2 D 103 ARG VAL VAL SER VAL LEU LEU LEU GLY LEU LEU PRO ALA
SEQRES 3 D 103 ALA TYR LEU ASN PRO CYS SER ALA MET ASP TYR SER LEU
SEQRES 4 D 103 ALA ALA ALA LEU THR LEU HIS GLY HIS TRP GLY ILE GLY
SEQRES 5 D 103 GLN VAL VAL THR ASP TYR VAL ARG GLY ASP ALA LEU GLN
SEQRES 6 D 103 LYS ALA ALA LYS ALA GLY LEU LEU ALA LEU SER ALA PHE
SEQRES 7 D 103 THR PHE ALA GLY LEU CYS TYR PHE ASN TYR HIS ASP VAL
SEQRES 8 D 103 GLY ILE CYS LYS ALA VAL ALA MET LEU TRP LYS LEU
HET FAD A 700 53
HET FES B 302 4
HET SF4 B 303 8
HET F3S B 304 7
HET 12J B1201 20
HET HEM C1305 43
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM F3S FE3-S4 CLUSTER
HETNAM 12J 2-IODO-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN 12J 2-IODO-N-(3-ISOPROPOXYPHENYL)BENZAMIDE
HETSYN HEM HEME
FORMUL 5 FAD C27 H33 N9 O15 P2
FORMUL 6 FES FE2 S2
FORMUL 7 SF4 FE4 S4
FORMUL 8 F3S FE3 S4
FORMUL 9 12J C16 H16 I N O2
FORMUL 10 HEM C34 H32 FE N4 O4
HELIX 1 1 GLY A 28 GLY A 42 1 15
HELIX 2 2 PHE A 52 ALA A 61 5 10
HELIX 3 3 ASN A 76 SER A 88 1 13
HELIX 4 4 ASP A 93 GLN A 103 1 11
HELIX 5 5 GLN A 103 GLY A 115 1 13
HELIX 6 6 ARG A 153 LEU A 167 1 15
HELIX 7 7 TYR A 217 TYR A 221 5 5
HELIX 8 8 GLY A 232 ALA A 241 1 10
HELIX 9 9 PHE A 284 ALA A 289 1 6
HELIX 10 10 ALA A 292 ALA A 296 5 5
HELIX 11 11 SER A 297 GLY A 312 1 16
HELIX 12 12 PRO A 330 LEU A 338 1 9
HELIX 13 13 LEU A 338 PHE A 348 1 11
HELIX 14 14 ASN A 413 SER A 432 1 20
HELIX 15 15 GLY A 447 PHE A 459 1 13
HELIX 16 16 THR A 466 ALA A 481 1 16
HELIX 17 17 VAL A 486 ASP A 503 1 18
HELIX 18 18 ASN A 517 ARG A 543 1 27
HELIX 19 19 MET B 43 GLU B 54 1 12
HELIX 20 20 LEU B 115 ILE B 125 1 11
HELIX 21 21 SER B 145 LYS B 151 1 7
HELIX 22 22 CYS B 168 ASN B 174 1 7
HELIX 23 23 GLY B 180 TRP B 190 1 11
HELIX 24 24 PHE B 198 ALA B 204 1 7
HELIX 25 25 LYS B 205 GLN B 207 5 3
HELIX 26 26 ASN B 230 THR B 244 1 15
HELIX 27 27 THR C 7 LEU C 20 1 14
HELIX 28 28 SER C 36 LEU C 66 1 31
HELIX 29 29 ASN C 69 LYS C 78 1 10
HELIX 30 30 SER C 79 CYS C 81 5 3
HELIX 31 31 GLY C 83 GLY C 114 1 32
HELIX 32 32 THR C 118 ALA C 142 1 25
HELIX 33 33 ALA D 38 ASN D 63 1 26
HELIX 34 34 CYS D 65 VAL D 92 1 28
HELIX 35 35 GLY D 94 HIS D 122 1 29
HELIX 36 36 GLY D 125 LYS D 135 1 11
SHEET 1 A 6 SER A 172 VAL A 175 0
SHEET 2 A 6 THR A 45 THR A 49 1 N CYS A 47 O SER A 172
SHEET 3 A 6 VAL A 15 VAL A 25 1 N VAL A 24 O ALA A 46
SHEET 4 A 6 ILE A 202 VAL A 212 1 O VAL A 211 N VAL A 23
SHEET 5 A 6 CYS A 189 CYS A 196 -1 N ALA A 194 O HIS A 203
SHEET 6 A 6 TYR A 177 MET A 184 -1 N LEU A 183 O ARG A 190
SHEET 1 B 6 SER A 172 VAL A 175 0
SHEET 2 B 6 THR A 45 THR A 49 1 N CYS A 47 O SER A 172
SHEET 3 B 6 VAL A 15 VAL A 25 1 N VAL A 24 O ALA A 46
SHEET 4 B 6 ILE A 202 VAL A 212 1 O VAL A 211 N VAL A 23
SHEET 5 B 6 GLN A 386 ALA A 395 1 O TYR A 394 N THR A 210
SHEET 6 B 6 GLN A 378 VAL A 383 -1 N ARG A 381 O GLN A 388
SHEET 1 C 3 ILE A 65 ASN A 66 0
SHEET 2 C 3 GLN A 143 CYS A 148 -1 O CYS A 148 N ILE A 65
SHEET 3 C 3 GLN A 128 SER A 135 -1 N GLN A 134 O ALA A 144
SHEET 1 D 3 CYS A 245 GLN A 246 0
SHEET 2 D 3 LYS A 582 VAL A 588 -1 O SER A 586 N CYS A 245
SHEET 3 D 3 VAL A 595 PRO A 601 -1 O ARG A 600 N HIS A 583
SHEET 1 E 2 VAL A 251 HIS A 254 0
SHEET 2 E 2 THR A 363 ASN A 367 -1 O TYR A 366 N GLN A 252
SHEET 1 F 3 ILE A 275 ILE A 277 0
SHEET 2 F 3 VAL A 322 GLN A 325 -1 O GLN A 325 N ILE A 275
SHEET 3 F 3 ILE A 358 VAL A 360 -1 O VAL A 360 N VAL A 322
SHEET 1 G 2 ILE A 371 PRO A 372 0
SHEET 2 G 2 ALA A 400 CYS A 401 1 O CYS A 401 N ILE A 371
SHEET 1 H 2 ILE A 464 ARG A 465 0
SHEET 2 H 2 LEU A 507 LYS A 508 1 O LYS A 508 N ILE A 464
SHEET 1 I 3 PHE A 484 ARG A 485 0
SHEET 2 I 3 HIS A 550 ARG A 552 1 O ALA A 551 N ARG A 485
SHEET 3 I 3 SER A 546 ARG A 547 -1 N ARG A 547 O HIS A 550
SHEET 1 J 5 HIS B 29 ASP B 36 0
SHEET 2 J 5 ILE B 11 ARG B 18 -1 N ILE B 16 O GLN B 31
SHEET 3 J 5 SER B 97 TYR B 100 1 O ILE B 99 N ALA B 15
SHEET 4 J 5 ALA B 74 ILE B 77 -1 N ASN B 76 O TYR B 100
SHEET 5 J 5 ASN B 81 LEU B 83 -1 O THR B 82 N MET B 75
LINK NE2 HIS A 57 C8M FAD A 700 1555 1555 2.08
LINK SG CYS B 65 FE2 FES B 302 1555 1555 2.22
LINK SG CYS B 70 FE2 FES B 302 1555 1555 2.32
LINK SG CYS B 73 FE1 FES B 302 1555 1555 1.94
LINK SG CYS B 158 FE4 SF4 B 303 1555 1555 2.26
LINK SG CYS B 161 FE1 SF4 B 303 1555 1555 2.42
LINK SG CYS B 164 FE2 SF4 B 303 1555 1555 2.22
LINK SG CYS B 221 FE1 F3S B 304 1555 1555 2.47
LINK SG CYS B 225 FE3 SF4 B 303 1555 1555 2.67
LINK NE2 HIS C 101 FE HEM C1305 1555 1555 2.16
LINK FE HEM C1305 NE2 HIS D 79 1555 1555 2.35
SITE 1 AC1 30 GLY A 26 ALA A 27 GLY A 28 VAL A 48
SITE 2 AC1 30 THR A 49 LYS A 50 LEU A 51 SER A 56
SITE 3 AC1 30 HIS A 57 THR A 58 ALA A 60 ALA A 61
SITE 4 AC1 30 GLN A 62 GLY A 63 GLY A 64 TYR A 177
SITE 5 AC1 30 PHE A 178 ALA A 179 ALA A 213 THR A 214
SITE 6 AC1 30 GLY A 215 THR A 225 SER A 226 ASP A 233
SITE 7 AC1 30 TYR A 366 GLU A 398 ARG A 409 SER A 414
SITE 8 AC1 30 LEU A 415 LEU A 418
SITE 1 AC2 8 SER B 64 CYS B 65 ARG B 66 GLY B 68
SITE 2 AC2 8 CYS B 70 GLY B 71 CYS B 73 CYS B 85
SITE 1 AC3 9 CYS B 158 ILE B 159 LEU B 160 CYS B 161
SITE 2 AC3 9 ALA B 162 CYS B 164 ALA B 182 CYS B 225
SITE 3 AC3 9 PRO B 226
SITE 1 AC4 9 CYS B 168 SER B 170 TYR B 178 PRO B 181
SITE 2 AC4 9 CYS B 215 THR B 217 ILE B 218 MET B 219
SITE 3 AC4 9 CYS B 221
SITE 1 AC5 13 HIS C 45 ARG C 46 GLY C 49 SER C 53
SITE 2 AC5 13 HIS C 101 HIS C 108 ARG D 47 SER D 50
SITE 3 AC5 13 LEU D 53 LEU D 54 LEU D 57 HIS D 79
SITE 4 AC5 13 GLY D 83
SITE 1 AC6 10 PRO B 169 TRP B 173 HIS B 216 ILE B 218
SITE 2 AC6 10 ILE C 30 TRP C 35 SER C 42 ARG C 46
SITE 3 AC6 10 ASP D 90 TYR D 91
CRYST1 71.175 83.988 293.691 90.00 90.00 90.00 P 21 21 21 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 0.014050 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011906 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003405 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
