HEADER OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 04-FEB-10 3AE2
TITLE CRYSTAL STRUCTURE OF PORCINE HEART MITOCHONDRIAL COMPLEX II BOUND WITH
TITLE 2 2-HYDROXY-N-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 1 09-FEB-11 3AE2 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-HYDROXY-N-PHENYL-BENZAMIDE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 33385
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.204
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1688
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) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.17
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2195
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.40
REMARK 3 BIN R VALUE (WORKING SET) : 0.3100
REMARK 3 BIN FREE R VALUE SET COUNT : 127
REMARK 3 BIN FREE R VALUE : 0.3410
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 : 1
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.83
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.03000
REMARK 3 B22 (A**2) : 0.37000
REMARK 3 B33 (A**2) : -0.40000
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): 0.409
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.329
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 39.194
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.936
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8866 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 12019 ; 1.068 ; 1.992
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1 ; 0.139 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1088 ; 5.251 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 375 ;35.199 ;23.413
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1469 ;18.380 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 59 ;16.469 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1304 ; 0.077 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6658 ; 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 ; 0.194 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2 ; 0.001 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8676 ; 0.371 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3455 ; 0.502 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3326 ; 0.881 ; 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 : 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 69
REMARK 3 ORIGIN FOR THE GROUP (A): 22.9030 -26.6130 22.1160
REMARK 3 T TENSOR
REMARK 3 T11: 0.2664 T22: 0.2360
REMARK 3 T33: 0.4570 T12: -0.0294
REMARK 3 T13: 0.0444 T23: 0.1068
REMARK 3 L TENSOR
REMARK 3 L11: 4.4305 L22: 2.0416
REMARK 3 L33: 3.4014 L12: -1.6323
REMARK 3 L13: -0.8896 L23: 0.5468
REMARK 3 S TENSOR
REMARK 3 S11: -0.1126 S12: -0.3773 S13: -0.1654
REMARK 3 S21: -0.1495 S22: 0.0675 S23: -0.1948
REMARK 3 S31: 0.4552 S32: 0.4089 S33: 0.0452
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 70 A 260
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6070 -15.2360 16.9130
REMARK 3 T TENSOR
REMARK 3 T11: 0.2338 T22: 0.1603
REMARK 3 T33: 0.3975 T12: -0.0882
REMARK 3 T13: 0.0256 T23: -0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 1.9226 L22: 1.3548
REMARK 3 L33: 3.5147 L12: -0.3540
REMARK 3 L13: -0.4545 L23: -0.5172
REMARK 3 S TENSOR
REMARK 3 S11: 0.0038 S12: -0.0193 S13: 0.0877
REMARK 3 S21: -0.0633 S22: -0.0244 S23: 0.0558
REMARK 3 S31: -0.3361 S32: 0.0370 S33: 0.0206
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 261 A 340
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6980 9.4400 23.1440
REMARK 3 T TENSOR
REMARK 3 T11: 0.9038 T22: 0.0904
REMARK 3 T33: 0.7698 T12: -0.0844
REMARK 3 T13: 0.1062 T23: -0.0329
REMARK 3 L TENSOR
REMARK 3 L11: 5.2700 L22: 2.8451
REMARK 3 L33: 6.2245 L12: 0.8809
REMARK 3 L13: -2.5401 L23: -1.2885
REMARK 3 S TENSOR
REMARK 3 S11: 0.6345 S12: -0.0320 S13: 0.8943
REMARK 3 S21: 0.1808 S22: -0.2263 S23: -0.0178
REMARK 3 S31: -1.5771 S32: -0.0147 S33: -0.4081
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 341 A 429
REMARK 3 ORIGIN FOR THE GROUP (A): 21.7200 -11.7890 15.2360
REMARK 3 T TENSOR
REMARK 3 T11: 0.2598 T22: 0.2191
REMARK 3 T33: 0.4516 T12: -0.1268
REMARK 3 T13: 0.0114 T23: 0.0408
REMARK 3 L TENSOR
REMARK 3 L11: 1.4945 L22: 2.7687
REMARK 3 L33: 2.9620 L12: -0.6575
REMARK 3 L13: -0.9127 L23: 0.5772
REMARK 3 S TENSOR
REMARK 3 S11: 0.1138 S12: 0.0771 S13: 0.2098
REMARK 3 S21: 0.0556 S22: -0.1882 S23: 0.0009
REMARK 3 S31: -0.3959 S32: 0.1123 S33: 0.0744
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 514
REMARK 3 ORIGIN FOR THE GROUP (A): 42.3110 -15.9690 21.0310
REMARK 3 T TENSOR
REMARK 3 T11: 0.2109 T22: 0.7032
REMARK 3 T33: 0.4331 T12: -0.1404
REMARK 3 T13: 0.0540 T23: 0.0533
REMARK 3 L TENSOR
REMARK 3 L11: 2.8839 L22: 2.4039
REMARK 3 L33: 2.2381 L12: -0.2164
REMARK 3 L13: -0.6674 L23: 0.1035
REMARK 3 S TENSOR
REMARK 3 S11: -0.1408 S12: -0.3125 S13: 0.0448
REMARK 3 S21: -0.2818 S22: 0.0010 S23: -0.3618
REMARK 3 S31: -0.1392 S32: 1.1762 S33: 0.1398
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 515 A 622
REMARK 3 ORIGIN FOR THE GROUP (A): 30.8950 -5.9950 4.2220
REMARK 3 T TENSOR
REMARK 3 T11: 0.4776 T22: 0.2716
REMARK 3 T33: 0.4063 T12: -0.1766
REMARK 3 T13: 0.0955 T23: 0.0492
REMARK 3 L TENSOR
REMARK 3 L11: 2.7910 L22: 1.6559
REMARK 3 L33: 4.0811 L12: -0.3153
REMARK 3 L13: -0.2863 L23: -1.2039
REMARK 3 S TENSOR
REMARK 3 S11: 0.0260 S12: 0.2298 S13: 0.5165
REMARK 3 S21: -0.1914 S22: -0.1805 S23: -0.2608
REMARK 3 S31: -0.8916 S32: 0.6028 S33: 0.1544
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): 33.2000 -12.4740 46.0760
REMARK 3 T TENSOR
REMARK 3 T11: 0.2653 T22: 0.7124
REMARK 3 T33: 0.3624 T12: -0.2724
REMARK 3 T13: -0.0139 T23: -0.0320
REMARK 3 L TENSOR
REMARK 3 L11: 3.3648 L22: 3.4691
REMARK 3 L33: 3.5914 L12: 0.2369
REMARK 3 L13: -0.1055 L23: 0.9177
REMARK 3 S TENSOR
REMARK 3 S11: 0.0339 S12: -0.7376 S13: 0.3119
REMARK 3 S21: 0.4218 S22: -0.0877 S23: -0.3561
REMARK 3 S31: -0.4590 S32: 1.2679 S33: 0.0538
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): 6.3660 -24.4640 40.0670
REMARK 3 T TENSOR
REMARK 3 T11: 0.3323 T22: 0.1233
REMARK 3 T33: 0.4623 T12: -0.0558
REMARK 3 T13: 0.0651 T23: -0.0611
REMARK 3 L TENSOR
REMARK 3 L11: 2.4477 L22: 1.0741
REMARK 3 L33: 5.0001 L12: -0.2841
REMARK 3 L13: -1.4154 L23: -0.5364
REMARK 3 S TENSOR
REMARK 3 S11: -0.0295 S12: 0.1872 S13: -0.0151
REMARK 3 S21: 0.0915 S22: -0.1387 S23: 0.2891
REMARK 3 S31: 0.2769 S32: -0.4061 S33: 0.1682
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 65
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0990 -30.2850 58.2900
REMARK 3 T TENSOR
REMARK 3 T11: 0.7216 T22: 0.2945
REMARK 3 T33: 0.6293 T12: 0.0275
REMARK 3 T13: 0.0950 T23: 0.0788
REMARK 3 L TENSOR
REMARK 3 L11: 1.4336 L22: 0.6644
REMARK 3 L33: 4.4086 L12: 0.2706
REMARK 3 L13: -1.0335 L23: -0.6740
REMARK 3 S TENSOR
REMARK 3 S11: -0.2327 S12: -0.2452 S13: -0.0262
REMARK 3 S21: 0.2576 S22: 0.0276 S23: -0.0165
REMARK 3 S31: 0.5116 S32: 0.8116 S33: 0.2051
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 66 C 107
REMARK 3 ORIGIN FOR THE GROUP (A): 2.1870 -24.4570 85.2430
REMARK 3 T TENSOR
REMARK 3 T11: 1.1684 T22: 0.6608
REMARK 3 T33: 0.8344 T12: -0.1206
REMARK 3 T13: 0.1034 T23: 0.0322
REMARK 3 L TENSOR
REMARK 3 L11: 0.1645 L22: 4.5392
REMARK 3 L33: 6.0116 L12: -0.2955
REMARK 3 L13: 0.4505 L23: -4.0753
REMARK 3 S TENSOR
REMARK 3 S11: 0.1901 S12: -0.5478 S13: 0.0484
REMARK 3 S21: 1.2332 S22: -0.1510 S23: -0.0822
REMARK 3 S31: -1.2423 S32: 0.6925 S33: -0.0392
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 108 C 143
REMARK 3 ORIGIN FOR THE GROUP (A): 0.7700 -13.1220 65.7120
REMARK 3 T TENSOR
REMARK 3 T11: 0.6550 T22: 0.1404
REMARK 3 T33: 0.5806 T12: 0.0873
REMARK 3 T13: 0.2458 T23: -0.0139
REMARK 3 L TENSOR
REMARK 3 L11: 1.4967 L22: 6.5950
REMARK 3 L33: 9.6562 L12: 1.7518
REMARK 3 L13: 1.3828 L23: 1.0339
REMARK 3 S TENSOR
REMARK 3 S11: 0.3149 S12: -0.1277 S13: -0.1521
REMARK 3 S21: 0.3589 S22: -0.1197 S23: 0.0995
REMARK 3 S31: -1.0785 S32: -0.6318 S33: -0.1952
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 35 D 71
REMARK 3 ORIGIN FOR THE GROUP (A): -9.6720 -29.8810 66.6460
REMARK 3 T TENSOR
REMARK 3 T11: 0.3497 T22: 0.1205
REMARK 3 T33: 0.4457 T12: 0.0193
REMARK 3 T13: 0.1905 T23: 0.0321
REMARK 3 L TENSOR
REMARK 3 L11: 3.4485 L22: 4.6745
REMARK 3 L33: 13.1683 L12: 0.9683
REMARK 3 L13: -1.9797 L23: 2.2755
REMARK 3 S TENSOR
REMARK 3 S11: -0.3457 S12: 0.0146 S13: -0.5721
REMARK 3 S21: 0.1500 S22: -0.0199 S23: 0.3984
REMARK 3 S31: -0.5216 S32: -0.6708 S33: 0.3656
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 : D 72 D 96
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2600 -36.1660 64.1730
REMARK 3 T TENSOR
REMARK 3 T11: 0.7023 T22: 0.1586
REMARK 3 T33: 0.6524 T12: -0.0052
REMARK 3 T13: 0.1977 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 8.1409 L22: -0.1006
REMARK 3 L33: 6.5634 L12: 1.5044
REMARK 3 L13: -2.8826 L23: -3.1257
REMARK 3 S TENSOR
REMARK 3 S11: -0.2703 S12: 0.0316 S13: -0.5307
REMARK 3 S21: -0.2551 S22: -0.1769 S23: -0.0895
REMARK 3 S31: 0.9470 S32: 0.7586 S33: 0.4472
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 97 D 124
REMARK 3 ORIGIN FOR THE GROUP (A): -1.2720 -42.5090 74.8730
REMARK 3 T TENSOR
REMARK 3 T11: 0.8047 T22: 0.0273
REMARK 3 T33: 0.6171 T12: -0.0127
REMARK 3 T13: 0.2108 T23: 0.0825
REMARK 3 L TENSOR
REMARK 3 L11: 9.4550 L22: 3.6766
REMARK 3 L33: 10.5105 L12: -1.5618
REMARK 3 L13: -8.0375 L23: 2.0989
REMARK 3 S TENSOR
REMARK 3 S11: -0.0806 S12: -0.0738 S13: -0.7984
REMARK 3 S21: -0.1012 S22: -0.2718 S23: -0.0101
REMARK 3 S31: 0.0521 S32: -0.1733 S33: 0.3524
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 125 D 136
REMARK 3 ORIGIN FOR THE GROUP (A): -6.5420 -26.7000 88.3120
REMARK 3 T TENSOR
REMARK 3 T11: 1.2261 T22: 0.4997
REMARK 3 T33: 0.3718 T12: 0.0192
REMARK 3 T13: 0.1493 T23: 0.0076
REMARK 3 L TENSOR
REMARK 3 L11: 29.7554 L22: 7.1288
REMARK 3 L33: 2.2491 L12: -1.4710
REMARK 3 L13: -6.9737 L23: -0.1653
REMARK 3 S TENSOR
REMARK 3 S11: 1.0215 S12: -0.9905 S13: 0.1204
REMARK 3 S21: 1.7852 S22: -0.7750 S23: 0.7014
REMARK 3 S31: -0.8816 S32: -0.8578 S33: -0.2465
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 3AE2 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-FEB-10.
REMARK 100 THE RCSB ID CODE IS RCSB029136.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-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 : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33467
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : 0.08500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.2880
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.30
REMARK 200 R MERGE FOR SHELL (I) : 0.49800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.160
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 (%): 65.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.61
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 35.92750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 147.30750
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 42.10050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 147.30750
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.92750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 42.10050
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: 12600 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 42350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -51.0 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 -13.17 66.39
REMARK 500 SER A 56 150.20 -49.17
REMARK 500 GLN A 62 -53.27 -140.57
REMARK 500 MET A 72 -76.57 -88.32
REMARK 500 HIS A 145 79.11 -117.38
REMARK 500 ALA A 151 -137.51 57.01
REMARK 500 ASP A 170 39.78 -83.24
REMARK 500 LEU A 180 -66.77 -92.81
REMARK 500 THR A 256 77.72 -112.28
REMARK 500 ARG A 283 87.54 -68.66
REMARK 500 LYS A 293 -132.93 57.18
REMARK 500 ARG A 313 47.78 -93.34
REMARK 500 HIS A 321 -168.16 -123.26
REMARK 500 HIS A 365 -57.25 -143.43
REMARK 500 CYS A 401 82.62 -153.45
REMARK 500 SER A 403 76.52 29.42
REMARK 500 LYS A 544 63.65 -102.76
REMARK 500 GLN A 569 -96.24 -40.88
REMARK 500 ASN A 608 108.53 -160.53
REMARK 500 ARG B 10 81.79 -165.24
REMARK 500 SER B 64 -62.99 -144.11
REMARK 500 ASP B 110 -126.00 43.72
REMARK 500 GLU B 126 69.86 60.13
REMARK 500 HIS C 29 -83.41 -120.92
REMARK 500 ASP D 95 -72.96 -92.62
REMARK 500 LYS D 135 36.46 -77.95
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 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 65 SG
REMARK 620 2 FES B 302 S1 125.9
REMARK 620 3 FES B 302 S2 111.1 91.9
REMARK 620 4 CYS B 70 SG 113.1 98.1 115.1
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 90.6
REMARK 620 3 HEM C1305 NB 93.6 89.7
REMARK 620 4 HEM C1305 NC 88.2 178.3 89.2
REMARK 620 5 HEM C1305 ND 88.0 91.0 178.3 90.2
REMARK 620 6 HIS D 79 NE2 175.4 86.7 82.7 94.4 95.7
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 73 SG
REMARK 620 2 FES B 302 S1 112.5
REMARK 620 3 FES B 302 S2 128.5 92.2
REMARK 620 4 CYS B 85 SG 106.3 119.0 98.7
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 112.6
REMARK 620 3 F3S B 304 S3 123.0 98.8
REMARK 620 4 F3S B 304 S4 103.5 120.4 99.1
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 98.1
REMARK 620 3 F3S B 304 S2 107.8 121.0
REMARK 620 4 F3S B 304 S3 133.4 98.8 99.8
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 118.4
REMARK 620 3 SF4 B 303 S2 114.3 105.9
REMARK 620 4 SF4 B 303 S4 107.7 103.1 106.2
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 87.1
REMARK 620 3 F3S B 304 S3 90.6 101.2
REMARK 620 4 F3S B 304 S4 95.8 157.6 101.0
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 96.6
REMARK 620 3 SF4 B 303 S3 129.7 105.9
REMARK 620 4 SF4 B 303 S4 112.1 103.1 105.8
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 116.5
REMARK 620 3 SF4 B 303 S3 88.2 106.2
REMARK 620 4 SF4 B 303 S4 129.9 105.7 105.2
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 98.6
REMARK 620 3 SF4 B 303 S2 123.4 105.8
REMARK 620 4 SF4 B 303 S3 115.2 105.5 106.2
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 MLI A 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPH D 1306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SLI 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: 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: 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 3AE2 A 1 622 UNP Q0QF01 DHSA_PIG 43 664
DBREF 3AE2 B 1 252 UNP Q007T0 DHSB_PIG 29 280
DBREF 3AE2 C 4 143 UNP D0VWV4 C560_PIG 30 169
DBREF 3AE2 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 MLI A 701 7
HET HEM C1305 43
HET EPH D1306 44
HET SLI C1201 16
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM F3S FE3-S4 CLUSTER
HETNAM MLI MALONATE ION
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM EPH L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-
HETNAM 2 EPH PHOSPHATIDYLETHANOLAMINE
HETNAM SLI 2-HYDROXY-N-PHENYLBENZAMIDE
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 MLI C3 H2 O4 2-
FORMUL 10 HEM C34 H32 FE N4 O4
FORMUL 11 EPH C39 H68 N O8 P
FORMUL 12 SLI C13 H11 N O2
FORMUL 13 HOH *(H2 O)
HELIX 1 1 GLY A 28 ALA A 41 1 14
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 GLY A 115 1 23
HELIX 5 5 ARG A 153 LEU A 167 1 15
HELIX 6 6 TYR A 217 TYR A 221 5 5
HELIX 7 7 GLY A 232 ALA A 241 1 10
HELIX 8 8 GLU A 267 GLY A 273 1 7
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 GLU A 311 1 15
HELIX 12 12 PRO A 330 LEU A 338 1 9
HELIX 13 13 LEU A 338 GLY A 350 1 13
HELIX 14 14 ASN A 413 GLU A 431 1 19
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 PRO A 575 HIS A 579 5 5
HELIX 20 20 ASN B 38 CYS B 40 5 3
HELIX 21 21 MET B 43 ILE B 55 1 13
HELIX 22 22 LEU B 115 SER B 124 1 10
HELIX 23 23 ASP B 133 GLU B 137 5 5
HELIX 24 24 SER B 145 LYS B 151 1 7
HELIX 25 25 CYS B 164 SER B 167 5 4
HELIX 26 26 CYS B 168 GLY B 175 1 8
HELIX 27 27 LEU B 179 ILE B 192 1 14
HELIX 28 28 PHE B 198 LYS B 205 1 8
HELIX 29 29 MET B 219 CYS B 225 1 7
HELIX 30 30 ASN B 230 TYR B 245 1 16
HELIX 31 31 THR C 7 GLY C 21 1 15
HELIX 32 32 SER C 36 LEU C 66 1 31
HELIX 33 33 ASN C 69 CYS C 81 1 13
HELIX 34 34 PRO C 84 LEU C 113 1 30
HELIX 35 35 THR C 118 ALA C 142 1 25
HELIX 36 36 LYS D 37 ASN D 63 1 27
HELIX 37 37 CYS D 65 VAL D 92 1 28
HELIX 38 38 ASP D 95 ASP D 123 1 29
HELIX 39 39 VAL D 124 LYS D 135 1 12
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 LEU A 180 O ILE A 193
SHEET 1 B 6 SER A 172 VAL A 175 0
SHEET 2 B 6 THR A 45 THR A 49 1 N THR A 45 O SER A 172
SHEET 3 B 6 ALA A 22 VAL A 25 1 N VAL A 24 O VAL A 48
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 VAL A 212
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 ASP A 589 -1 O SER A 586 N CYS A 245
SHEET 3 D 3 LYS A 594 PRO A 601 -1 O ARG A 600 N HIS A 583
SHEET 1 E 4 VAL A 251 ILE A 258 0
SHEET 2 E 4 ILE A 358 ASN A 367 -1 O TYR A 366 N GLN A 252
SHEET 3 E 4 VAL A 322 GLN A 325 -1 N VAL A 322 O VAL A 360
SHEET 4 E 4 ILE A 275 ILE A 277 -1 N ILE A 275 O GLN A 325
SHEET 1 F 2 ILE A 371 PRO A 372 0
SHEET 2 F 2 ALA A 400 CYS A 401 1 O CYS A 401 N ILE A 371
SHEET 1 G 2 ILE A 464 ARG A 465 0
SHEET 2 G 2 LEU A 507 LYS A 508 1 O LYS A 508 N ILE A 464
SHEET 1 H 2 PHE A 484 ARG A 485 0
SHEET 2 H 2 ALA A 551 ARG A 552 1 O ALA A 551 N ARG A 485
SHEET 1 I 5 HIS B 29 ASP B 36 0
SHEET 2 I 5 ILE B 11 ARG B 18 -1 N ARG B 18 O HIS B 29
SHEET 3 I 5 SER B 97 TYR B 100 1 O SER B 97 N ALA B 15
SHEET 4 I 5 ALA B 74 ILE B 77 -1 N ASN B 76 O TYR B 100
SHEET 5 I 5 GLY B 80 LEU B 83 -1 O THR B 82 N MET B 75
SHEET 1 J 2 VAL B 107 LYS B 109 0
SHEET 2 J 2 VAL B 112 PRO B 113 -1 O VAL B 112 N LYS B 109
LINK NE2 HIS A 57 C8M FAD A 700 1555 1555 1.95
LINK SG CYS B 65 FE2 FES B 302 1555 1555 2.03
LINK NE2 HIS C 101 FE HEM C1305 1555 1555 2.10
LINK NE2 HIS D 79 FE HEM C1305 1555 1555 2.20
LINK SG CYS B 73 FE1 FES B 302 1555 1555 2.22
LINK SG CYS B 70 FE2 FES B 302 1555 1555 2.22
LINK SG CYS B 221 FE3 F3S B 304 1555 1555 2.23
LINK SG CYS B 215 FE1 F3S B 304 1555 1555 2.25
LINK SG CYS B 225 FE3 SF4 B 303 1555 1555 2.31
LINK SG CYS B 168 FE4 F3S B 304 1555 1555 2.32
LINK SG CYS B 161 FE2 SF4 B 303 1555 1555 2.33
LINK SG CYS B 158 FE1 SF4 B 303 1555 1555 2.38
LINK SG CYS B 164 FE4 SF4 B 303 1555 1555 2.39
LINK SG CYS B 85 FE1 FES B 302 1555 1555 2.45
SITE 1 AC1 36 GLY A 26 ALA A 27 GLY A 28 GLY A 29
SITE 2 AC1 36 ALA A 30 VAL A 48 THR A 49 LYS A 50
SITE 3 AC1 36 LEU A 51 SER A 56 HIS A 57 THR A 58
SITE 4 AC1 36 ALA A 60 ALA A 61 GLN A 62 GLY A 63
SITE 5 AC1 36 GLY A 64 TYR A 177 PHE A 178 ALA A 179
SITE 6 AC1 36 THR A 214 GLY A 215 THR A 225 ASP A 233
SITE 7 AC1 36 LEU A 264 HIS A 365 TYR A 366 GLY A 397
SITE 8 AC1 36 GLU A 398 ARG A 409 ALA A 412 ASN A 413
SITE 9 AC1 36 SER A 414 LEU A 415 LEU A 418 MLI A 701
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 LEU B 160 CYS B 161
SITE 2 AC3 8 CYS B 163 CYS B 164 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 GLN A 62 GLY A 63 PHE A 131 HIS A 254
SITE 2 AC5 12 LEU A 264 THR A 266 GLU A 267 ARG A 298
SITE 3 AC5 12 HIS A 365 ARG A 409 ALA A 412 FAD A 700
SITE 1 AC6 13 HIS C 45 ARG C 46 GLY C 49 LEU C 52
SITE 2 AC6 13 SER C 53 HIS C 101 HIS C 108 SLI C1201
SITE 3 AC6 13 ARG D 47 LEU D 53 LEU D 54 HIS D 79
SITE 4 AC6 13 GLY D 83
SITE 1 AC7 2 TYR D 61 TRP D 134
SITE 1 AC8 7 HIS B 216 HOH B1202 SER C 42 ILE C 43
SITE 2 AC8 7 ARG C 46 HEM C1305 TYR D 91
CRYST1 71.855 84.201 294.615 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 0.013917 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011876 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003394 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
