HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10 3AE8
TITLE CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE 2 N-(3-ISOPROPOXY-PHENYL)-2-TRIFLUOROMETHYLBENZAMIDE
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 3AE8 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 N-(3-ISOPROPOXY-PHENYL)-2-
JRNL TITL 3 TRIFLUOROMETHYLBENZAMIDE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.40 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) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.6
REMARK 3 NUMBER OF REFLECTIONS : 21173
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) : 0.242
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.288
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1067
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) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1493
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.3480
REMARK 3 BIN FREE R VALUE SET COUNT : 80
REMARK 3 BIN FREE R VALUE : 0.3800
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 : 182
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) : 99.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.46000
REMARK 3 B22 (A**2) : -0.03000
REMARK 3 B33 (A**2) : -0.43000
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): 0.695
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.502
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 65.844
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.902
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.878
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8867 ; 0.005 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12024 ; 0.853 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1088 ; 3.909 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 375 ;33.474 ;23.413
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1469 ;15.376 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ; 9.797 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1306 ; 0.054 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6652 ; 0.003 ; 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): 5411 ; 0.089 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8676 ; 0.160 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3456 ; 0.095 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3331 ; 0.177 ; 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): 16.7220 -17.5080 -18.0590
REMARK 3 T TENSOR
REMARK 3 T11: 0.0574 T22: 0.3183
REMARK 3 T33: 0.3952 T12: 0.1058
REMARK 3 T13: -0.0176 T23: -0.0400
REMARK 3 L TENSOR
REMARK 3 L11: 2.1213 L22: 1.2571
REMARK 3 L33: 3.7662 L12: 0.4874
REMARK 3 L13: -0.6274 L23: 0.5079
REMARK 3 S TENSOR
REMARK 3 S11: 0.0172 S12: 0.1139 S13: -0.0141
REMARK 3 S21: 0.0425 S22: -0.0930 S23: -0.0394
REMARK 3 S31: -0.4319 S32: -0.0937 S33: 0.0757
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 349
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4220 8.8360 -24.3360
REMARK 3 T TENSOR
REMARK 3 T11: 1.1478 T22: 0.3665
REMARK 3 T33: 0.7200 T12: 0.0770
REMARK 3 T13: 0.2820 T23: 0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 4.0335 L22: 1.5008
REMARK 3 L33: -1.2844 L12: 0.6122
REMARK 3 L13: 0.7575 L23: 1.0477
REMARK 3 S TENSOR
REMARK 3 S11: 0.4390 S12: 0.3364 S13: 0.9952
REMARK 3 S21: -0.5650 S22: -0.2087 S23: -0.2676
REMARK 3 S31: -0.6333 S32: 0.0212 S33: -0.2303
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 350 A 622
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2070 -10.7020 -11.6480
REMARK 3 T TENSOR
REMARK 3 T11: 0.1260 T22: 0.3447
REMARK 3 T33: 0.3395 T12: 0.1797
REMARK 3 T13: 0.0319 T23: -0.0879
REMARK 3 L TENSOR
REMARK 3 L11: 2.1885 L22: 1.7125
REMARK 3 L33: 3.3459 L12: 0.3100
REMARK 3 L13: 0.0310 L23: 0.7405
REMARK 3 S TENSOR
REMARK 3 S11: -0.0429 S12: 0.0322 S13: 0.2210
REMARK 3 S21: 0.0964 S22: -0.0493 S23: 0.1980
REMARK 3 S31: -0.6510 S32: -0.5507 S33: 0.0922
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): 2.8590 -11.6230 -46.0170
REMARK 3 T TENSOR
REMARK 3 T11: 0.1035 T22: 0.6284
REMARK 3 T33: 0.3404 T12: 0.2734
REMARK 3 T13: -0.0809 T23: -0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 3.1517 L22: 3.5434
REMARK 3 L33: 5.8373 L12: -0.1101
REMARK 3 L13: 0.1871 L23: 0.6450
REMARK 3 S TENSOR
REMARK 3 S11: -0.3264 S12: 0.4507 S13: 0.3161
REMARK 3 S21: -0.3743 S22: 0.0576 S23: 0.2564
REMARK 3 S31: -0.4518 S32: -1.0119 S33: 0.2687
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): 29.5910 -24.1700 -40.1890
REMARK 3 T TENSOR
REMARK 3 T11: 0.2139 T22: 0.2557
REMARK 3 T33: 0.5184 T12: 0.0352
REMARK 3 T13: 0.0559 T23: 0.0911
REMARK 3 L TENSOR
REMARK 3 L11: 2.0036 L22: 0.3302
REMARK 3 L33: 4.5226 L12: 0.6026
REMARK 3 L13: -1.7824 L23: 0.6072
REMARK 3 S TENSOR
REMARK 3 S11: -0.0486 S12: -0.1982 S13: -0.0331
REMARK 3 S21: -0.0872 S22: -0.0470 S23: -0.1780
REMARK 3 S31: 0.1269 S32: 0.5302 S33: 0.0955
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 38
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6390 -29.4490 -48.2660
REMARK 3 T TENSOR
REMARK 3 T11: 0.5707 T22: 0.5907
REMARK 3 T33: 0.4127 T12: 0.0119
REMARK 3 T13: 0.2048 T23: -0.2179
REMARK 3 L TENSOR
REMARK 3 L11: 6.3987 L22: 4.0368
REMARK 3 L33: 1.4789 L12: 2.2298
REMARK 3 L13: 1.1675 L23: -2.0180
REMARK 3 S TENSOR
REMARK 3 S11: -0.5199 S12: 0.0607 S13: -0.2940
REMARK 3 S21: -1.2807 S22: 0.3442 S23: -0.2752
REMARK 3 S31: 0.7366 S32: -1.0567 S33: 0.1757
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 39 C 63
REMARK 3 ORIGIN FOR THE GROUP (A): 29.8460 -28.6410 -72.9500
REMARK 3 T TENSOR
REMARK 3 T11: 1.0811 T22: -0.0130
REMARK 3 T33: 0.3730 T12: 0.1407
REMARK 3 T13: 0.1143 T23: -0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 2.1873 L22: 0.0561
REMARK 3 L33: 4.8425 L12: 0.7923
REMARK 3 L13: 2.1668 L23: -4.4266
REMARK 3 S TENSOR
REMARK 3 S11: -0.3527 S12: 0.0927 S13: -0.2688
REMARK 3 S21: -0.6152 S22: -0.1666 S23: 0.3338
REMARK 3 S31: -0.4783 S32: -0.0386 S33: 0.5192
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 64 C 88
REMARK 3 ORIGIN FOR THE GROUP (A): 33.9580 -29.6880 -94.1330
REMARK 3 T TENSOR
REMARK 3 T11: 1.1942 T22: 0.6955
REMARK 3 T33: 1.0139 T12: -0.0149
REMARK 3 T13: -0.1707 T23: -0.1994
REMARK 3 L TENSOR
REMARK 3 L11: 0.2670 L22: -4.3112
REMARK 3 L33: 25.3436 L12: -1.5549
REMARK 3 L13: -7.7085 L23: -2.6176
REMARK 3 S TENSOR
REMARK 3 S11: -0.1180 S12: 1.5754 S13: 0.3662
REMARK 3 S21: -1.2877 S22: -0.5309 S23: 0.4135
REMARK 3 S31: 1.0339 S32: 0.0807 S33: 0.6489
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 89 C 143
REMARK 3 ORIGIN FOR THE GROUP (A): 34.5690 -14.9020 -69.2340
REMARK 3 T TENSOR
REMARK 3 T11: 0.6857 T22: 0.0840
REMARK 3 T33: 0.5201 T12: -0.0413
REMARK 3 T13: 0.2368 T23: 0.0222
REMARK 3 L TENSOR
REMARK 3 L11: 2.6545 L22: 2.5820
REMARK 3 L33: 0.9179 L12: -0.6894
REMARK 3 L13: -0.6222 L23: -0.9262
REMARK 3 S TENSOR
REMARK 3 S11: 0.4815 S12: -0.0081 S13: 0.0728
REMARK 3 S21: -0.3479 S22: 0.0602 S23: -0.2617
REMARK 3 S31: -0.4072 S32: -0.0482 S33: -0.5417
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 35 D 70
REMARK 3 ORIGIN FOR THE GROUP (A): 45.3940 -29.3390 -66.7720
REMARK 3 T TENSOR
REMARK 3 T11: 0.1826 T22: 0.3741
REMARK 3 T33: 0.4292 T12: -0.0649
REMARK 3 T13: 0.1232 T23: 0.0174
REMARK 3 L TENSOR
REMARK 3 L11: 1.8033 L22: 6.4571
REMARK 3 L33: 4.7402 L12: -1.7547
REMARK 3 L13: -0.3881 L23: -0.8914
REMARK 3 S TENSOR
REMARK 3 S11: -0.0976 S12: -0.1459 S13: -0.2772
REMARK 3 S21: -0.0601 S22: -0.0393 S23: -0.4969
REMARK 3 S31: -0.5102 S32: 0.5660 S33: 0.1369
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 71 D 96
REMARK 3 ORIGIN FOR THE GROUP (A): 32.0360 -35.4690 -64.7460
REMARK 3 T TENSOR
REMARK 3 T11: 0.6376 T22: 0.0307
REMARK 3 T33: 0.5027 T12: 0.0537
REMARK 3 T13: 0.1116 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: -0.4528 L22: 4.1732
REMARK 3 L33: 1.0954 L12: -4.7787
REMARK 3 L13: 4.9530 L23: 3.0150
REMARK 3 S TENSOR
REMARK 3 S11: 0.0927 S12: -0.2884 S13: -0.4005
REMARK 3 S21: 0.4811 S22: -0.1716 S23: 0.5110
REMARK 3 S31: 0.5996 S32: -0.3884 S33: 0.0789
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 97 D 136
REMARK 3 ORIGIN FOR THE GROUP (A): 38.6810 -37.1810 -79.1340
REMARK 3 T TENSOR
REMARK 3 T11: 0.5790 T22: 0.1531
REMARK 3 T33: 0.5538 T12: 0.0135
REMARK 3 T13: 0.2540 T23: -0.0365
REMARK 3 L TENSOR
REMARK 3 L11: 3.6901 L22: 3.1890
REMARK 3 L33: 5.7424 L12: -2.6538
REMARK 3 L13: -0.5106 L23: 3.8084
REMARK 3 S TENSOR
REMARK 3 S11: -0.3737 S12: 0.2097 S13: -0.2661
REMARK 3 S21: -0.0285 S22: -0.1209 S23: -0.1339
REMARK 3 S31: 0.2912 S32: 0.4377 S33: 0.4946
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 3AE8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-FEB-10.
REMARK 100 THE RCSB ID CODE IS RCSB029142.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUN-08
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 : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.90000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAC SCIENCE DIP-2040
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21305
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
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 (%) : 83.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.08600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2680
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.52
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.5
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.44000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.280
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 (%): 65.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 25MM HEPES-NAOH, 8% 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 35.82750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 147.65850
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 147.65850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.82750
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: 12930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 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 -3.72 61.81
REMARK 500 THR A 121 -167.35 -122.44
REMARK 500 VAL A 150 70.19 -102.31
REMARK 500 ALA A 151 61.76 39.13
REMARK 500 ASP A 170 39.42 -82.22
REMARK 500 LYS A 293 -128.05 59.57
REMARK 500 LEU A 295 50.02 -99.30
REMARK 500 ARG A 313 57.60 -97.47
REMARK 500 LYS A 319 77.36 56.75
REMARK 500 ASP A 320 -33.77 -142.67
REMARK 500 HIS A 365 -58.58 -130.33
REMARK 500 ALA A 481 50.16 -114.37
REMARK 500 ALA A 482 -155.84 -78.10
REMARK 500 TRP A 516 72.64 45.25
REMARK 500 LYS A 544 56.90 -106.23
REMARK 500 GLN A 569 -64.75 -169.32
REMARK 500 GLN A 577 30.49 -89.18
REMARK 500 THR B 24 82.33 52.77
REMARK 500 GLU B 54 -55.28 -124.81
REMARK 500 SER B 64 -80.77 -153.72
REMARK 500 ARG B 66 21.94 45.30
REMARK 500 CYS B 70 -36.51 -134.35
REMARK 500 LYS B 109 -153.70 -149.87
REMARK 500 LEU B 111 14.30 59.12
REMARK 500 GLU B 126 80.05 63.94
REMARK 500 LYS B 139 -35.35 -139.62
REMARK 500 PHE B 198 49.51 -89.19
REMARK 500 TYR B 213 20.06 -77.28
REMARK 500 MET B 219 36.29 71.69
REMARK 500 HIS C 29 -71.25 -119.19
REMARK 500 PRO D 64 53.76 -90.20
REMARK 500 ASP D 95 -7.93 62.52
REMARK 500 ALA D 96 -45.40 -147.67
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 FES B 302 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 70 SG
REMARK 620 2 FES B 302 S1 115.7
REMARK 620 3 FES B 302 S2 114.2 90.1
REMARK 620 4 CYS B 65 SG 106.9 107.1 122.1
REMARK 620 N 1 2 3
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 73 SG
REMARK 620 2 FES B 302 S1 123.5
REMARK 620 3 FES B 302 S2 113.1 90.2
REMARK 620 4 CYS B 85 SG 103.8 102.8 124.5
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 161 SG
REMARK 620 2 SF4 B 303 S1 116.5
REMARK 620 3 SF4 B 303 S2 112.1 105.2
REMARK 620 4 SF4 B 303 S4 112.0 105.0 105.0
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 164 SG
REMARK 620 2 SF4 B 303 S2 121.8
REMARK 620 3 SF4 B 303 S3 112.0 105.5
REMARK 620 4 SF4 B 303 S4 105.9 104.9 105.5
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 168 SG
REMARK 620 2 F3S B 304 S1 112.5
REMARK 620 3 F3S B 304 S2 109.0 116.5
REMARK 620 4 F3S B 304 S3 117.3 101.3 99.8
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 D 79 NE2
REMARK 620 2 HEM C1305 NA 92.5
REMARK 620 3 HEM C1305 NB 89.3 88.9
REMARK 620 4 HEM C1305 NC 93.0 174.4 90.2
REMARK 620 5 HEM C1305 ND 92.1 90.9 178.6 90.0
REMARK 620 6 HIS C 101 NE2 172.1 90.7 98.0 83.9 80.7
REMARK 620 N 1 2 3 4 5
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 127.4
REMARK 620 3 SF4 B 303 S2 107.4 105.1
REMARK 620 4 SF4 B 303 S3 104.7 105.0 105.5
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 107.1
REMARK 620 3 F3S B 304 S3 134.6 101.4
REMARK 620 4 F3S B 304 S4 99.5 114.6 99.8
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 FTN 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: 3AE7 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
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 3AE8 A 1 622 UNP Q0QF01 DHSA_PIG 43 664
DBREF 3AE8 B 1 252 UNP Q007T0 DHSB_PIG 29 280
DBREF 3AE8 C 4 143 UNP D0VWV4 C560_PIG 30 169
DBREF 3AE8 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 FTN B1201 23
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 FTN N-[3-(1-METHYLETHOXY)PHENYL]-2-(TRIFLUOROMETHYL)
HETNAM 2 FTN BENZAMIDE
HETSYN HEM HEME
HETSYN FTN N-(3-ISOPROPOXY-PHENYL)-2-TRIFLUOROMETHYLBENZAMIDE
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 FTN C17 H16 F3 N O2
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 LYS A 137 LYS A 140 5 4
HELIX 7 7 ARG A 153 LEU A 167 1 15
HELIX 8 8 TYR A 217 TYR A 221 5 5
HELIX 9 9 GLY A 234 ALA A 241 1 8
HELIX 10 10 GLU A 267 GLY A 273 1 7
HELIX 11 11 PHE A 284 ALA A 289 1 6
HELIX 12 12 SER A 297 GLU A 311 1 15
HELIX 13 13 PRO A 330 ALA A 335 1 6
HELIX 14 14 LEU A 338 ALA A 349 1 12
HELIX 15 15 ASN A 413 GLU A 431 1 19
HELIX 16 16 GLY A 447 PHE A 459 1 13
HELIX 17 17 THR A 466 ALA A 481 1 16
HELIX 18 18 VAL A 486 GLY A 502 1 17
HELIX 19 19 ASN A 517 ARG A 543 1 27
HELIX 20 20 ASN B 38 CYS B 40 5 3
HELIX 21 21 MET B 43 GLU B 54 1 12
HELIX 22 22 LEU B 115 ILE B 125 1 11
HELIX 23 23 SER B 145 GLU B 150 1 6
HELIX 24 24 ALA B 162 CYS B 168 1 7
HELIX 25 25 CYS B 168 ASN B 174 1 7
HELIX 26 26 GLY B 180 TRP B 190 1 11
HELIX 27 27 PHE B 198 LYS B 205 1 8
HELIX 28 28 MET B 219 CYS B 225 1 7
HELIX 29 29 ASN B 230 ALA B 243 1 14
HELIX 30 30 THR C 7 LEU C 20 1 14
HELIX 31 31 SER C 36 LEU C 66 1 31
HELIX 32 32 ASN C 69 LEU C 80 1 12
HELIX 33 33 GLY C 83 LEU C 113 1 31
HELIX 34 34 THR C 118 ALA C 142 1 25
HELIX 35 35 LYS D 37 ASN D 63 1 27
HELIX 36 36 CYS D 65 VAL D 92 1 28
HELIX 37 37 ALA D 96 ASP D 123 1 28
HELIX 38 38 GLY D 125 LYS D 135 1 11
SHEET 1 A 4 VAL A 15 GLU A 19 0
SHEET 2 A 4 ILE A 202 ARG A 206 1 O ARG A 204 N HIS A 18
SHEET 3 A 4 GLU A 188 CYS A 196 -1 N ALA A 194 O HIS A 203
SHEET 4 A 4 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 ALA A 22 VAL A 25 1 N ALA A 22 O ALA A 46
SHEET 4 B 6 ASN A 209 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 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 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 SER A 596 N TYR A 587
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 PHE B 14 O TYR B 33
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 GLY B 80 LEU B 83 -1 O GLY B 80 N ILE B 77
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 1.99
LINK SG CYS B 70 FE1 FES B 302 1555 1555 2.09
LINK SG CYS B 73 FE2 FES B 302 1555 1555 2.11
LINK SG CYS B 161 FE3 SF4 B 303 1555 1555 2.11
LINK SG CYS B 164 FE1 SF4 B 303 1555 1555 2.15
LINK SG CYS B 168 FE1 F3S B 304 1555 1555 2.15
LINK NE2 HIS D 79 FE HEM C1305 1555 1555 2.16
LINK SG CYS B 158 FE4 SF4 B 303 1555 1555 2.29
LINK NE2 HIS C 101 FE HEM C1305 1555 1555 2.30
LINK SG CYS B 65 FE1 FES B 302 1555 1555 2.34
LINK SG CYS B 85 FE2 FES B 302 1555 1555 2.45
LINK SG CYS B 221 FE3 F3S B 304 1555 1555 2.47
SITE 1 AC1 29 GLY A 26 GLY A 28 GLY A 29 ALA A 30
SITE 2 AC1 29 THR A 49 LYS A 50 LEU A 51 SER A 56
SITE 3 AC1 29 HIS A 57 THR A 58 ALA A 60 ALA A 61
SITE 4 AC1 29 GLN A 62 GLY A 63 GLY A 64 TYR A 177
SITE 5 AC1 29 PHE A 178 ALA A 179 GLY A 215 THR A 225
SITE 6 AC1 29 ASP A 233 LEU A 264 TYR A 366 GLU A 398
SITE 7 AC1 29 ARG A 409 ALA A 412 SER A 414 LEU A 415
SITE 8 AC1 29 LEU A 418
SITE 1 AC2 7 SER B 64 CYS B 65 ARG B 66 CYS B 70
SITE 2 AC2 7 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 8 CYS B 168 TYR B 178 PRO B 181 CYS B 215
SITE 2 AC4 8 HIS B 216 MET B 219 ASN B 220 CYS B 221
SITE 1 AC5 14 HIS C 45 ARG C 46 GLY C 49 LEU C 52
SITE 2 AC5 14 SER C 53 HIS C 101 HIS C 108 ARG D 47
SITE 3 AC5 14 LEU D 53 LEU D 54 LEU D 57 LEU D 76
SITE 4 AC5 14 HIS D 79 GLY D 83
SITE 1 AC6 6 MET C 143 ALA D 60 TYR D 61 CYS D 127
SITE 2 AC6 6 ALA D 131 TRP D 134
SITE 1 AC7 12 PRO B 169 SER B 170 TRP B 173 HIS B 216
SITE 2 AC7 12 ILE B 218 ILE C 30 TRP C 35 SER C 42
SITE 3 AC7 12 ILE C 43 ARG C 46 ASP D 90 TYR D 91
CRYST1 71.655 83.994 295.317 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 0.013956 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011906 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003386 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
