HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10 3AEC
TITLE CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE 2 2-IODO-N-(1-METHYLETHYL)-BENZAMID
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 1 09-FEB-11 3AEC 0
JRNL AUTH S.HARADA,T.SASAKI,M.SHINDO,Y.KIDO,D.K.INAOKA,J.OMORI,
JRNL AUTH 2 A.OSANAI,K.SAKAMOTO,J.MAO,S.MATSUOKA,M.INOUE,T.HONMA,
JRNL AUTH 3 A.TANAKA,K.KITA
JRNL TITL CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II
JRNL TITL 2 BOUND WITH 2-IODO-N-(1-METHYLETHYL)-BENZAMID
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.61 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.61
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 20635
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) : 0.248
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1044
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) : 3.61
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.70
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1296
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 90.15
REMARK 3 BIN R VALUE (WORKING SET) : 0.3380
REMARK 3 BIN FREE R VALUE SET COUNT : 67
REMARK 3 BIN FREE R VALUE : 0.3220
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 : 172
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) : 92.54
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.46000
REMARK 3 B22 (A**2) : 0.30000
REMARK 3 B33 (A**2) : 0.16000
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): 0.722
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.570
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 80.878
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.892
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.850
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8856 ; 0.005 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12007 ; 0.857 ; 1.991
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1088 ; 4.109 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 375 ;34.273 ;23.413
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1469 ;15.961 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;11.184 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1305 ; 0.057 ; 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): 5412 ; 0.091 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8677 ; 0.168 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3444 ; 0.129 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3313 ; 0.232 ; 4.500
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 : 12
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 259
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1540 -17.6460 18.0330
REMARK 3 T TENSOR
REMARK 3 T11: 0.5522 T22: 0.5090
REMARK 3 T33: 0.5063 T12: -0.0935
REMARK 3 T13: 0.0341 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 2.1076 L22: 1.4483
REMARK 3 L33: 3.7833 L12: -0.2911
REMARK 3 L13: -0.2003 L23: -0.2571
REMARK 3 S TENSOR
REMARK 3 S11: -0.0212 S12: -0.1196 S13: -0.0807
REMARK 3 S21: -0.0363 S22: 0.0039 S23: 0.0784
REMARK 3 S31: -0.2227 S32: 0.0473 S33: 0.0173
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 260 A 348
REMARK 3 ORIGIN FOR THE GROUP (A): -18.7720 8.6700 24.4790
REMARK 3 T TENSOR
REMARK 3 T11: 0.9965 T22: 0.3321
REMARK 3 T33: 0.7753 T12: -0.0948
REMARK 3 T13: 0.0777 T23: -0.1458
REMARK 3 L TENSOR
REMARK 3 L11: 3.4853 L22: 0.9462
REMARK 3 L33: 4.3308 L12: 0.4766
REMARK 3 L13: -2.3586 L23: -1.8573
REMARK 3 S TENSOR
REMARK 3 S11: 0.1025 S12: -0.1994 S13: 0.4591
REMARK 3 S21: 0.4278 S22: -0.1250 S23: -0.0484
REMARK 3 S31: -1.1766 S32: -0.2764 S33: 0.0225
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 349 A 622
REMARK 3 ORIGIN FOR THE GROUP (A): -3.6370 -10.9100 11.8190
REMARK 3 T TENSOR
REMARK 3 T11: 0.6518 T22: 0.5941
REMARK 3 T33: 0.4938 T12: -0.1571
REMARK 3 T13: 0.0466 T23: 0.0561
REMARK 3 L TENSOR
REMARK 3 L11: 1.7173 L22: 1.2215
REMARK 3 L33: 1.9840 L12: -0.2519
REMARK 3 L13: -0.5874 L23: -0.3545
REMARK 3 S TENSOR
REMARK 3 S11: 0.0650 S12: 0.0698 S13: 0.0778
REMARK 3 S21: -0.0970 S22: -0.0601 S23: -0.1158
REMARK 3 S31: -0.4360 S32: 0.6017 S33: -0.0048
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 : B 9 B 106
REMARK 3 ORIGIN FOR THE GROUP (A): -2.5530 -12.2290 46.1780
REMARK 3 T TENSOR
REMARK 3 T11: 0.4967 T22: 1.1072
REMARK 3 T33: 0.5436 T12: -0.2335
REMARK 3 T13: -0.0672 T23: -0.0432
REMARK 3 L TENSOR
REMARK 3 L11: 0.3339 L22: 3.9044
REMARK 3 L33: 4.0994 L12: 0.2013
REMARK 3 L13: -0.1574 L23: 1.2025
REMARK 3 S TENSOR
REMARK 3 S11: 0.1067 S12: -0.7594 S13: 0.4341
REMARK 3 S21: 0.3036 S22: -0.1445 S23: -0.3739
REMARK 3 S31: -0.3441 S32: 1.2307 S33: 0.0378
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 : B 107 B 247
REMARK 3 ORIGIN FOR THE GROUP (A): -29.2450 -24.2350 40.0940
REMARK 3 T TENSOR
REMARK 3 T11: 0.7165 T22: 0.4014
REMARK 3 T33: 0.6489 T12: -0.0129
REMARK 3 T13: 0.0093 T23: -0.0434
REMARK 3 L TENSOR
REMARK 3 L11: 1.9831 L22: 0.1409
REMARK 3 L33: 4.8302 L12: -0.8463
REMARK 3 L13: -1.4160 L23: -0.8366
REMARK 3 S TENSOR
REMARK 3 S11: -0.0256 S12: 0.1554 S13: -0.1276
REMARK 3 S21: -0.1332 S22: 0.0122 S23: 0.2473
REMARK 3 S31: 0.1302 S32: -0.6825 S33: 0.0134
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 : C 6 C 47
REMARK 3 ORIGIN FOR THE GROUP (A): -15.0490 -28.3250 51.4830
REMARK 3 T TENSOR
REMARK 3 T11: 0.8911 T22: 0.4719
REMARK 3 T33: 0.4965 T12: 0.0296
REMARK 3 T13: 0.0220 T23: 0.2597
REMARK 3 L TENSOR
REMARK 3 L11: 6.2029 L22: 2.6285
REMARK 3 L33: 5.8110 L12: -1.0358
REMARK 3 L13: -2.5986 L23: 3.1320
REMARK 3 S TENSOR
REMARK 3 S11: 0.0291 S12: 0.1544 S13: -0.1161
REMARK 3 S21: 0.3749 S22: 0.1252 S23: -0.0865
REMARK 3 S31: -0.1235 S32: 0.8510 S33: -0.1543
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 : C 48 C 106
REMARK 3 ORIGIN FOR THE GROUP (A): -33.1920 -27.2840 84.3750
REMARK 3 T TENSOR
REMARK 3 T11: 1.2874 T22: 0.4303
REMARK 3 T33: 0.4500 T12: -0.0127
REMARK 3 T13: 0.1409 T23: 0.0434
REMARK 3 L TENSOR
REMARK 3 L11: 3.0844 L22: 5.8499
REMARK 3 L33: 9.9826 L12: 2.4026
REMARK 3 L13: -1.0016 L23: -3.8458
REMARK 3 S TENSOR
REMARK 3 S11: 0.0920 S12: -1.0272 S13: -0.1412
REMARK 3 S21: 1.0720 S22: -0.1474 S23: -0.3469
REMARK 3 S31: -0.6738 S32: 0.4760 S33: 0.0554
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 : C 107 C 143
REMARK 3 ORIGIN FOR THE GROUP (A): -34.6340 -12.9350 65.6630
REMARK 3 T TENSOR
REMARK 3 T11: 0.8482 T22: 0.0339
REMARK 3 T33: 0.7371 T12: 0.0106
REMARK 3 T13: 0.1190 T23: -0.0188
REMARK 3 L TENSOR
REMARK 3 L11: 6.5006 L22: 6.4151
REMARK 3 L33: 22.6394 L12: 2.3213
REMARK 3 L13: -5.1226 L23: 0.6324
REMARK 3 S TENSOR
REMARK 3 S11: 0.6890 S12: 0.3276 S13: 0.0842
REMARK 3 S21: 0.3952 S22: -0.0622 S23: 0.2594
REMARK 3 S31: -1.0672 S32: -0.6822 S33: -0.6268
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 : D 35 D 67
REMARK 3 ORIGIN FOR THE GROUP (A): -44.6850 -28.8400 65.2490
REMARK 3 T TENSOR
REMARK 3 T11: 0.6289 T22: 0.7127
REMARK 3 T33: 0.5839 T12: 0.0590
REMARK 3 T13: 0.0137 T23: 0.1573
REMARK 3 L TENSOR
REMARK 3 L11: 5.0822 L22: 8.9335
REMARK 3 L33: 17.4591 L12: 2.3154
REMARK 3 L13: -2.7534 L23: 1.5244
REMARK 3 S TENSOR
REMARK 3 S11: 0.0461 S12: 0.0453 S13: -0.1615
REMARK 3 S21: -0.0987 S22: 0.2811 S23: 0.3507
REMARK 3 S31: -0.9138 S32: 0.4581 S33: -0.3272
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 : D 68 D 96
REMARK 3 ORIGIN FOR THE GROUP (A): -34.1090 -35.4440 66.3630
REMARK 3 T TENSOR
REMARK 3 T11: 1.0399 T22: 0.1457
REMARK 3 T33: 0.7114 T12: -0.0574
REMARK 3 T13: 0.1666 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 2.1542 L22: 2.2726
REMARK 3 L33: 7.0111 L12: 1.2182
REMARK 3 L13: 2.1779 L23: -1.6643
REMARK 3 S TENSOR
REMARK 3 S11: -0.0161 S12: 0.0802 S13: -0.6772
REMARK 3 S21: 0.1493 S22: -0.3406 S23: 0.2312
REMARK 3 S31: 0.1841 S32: 0.2412 S33: 0.3567
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 : D 97 D 124
REMARK 3 ORIGIN FOR THE GROUP (A): -36.8810 -42.0510 75.1390
REMARK 3 T TENSOR
REMARK 3 T11: 1.1392 T22: 0.2742
REMARK 3 T33: 0.7578 T12: -0.0285
REMARK 3 T13: 0.2537 T23: 0.2065
REMARK 3 L TENSOR
REMARK 3 L11: 6.4533 L22: 6.1754
REMARK 3 L33: 22.3815 L12: -1.4955
REMARK 3 L13: -12.2388 L23: 5.0736
REMARK 3 S TENSOR
REMARK 3 S11: 0.0688 S12: -0.7801 S13: 0.1371
REMARK 3 S21: 0.0537 S22: 0.2972 S23: -0.8124
REMARK 3 S31: 0.6590 S32: 0.0499 S33: -0.3660
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 : D 125 D 136
REMARK 3 ORIGIN FOR THE GROUP (A): -42.0140 -26.3370 88.4730
REMARK 3 T TENSOR
REMARK 3 T11: 1.3137 T22: 0.4731
REMARK 3 T33: 0.9588 T12: -0.0346
REMARK 3 T13: 0.0999 T23: 0.0736
REMARK 3 L TENSOR
REMARK 3 L11: 36.0313 L22: 33.1170
REMARK 3 L33: 12.1283 L12: -0.6746
REMARK 3 L13: -12.2028 L23: 12.3283
REMARK 3 S TENSOR
REMARK 3 S11: 1.4674 S12: -2.0795 S13: 2.3572
REMARK 3 S21: -1.0722 S22: -0.4162 S23: 2.2929
REMARK 3 S31: -1.2862 S32: -1.7525 S33: -1.0512
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 3AEC COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 23-FEB-10.
REMARK 100 THE RCSB ID CODE IS RCSB029146.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-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) : 1.30001
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20826
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 (%) : 99.1
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4310
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 (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.70
REMARK 200 R MERGE FOR SHELL (I) : 0.56300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.520
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 (%): 65.53
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM HEPES-NAOH, 7% 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 35.48300
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 147.62700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.99700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 147.62700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.48300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.99700
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: 12950 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42230 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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: 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 SG CYS B 73 FE2 FES B 302 1.87
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 THR A 11 -22.64 65.23
REMARK 500 ARG A 55 32.39 -89.71
REMARK 500 SER A 56 -138.60 -76.69
REMARK 500 ALA A 68 57.44 -91.31
REMARK 500 TRP A 90 17.63 59.30
REMARK 500 THR A 121 -169.90 -112.63
REMARK 500 ARG A 146 24.98 -140.91
REMARK 500 VAL A 150 58.52 -107.57
REMARK 500 ALA A 151 72.50 43.68
REMARK 500 ASP A 152 -17.41 69.72
REMARK 500 ARG A 153 52.12 -114.53
REMARK 500 MET A 285 45.92 -78.47
REMARK 500 TYR A 288 -60.81 -96.82
REMARK 500 LYS A 293 -133.77 49.69
REMARK 500 ARG A 313 44.18 -102.28
REMARK 500 ASP A 320 -36.16 -134.68
REMARK 500 HIS A 365 -72.30 -131.54
REMARK 500 ALA A 481 55.33 -95.62
REMARK 500 TRP A 516 74.94 46.97
REMARK 500 PHE A 555 77.26 -111.41
REMARK 500 GLN A 569 -73.24 -159.35
REMARK 500 GLN A 577 32.74 -91.69
REMARK 500 ASP B 22 54.70 -102.27
REMARK 500 THR B 24 95.06 54.61
REMARK 500 ASN B 39 46.09 -104.56
REMARK 500 GLU B 54 -60.37 -133.93
REMARK 500 SER B 64 -83.54 -161.86
REMARK 500 ARG B 66 40.75 38.86
REMARK 500 ILE B 69 -0.29 -141.22
REMARK 500 CYS B 73 46.15 -79.41
REMARK 500 LYS B 109 133.88 -171.78
REMARK 500 ASP B 110 85.43 26.37
REMARK 500 GLU B 126 79.16 58.79
REMARK 500 ASP B 133 76.67 -103.83
REMARK 500 LYS B 139 -35.27 -136.92
REMARK 500 LEU B 155 -44.90 -135.47
REMARK 500 PHE B 198 49.37 -83.93
REMARK 500 GLN B 207 40.87 -79.04
REMARK 500 THR C 7 -169.96 -107.52
REMARK 500 HIS C 29 -89.29 -106.45
REMARK 500 CYS C 81 121.69 -38.05
REMARK 500 ALA C 142 40.69 -105.67
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 EPH D 1306
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 HEM C1305 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 101 NE2
REMARK 620 2 HEM C1305 NA 96.3
REMARK 620 3 HEM C1305 NB 96.3 88.5
REMARK 620 4 HEM C1305 NC 84.5 177.9 89.5
REMARK 620 5 HEM C1305 ND 88.4 91.4 175.3 90.6
REMARK 620 6 HIS D 79 NE2 172.5 88.9 89.2 90.4 86.1
REMARK 620 N 1 2 3 4 5
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 70 SG
REMARK 620 2 FES B 302 S1 104.3
REMARK 620 3 FES B 302 S2 116.5 90.7
REMARK 620 4 CYS B 65 SG 109.0 123.0 112.7
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 161 SG
REMARK 620 2 SF4 B 303 S1 123.9
REMARK 620 3 SF4 B 303 S3 107.4 105.3
REMARK 620 4 SF4 B 303 S4 109.0 104.5 105.3
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 158 SG
REMARK 620 2 SF4 B 303 S2 97.9
REMARK 620 3 SF4 B 303 S3 103.9 106.0
REMARK 620 4 SF4 B 303 S4 136.2 104.7 105.1
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 215 SG
REMARK 620 2 F3S B 304 S1 102.2
REMARK 620 3 F3S B 304 S2 101.5 122.0
REMARK 620 4 F3S B 304 S3 134.5 100.3 99.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 304 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 221 SG
REMARK 620 2 F3S B 304 S1 106.2
REMARK 620 3 F3S B 304 S3 123.8 100.3
REMARK 620 4 F3S B 304 S4 104.7 123.5 100.1
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 97.4
REMARK 620 3 SF4 B 303 S2 132.0 105.1
REMARK 620 4 SF4 B 303 S4 109.6 104.7 105.0
REMARK 620 N 1 2 3
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 164 SG
REMARK 620 2 SF4 B 303 S1 93.0
REMARK 620 3 SF4 B 303 S2 107.5 104.9
REMARK 620 4 SF4 B 303 S3 136.0 105.1 106.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S B 304 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 168 SG
REMARK 620 2 F3S B 304 S2 83.6
REMARK 620 3 F3S B 304 S3 88.9 99.5
REMARK 620 4 F3S B 304 S4 98.3 160.0 100.5
REMARK 620 N 1 2 3
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 EPH D 1306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EBM C 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: 3AE7 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: 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
REMARK 900 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 3AEC A 1 622 UNP Q0QF01 DHSA_PIG 43 664
DBREF 3AEC B 1 252 UNP Q007T0 DHSB_PIG 29 280
DBREF 3AEC C 4 143 UNP D0VWV4 C560_PIG 30 169
DBREF 3AEC 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 HEM C1305 43
HET EPH D1306 44
HET EBM C1201 13
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM F3S FE3-S4 CLUSTER
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM EPH L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-
HETNAM 2 EPH PHOSPHATIDYLETHANOLAMINE
HETNAM EBM 2-IODO-N-(1-METHYLETHYL)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 HEM C34 H32 FE N4 O4
FORMUL 10 EPH C39 H68 N O8 P
FORMUL 11 EBM C10 H12 I N O
HELIX 1 1 GLY A 28 GLY A 42 1 15
HELIX 2 2 PHE A 52 SER A 56 5 5
HELIX 3 3 HIS A 57 ALA A 61 5 5
HELIX 4 4 ASN A 76 SER A 88 1 13
HELIX 5 5 ASP A 93 GLY A 115 1 23
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 GLU A 267 GLY A 273 1 7
HELIX 10 10 SER A 297 GLY A 312 1 16
HELIX 11 11 PRO A 330 LEU A 338 1 9
HELIX 12 12 LEU A 338 PHE A 348 1 11
HELIX 13 13 ASN A 413 GLU A 431 1 19
HELIX 14 14 GLY A 447 PHE A 459 1 13
HELIX 15 15 THR A 466 ALA A 481 1 16
HELIX 16 16 VAL A 486 ASP A 503 1 18
HELIX 17 17 ASN A 517 ARG A 543 1 27
HELIX 18 18 PRO A 575 HIS A 579 5 5
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 ASP B 133 GLU B 137 5 5
HELIX 22 22 SER B 145 LYS B 151 1 7
HELIX 23 23 CYS B 164 SER B 167 5 4
HELIX 24 24 CYS B 168 ASN B 174 1 7
HELIX 25 25 GLY B 180 TRP B 190 1 11
HELIX 26 26 PHE B 198 LYS B 205 1 8
HELIX 27 27 CYS B 221 CYS B 225 5 5
HELIX 28 28 ASN B 230 TYR B 245 1 16
HELIX 29 29 LYS C 9 LEU C 20 1 12
HELIX 30 30 SER C 36 LEU C 66 1 31
HELIX 31 31 ASN C 69 LEU C 80 1 12
HELIX 32 32 THR C 85 GLY C 114 1 30
HELIX 33 33 THR C 118 ALA C 142 1 25
HELIX 34 34 ALA D 38 GLY D 55 1 18
HELIX 35 35 LEU D 56 ASN D 63 1 8
HELIX 36 36 CYS D 65 VAL D 92 1 28
HELIX 37 37 ASP D 95 HIS D 122 1 28
HELIX 38 38 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 PHE A 174
SHEET 3 A 6 VAL A 15 VAL A 25 1 N ALA A 22 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 GLU A 188 CYS A 196 -1 N ALA A 194 O HIS A 203
SHEET 6 A 6 TYR A 177 GLU A 185 -1 N PHE A 178 O LEU A 195
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 PHE A 174
SHEET 3 B 6 VAL A 15 VAL A 25 1 N ALA A 22 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 VAL A 379 O VAL A 390
SHEET 1 C 3 ILE A 65 ASN A 66 0
SHEET 2 C 3 HIS A 145 CYS A 148 -1 O CYS A 148 N ILE A 65
SHEET 3 C 3 GLN A 128 ALA A 130 -1 N ARG A 129 O CYS A 147
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 HIS A 365 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 ILE A 358 N LEU A 324
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 2 PHE A 484 ARG A 485 0
SHEET 2 I 2 ALA A 551 ARG A 552 1 O ALA A 551 N ARG A 485
SHEET 1 J 5 HIS B 29 ASP B 36 0
SHEET 2 J 5 ILE B 11 ARG B 18 -1 N LYS B 12 O ILE B 35
SHEET 3 J 5 SER B 97 TYR B 100 1 O SER B 97 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
SHEET 1 K 2 VAL B 107 LYS B 109 0
SHEET 2 K 2 VAL B 112 PRO B 113 -1 O VAL B 112 N ILE B 108
LINK NE2 HIS A 57 C8M FAD A 700 1555 1555 2.01
LINK NE2 HIS C 101 FE HEM C1305 1555 1555 2.08
LINK SG CYS B 70 FE1 FES B 302 1555 1555 2.11
LINK SG CYS B 65 FE1 FES B 302 1555 1555 2.17
LINK SG CYS B 161 FE2 SF4 B 303 1555 1555 2.26
LINK NE2 HIS D 79 FE HEM C1305 1555 1555 2.32
LINK SG CYS B 158 FE1 SF4 B 303 1555 1555 2.42
LINK SG CYS B 215 FE1 F3S B 304 1555 1555 2.44
LINK SG CYS B 221 FE3 F3S B 304 1555 1555 2.46
LINK SG CYS B 225 FE3 SF4 B 303 1555 1555 2.60
LINK SG CYS B 164 FE4 SF4 B 303 1555 1555 2.61
LINK SG CYS B 168 FE4 F3S B 304 1555 1555 2.68
SITE 1 AC1 30 GLY A 26 ALA A 27 GLY A 28 GLY A 29
SITE 2 AC1 30 ALA A 30 THR A 49 LYS A 50 LEU A 51
SITE 3 AC1 30 SER A 56 HIS A 57 THR A 58 ALA A 60
SITE 4 AC1 30 ALA A 61 GLN A 62 GLY A 63 GLY A 64
SITE 5 AC1 30 TYR A 177 PHE A 178 ALA A 179 THR A 214
SITE 6 AC1 30 GLY A 215 THR A 225 SER A 226 ASP A 233
SITE 7 AC1 30 GLU A 398 ARG A 409 ALA A 412 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 8 CYS B 158 ILE B 159 CYS B 161 ALA B 162
SITE 2 AC3 8 CYS B 164 ALA B 182 CYS B 225 PRO B 226
SITE 1 AC4 10 CYS B 168 TYR B 178 PRO B 181 CYS B 215
SITE 2 AC4 10 HIS B 216 THR B 217 ILE B 218 MET B 219
SITE 3 AC4 10 ASN B 220 CYS B 221
SITE 1 AC5 12 HIS B 216 HIS C 45 ARG C 46 GLY C 49
SITE 2 AC5 12 LEU C 52 SER C 53 HIS C 101 HIS C 108
SITE 3 AC5 12 LEU D 53 LEU D 57 HIS D 79 GLY D 83
SITE 1 AC6 8 LEU C 140 ALA D 60 TYR D 61 LEU D 62
SITE 2 AC6 8 PRO D 64 CYS D 127 ALA D 131 TRP D 134
SITE 1 AC7 8 SER B 170 TRP B 173 HIS B 216 ILE B 218
SITE 2 AC7 8 SER C 42 ARG C 46 ASP D 90 TYR D 91
CRYST1 70.966 83.994 295.254 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 0.014091 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011906 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003387 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
