HEADER OXIDOREDUCTASE 03-SEP-09 2WS3
TITLE CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE
TITLE 2 (SQR) SDHD TYR83PHE MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT;
COMPND 3 CHAIN: A, E, I;
COMPND 4 EC: 1.3.99.1;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: FAD ATOM C8M IS COVALENTLY LINKED TO NE2 OF SDHA
COMPND 7 HIS45;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT;
COMPND 10 CHAIN: B, F, J;
COMPND 11 EC: 1.3.99.1;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: SUCCINATE DEHYDROGENASE CYTOCHROME B-556 SUBUNIT;
COMPND 15 CHAIN: C, G, K;
COMPND 16 SYNONYM: CYTOCHROME B-556;
COMPND 17 EC: 1.3.5.1;
COMPND 18 ENGINEERED: YES;
COMPND 19 OTHER_DETAILS: RESIDUES 8-128 MODELLED;
COMPND 20 MOL_ID: 4;
COMPND 21 MOLECULE: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR
COMPND 22 SUBUNIT;
COMPND 23 CHAIN: D, H, L;
COMPND 24 EC: 1.3.5.1;
COMPND 25 ENGINEERED: YES;
COMPND 26 MUTATION: YES;
COMPND 27 OTHER_DETAILS: RESIDUES 11-115 MODELLED
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: DW35;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PFAS;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 11 ORGANISM_TAXID: 562;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 EXPRESSION_SYSTEM_STRAIN: DW35;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: PFAS;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 19 ORGANISM_TAXID: 562;
SOURCE 20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 21 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 22 EXPRESSION_SYSTEM_STRAIN: DW35;
SOURCE 23 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 24 EXPRESSION_SYSTEM_PLASMID: PFAS;
SOURCE 25 MOL_ID: 4;
SOURCE 26 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 27 ORGANISM_TAXID: 562;
SOURCE 28 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 29 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 30 EXPRESSION_SYSTEM_STRAIN: DW35;
SOURCE 31 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 32 EXPRESSION_SYSTEM_PLASMID: PFAS
KEYWDS ELECTRON TRANSPORT, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.RUPRECHT,V.YANKOVSKAYA,E.MAKLASHINA,S.IWATA,G.CECCHINI
REVDAT 4 20-DEC-23 2WS3 1 REMARK LINK
REVDAT 3 29-SEP-10 2WS3 1 DBREF
REVDAT 2 22-SEP-10 2WS3 1 DBREF
REVDAT 1 25-AUG-10 2WS3 0
JRNL AUTH J.RUPRECHT,V.YANKOVSKAYA,E.MAKLASHINA,S.IWATA,G.CECCHINI
JRNL TITL SUCCINATE DEHYDROGENASE ACTIVITY
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 3.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0072
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.03
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 71105
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : IDENTICAL TO 2WDQ
REMARK 3 R VALUE (WORKING + TEST SET) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.253
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3797
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.28
REMARK 3 REFLECTION IN BIN (WORKING SET) : 5162
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.84
REMARK 3 BIN R VALUE (WORKING SET) : 0.3000
REMARK 3 BIN FREE R VALUE SET COUNT : 289
REMARK 3 BIN FREE R VALUE : 0.3300
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 24477
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 423
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) : 72.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -4.70000
REMARK 3 B22 (A**2) : 1.19000
REMARK 3 B33 (A**2) : 3.51000
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): 0.487
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.412
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 52.792
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.911
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.885
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 25501 ; 0.012 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 34581 ; 1.301 ; 1.989
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 3144 ; 5.420 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 1107 ;33.907 ;23.388
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 4200 ;16.248 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 192 ;17.774 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 3831 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 19230 ; 0.005 ; 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): 15636 ; 0.139 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 25125 ; 0.230 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 9865 ; 0.638 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 9405 ; 0.869 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 4
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A E I
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 588 1
REMARK 3 1 E 1 E 588 1
REMARK 3 1 I 1 I 588 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 4522 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 E (A): 4522 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 1 I (A): 4522 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 1 A (A**2): 4522 ; 0.08 ; 0.50
REMARK 3 TIGHT THERMAL 1 E (A**2): 4522 ; 0.07 ; 0.50
REMARK 3 TIGHT THERMAL 1 I (A**2): 4522 ; 0.07 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : B F J
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 B 1 B 238 1
REMARK 3 1 F 1 F 238 1
REMARK 3 1 J 1 J 238 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 2 B (A): 1869 ; 0.05 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 F (A): 1869 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 2 J (A): 1869 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 2 B (A**2): 1869 ; 0.10 ; 0.50
REMARK 3 TIGHT THERMAL 2 F (A**2): 1869 ; 0.07 ; 0.50
REMARK 3 TIGHT THERMAL 2 J (A**2): 1869 ; 0.08 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
REMARK 3 CHAIN NAMES : C G K
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 8 C 128 1
REMARK 3 1 G 8 G 128 1
REMARK 3 1 K 8 K 128 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 3 C (A): 933 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 G (A): 933 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 3 K (A): 933 ; 0.04 ; 0.05
REMARK 3 TIGHT THERMAL 3 C (A**2): 933 ; 0.06 ; 0.50
REMARK 3 TIGHT THERMAL 3 G (A**2): 933 ; 0.05 ; 0.50
REMARK 3 TIGHT THERMAL 3 K (A**2): 933 ; 0.06 ; 0.50
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
REMARK 3 CHAIN NAMES : D H L
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 11 D 115 1
REMARK 3 1 H 11 H 115 1
REMARK 3 1 L 11 L 115 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 4 D (A): 835 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 4 H (A): 835 ; 0.04 ; 0.05
REMARK 3 TIGHT POSITIONAL 4 L (A): 835 ; 0.03 ; 0.05
REMARK 3 TIGHT THERMAL 4 D (A**2): 835 ; 0.07 ; 0.50
REMARK 3 TIGHT THERMAL 4 H (A**2): 835 ; 0.06 ; 0.50
REMARK 3 TIGHT THERMAL 4 L (A**2): 835 ; 0.06 ; 0.50
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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 588
REMARK 3 RESIDUE RANGE : A 601 A 601
REMARK 3 ORIGIN FOR THE GROUP (A): 1.2867 -10.8839 -23.6106
REMARK 3 T TENSOR
REMARK 3 T11: 0.0674 T22: 0.0384
REMARK 3 T33: 0.1940 T12: -0.0072
REMARK 3 T13: 0.1023 T23: -0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 1.7033 L22: 1.9944
REMARK 3 L33: 1.8113 L12: -0.0217
REMARK 3 L13: 0.1770 L23: -0.1365
REMARK 3 S TENSOR
REMARK 3 S11: 0.0299 S12: 0.0145 S13: 0.2576
REMARK 3 S21: 0.3454 S22: -0.0802 S23: 0.4508
REMARK 3 S31: -0.0047 S32: -0.2080 S33: 0.0503
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 238
REMARK 3 RESIDUE RANGE : B 302 B 304
REMARK 3 ORIGIN FOR THE GROUP (A): 28.6688 -8.1688 -29.7650
REMARK 3 T TENSOR
REMARK 3 T11: 0.0598 T22: 0.0762
REMARK 3 T33: 0.1040 T12: -0.0002
REMARK 3 T13: -0.0598 T23: 0.0493
REMARK 3 L TENSOR
REMARK 3 L11: 2.8210 L22: 3.2648
REMARK 3 L33: 1.7589 L12: 0.0613
REMARK 3 L13: 0.1999 L23: -0.7221
REMARK 3 S TENSOR
REMARK 3 S11: -0.0968 S12: 0.3654 S13: 0.4308
REMARK 3 S21: 0.4190 S22: 0.0342 S23: -0.3362
REMARK 3 S31: -0.0467 S32: 0.2111 S33: 0.0626
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 : C 8 C 128
REMARK 3 ORIGIN FOR THE GROUP (A): 60.4974 -4.4443 -30.5164
REMARK 3 T TENSOR
REMARK 3 T11: 0.1713 T22: 0.2499
REMARK 3 T33: 0.5761 T12: -0.0183
REMARK 3 T13: -0.0474 T23: 0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 4.7929 L22: 1.5258
REMARK 3 L33: 1.4693 L12: -0.7876
REMARK 3 L13: 0.3362 L23: -0.1820
REMARK 3 S TENSOR
REMARK 3 S11: -0.0236 S12: -0.0610 S13: 0.6350
REMARK 3 S21: 0.1596 S22: 0.0964 S23: -0.5230
REMARK 3 S31: 0.0296 S32: 0.2758 S33: -0.0727
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 : D 11 D 115
REMARK 3 ORIGIN FOR THE GROUP (A): 66.8484 -16.6032 -37.2742
REMARK 3 T TENSOR
REMARK 3 T11: 0.0795 T22: 0.3070
REMARK 3 T33: 0.5489 T12: 0.0596
REMARK 3 T13: 0.0029 T23: 0.0484
REMARK 3 L TENSOR
REMARK 3 L11: 3.5287 L22: 2.1208
REMARK 3 L33: 2.4375 L12: -0.4842
REMARK 3 L13: -0.3677 L23: -0.5294
REMARK 3 S TENSOR
REMARK 3 S11: 0.1613 S12: 0.5077 S13: 0.2095
REMARK 3 S21: -0.0489 S22: -0.1285 S23: -0.7178
REMARK 3 S31: 0.0407 S32: 0.5794 S33: -0.0328
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 1 E 588
REMARK 3 RESIDUE RANGE : E 601 E 601
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8631 -71.9087 -28.1864
REMARK 3 T TENSOR
REMARK 3 T11: 0.3590 T22: 0.0428
REMARK 3 T33: 0.2717 T12: 0.0006
REMARK 3 T13: -0.0886 T23: -0.0753
REMARK 3 L TENSOR
REMARK 3 L11: 1.6660 L22: 2.0360
REMARK 3 L33: 1.5426 L12: 0.4347
REMARK 3 L13: 0.2919 L23: 0.2069
REMARK 3 S TENSOR
REMARK 3 S11: 0.1003 S12: 0.0905 S13: -0.4520
REMARK 3 S21: 0.4611 S22: -0.0059 S23: 0.1437
REMARK 3 S31: 0.2657 S32: -0.0288 S33: -0.0943
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 1 F 238
REMARK 3 RESIDUE RANGE : F 302 F 304
REMARK 3 ORIGIN FOR THE GROUP (A): 38.6012 -60.4421 -27.3896
REMARK 3 T TENSOR
REMARK 3 T11: 0.2941 T22: 0.1253
REMARK 3 T33: 0.2626 T12: 0.1028
REMARK 3 T13: -0.2333 T23: -0.1061
REMARK 3 L TENSOR
REMARK 3 L11: 2.7109 L22: 1.9028
REMARK 3 L33: 1.9438 L12: 0.6262
REMARK 3 L13: 0.0060 L23: 0.1834
REMARK 3 S TENSOR
REMARK 3 S11: 0.1059 S12: 0.2247 S13: -0.2625
REMARK 3 S21: 0.3891 S22: 0.0096 S23: -0.4336
REMARK 3 S31: 0.3159 S32: 0.3368 S33: -0.1155
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 : G 8 G 128
REMARK 3 ORIGIN FOR THE GROUP (A): 69.8194 -52.8861 -29.4649
REMARK 3 T TENSOR
REMARK 3 T11: 0.3583 T22: 0.4062
REMARK 3 T33: 0.8701 T12: 0.2383
REMARK 3 T13: -0.3313 T23: -0.1457
REMARK 3 L TENSOR
REMARK 3 L11: 3.9511 L22: 2.1538
REMARK 3 L33: 1.6316 L12: 1.7228
REMARK 3 L13: -1.4324 L23: -0.4768
REMARK 3 S TENSOR
REMARK 3 S11: 0.1475 S12: 0.1301 S13: -0.8298
REMARK 3 S21: -0.0255 S22: -0.1279 S23: -0.9757
REMARK 3 S31: 0.3091 S32: 0.3971 S33: -0.0196
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 : H 11 H 115
REMARK 3 ORIGIN FOR THE GROUP (A): 71.3585 -39.9454 -37.4617
REMARK 3 T TENSOR
REMARK 3 T11: 0.1505 T22: 0.4533
REMARK 3 T33: 0.7239 T12: 0.1474
REMARK 3 T13: -0.1364 T23: -0.1371
REMARK 3 L TENSOR
REMARK 3 L11: 1.9402 L22: 2.6576
REMARK 3 L33: 3.3943 L12: 0.4883
REMARK 3 L13: -0.3236 L23: 0.1938
REMARK 3 S TENSOR
REMARK 3 S11: 0.2058 S12: 0.5610 S13: -0.2986
REMARK 3 S21: -0.1223 S22: -0.0330 S23: -0.9741
REMARK 3 S31: 0.0808 S32: 0.5372 S33: -0.1729
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : I 1 I 588
REMARK 3 RESIDUE RANGE : I 601 I 601
REMARK 3 ORIGIN FOR THE GROUP (A): 6.3316 -37.4470 -80.4759
REMARK 3 T TENSOR
REMARK 3 T11: 0.7582 T22: 1.5265
REMARK 3 T33: 0.4914 T12: 0.0487
REMARK 3 T13: -0.2433 T23: -0.0878
REMARK 3 L TENSOR
REMARK 3 L11: 1.8886 L22: 2.0358
REMARK 3 L33: 0.8853 L12: -0.1993
REMARK 3 L13: 0.0631 L23: 0.1587
REMARK 3 S TENSOR
REMARK 3 S11: 0.0306 S12: 1.0057 S13: -0.0773
REMARK 3 S21: -0.7076 S22: 0.1108 S23: 0.3906
REMARK 3 S31: 0.0610 S32: -0.2038 S33: -0.1413
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : J 1 J 238
REMARK 3 RESIDUE RANGE : J 302 J 304
REMARK 3 ORIGIN FOR THE GROUP (A): 34.0370 -36.5463 -75.0261
REMARK 3 T TENSOR
REMARK 3 T11: 0.5491 T22: 1.1139
REMARK 3 T33: 0.2429 T12: 0.0853
REMARK 3 T13: -0.0402 T23: -0.1148
REMARK 3 L TENSOR
REMARK 3 L11: 2.6004 L22: 2.3094
REMARK 3 L33: 1.7470 L12: 0.3612
REMARK 3 L13: -0.1263 L23: -0.0423
REMARK 3 S TENSOR
REMARK 3 S11: -0.0141 S12: 1.0614 S13: -0.2244
REMARK 3 S21: -0.6824 S22: 0.2131 S23: -0.0410
REMARK 3 S31: 0.1689 S32: -0.0389 S33: -0.1990
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 : K 8 K 128
REMARK 3 ORIGIN FOR THE GROUP (A): 65.2565 -29.5913 -72.7546
REMARK 3 T TENSOR
REMARK 3 T11: 0.6189 T22: 1.3439
REMARK 3 T33: 0.4297 T12: 0.1114
REMARK 3 T13: 0.2326 T23: -0.1387
REMARK 3 L TENSOR
REMARK 3 L11: 2.6512 L22: 2.4007
REMARK 3 L33: 1.9598 L12: 1.2428
REMARK 3 L13: -0.0625 L23: -0.0690
REMARK 3 S TENSOR
REMARK 3 S11: -0.0417 S12: 1.2560 S13: -0.0547
REMARK 3 S21: -0.5677 S22: 0.1239 S23: -0.3743
REMARK 3 S31: -0.1269 S32: 0.2329 S33: -0.0821
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 : L 11 L 115
REMARK 3 ORIGIN FOR THE GROUP (A): 69.0119 -28.0028 -57.9783
REMARK 3 T TENSOR
REMARK 3 T11: 0.2589 T22: 0.9204
REMARK 3 T33: 0.4392 T12: 0.1204
REMARK 3 T13: 0.1570 T23: -0.0849
REMARK 3 L TENSOR
REMARK 3 L11: 2.5586 L22: 3.9518
REMARK 3 L33: 2.0701 L12: -0.0692
REMARK 3 L13: 0.5422 L23: -0.2065
REMARK 3 S TENSOR
REMARK 3 S11: 0.0096 S12: 0.8958 S13: -0.0548
REMARK 3 S21: -0.1220 S22: 0.0607 S23: -0.8173
REMARK 3 S31: -0.0321 S32: 0.6175 S33: -0.0704
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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. DENSITY FOR THE N-TERMINUS OF SDH C (RESIDUES 1-7 OF
REMARK 3 CHAINS C, G, K) AND THE N-TERMINUS OF SDHD (RESIDUES 1-10 OF
REMARK 3 CHAINS D, H AND L) WAS WEAK AND THESE REGIONS ARE NOT INCLUDED
REMARK 3 IN THE MODEL. THE SIDE CHAIN OF SDHD TRP113 IS TRUNCATED AT THE
REMARK 3 CBETA ATOM SINCE DENSITY FOR THE SIDE CHAIN WAS POOR. ATOM
REMARK 3 RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD
REMARK 3 CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.
REMARK 4
REMARK 4 2WS3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-SEP-09.
REMARK 100 THE DEPOSITION ID IS D_1290041026.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-JUL-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71105
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 49.030
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 6.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.61000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 2WDQ
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5
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 59.92500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.65500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 92.35500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 101.65500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 59.92500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 92.35500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: 15680 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -163.4 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 15610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37770 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -158.7 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
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: 15620 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 37720 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -160.2 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 ENGINEERED RESIDUE IN CHAIN D, TYR 83 TO PHE
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, TYR 83 TO PHE
REMARK 400 ENGINEERED RESIDUE IN CHAIN L, TYR 83 TO PHE
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET C 1
REMARK 465 ILE C 2
REMARK 465 ARG C 3
REMARK 465 ASN C 4
REMARK 465 VAL C 5
REMARK 465 LYS C 6
REMARK 465 LYS C 7
REMARK 465 TRP C 129
REMARK 465 MET D 1
REMARK 465 VAL D 2
REMARK 465 SER D 3
REMARK 465 ASN D 4
REMARK 465 ALA D 5
REMARK 465 SER D 6
REMARK 465 ALA D 7
REMARK 465 LEU D 8
REMARK 465 GLY D 9
REMARK 465 ARG D 10
REMARK 465 MET G 1
REMARK 465 ILE G 2
REMARK 465 ARG G 3
REMARK 465 ASN G 4
REMARK 465 VAL G 5
REMARK 465 LYS G 6
REMARK 465 LYS G 7
REMARK 465 TRP G 129
REMARK 465 MET H 1
REMARK 465 VAL H 2
REMARK 465 SER H 3
REMARK 465 ASN H 4
REMARK 465 ALA H 5
REMARK 465 SER H 6
REMARK 465 ALA H 7
REMARK 465 LEU H 8
REMARK 465 GLY H 9
REMARK 465 ARG H 10
REMARK 465 MET K 1
REMARK 465 ILE K 2
REMARK 465 ARG K 3
REMARK 465 ASN K 4
REMARK 465 VAL K 5
REMARK 465 LYS K 6
REMARK 465 LYS K 7
REMARK 465 TRP K 129
REMARK 465 MET L 1
REMARK 465 VAL L 2
REMARK 465 SER L 3
REMARK 465 ASN L 4
REMARK 465 ALA L 5
REMARK 465 SER L 6
REMARK 465 ALA L 7
REMARK 465 LEU L 8
REMARK 465 GLY L 9
REMARK 465 ARG L 10
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 TRP D 113 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 113 CZ3 CH2
REMARK 470 TRP H 113 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP H 113 CZ3 CH2
REMARK 470 TRP L 113 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP L 113 CZ3 CH2
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 NE2 HIS A 45 C8M FAD A 601 1.94
REMARK 500 NE2 HIS E 45 C8M FAD E 601 2.08
REMARK 500 OG SER I 404 O3' FAD I 601 2.15
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 GLN A 50 -65.24 -124.20
REMARK 500 ALA A 138 -123.84 45.73
REMARK 500 ALA A 205 34.52 -156.07
REMARK 500 THR A 244 79.22 -117.81
REMARK 500 ALA A 249 -45.35 -133.49
REMARK 500 LYS A 281 -125.61 60.27
REMARK 500 ASP A 304 -167.85 -112.79
REMARK 500 HIS A 354 -58.10 -132.05
REMARK 500 ASN A 398 116.66 -163.39
REMARK 500 SER A 472 -153.74 -72.20
REMARK 500 VAL B 14 -57.00 -126.66
REMARK 500 ARG B 53 147.20 -171.44
REMARK 500 SER B 54 -67.19 -147.04
REMARK 500 ARG B 56 16.82 49.67
REMARK 500 ASP B 63 59.99 -105.77
REMARK 500 ARG B 101 131.24 -171.14
REMARK 500 ASP B 102 -110.33 43.40
REMARK 500 ARG B 131 -116.79 -127.81
REMARK 500 ALA B 153 -5.62 78.48
REMARK 500 GLU B 189 31.93 -87.40
REMARK 500 SER C 51 4.93 -66.39
REMARK 500 SER D 40 -16.03 -141.35
REMARK 500 PRO E 41 -38.71 -38.30
REMARK 500 GLN E 50 -66.20 -121.89
REMARK 500 VAL E 55 131.30 -170.44
REMARK 500 ALA E 138 -126.35 43.79
REMARK 500 LEU E 167 -70.43 -87.26
REMARK 500 ALA E 205 36.70 -146.11
REMARK 500 THR E 244 74.69 -109.27
REMARK 500 ALA E 249 -44.53 -133.01
REMARK 500 LYS E 281 -123.09 66.77
REMARK 500 ALA E 284 -177.85 -69.49
REMARK 500 ASP E 304 -167.19 -114.57
REMARK 500 HIS E 354 -56.56 -134.36
REMARK 500 SER E 472 -153.23 -73.76
REMARK 500 VAL F 14 -58.41 -128.87
REMARK 500 SER F 54 -71.86 -145.85
REMARK 500 ARG F 56 16.11 49.63
REMARK 500 ASP F 63 57.90 -102.46
REMARK 500 ARG F 101 130.76 -170.92
REMARK 500 ASP F 102 -110.19 43.32
REMARK 500 LYS F 118 70.38 56.40
REMARK 500 ARG F 131 -116.12 -128.78
REMARK 500 ALA F 153 -8.85 78.51
REMARK 500 GLU F 189 33.57 -88.79
REMARK 500 ASP G 14 101.59 -56.08
REMARK 500 SER G 51 5.25 -69.83
REMARK 500 SER H 40 -14.51 -141.79
REMARK 500 PRO I 41 -36.77 -37.03
REMARK 500 GLN I 50 -64.72 -122.12
REMARK 500
REMARK 500 THIS ENTRY HAS 71 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1589 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 356 O
REMARK 620 2 MET A 357 O 78.3
REMARK 620 3 GLY A 358 O 77.5 65.0
REMARK 620 4 GLU A 388 O 97.7 155.9 90.9
REMARK 620 5 ALA A 390 O 172.0 97.6 94.5 83.1
REMARK 620 N 1 2 3 4
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 55 SG
REMARK 620 2 FES B 302 S1 101.7
REMARK 620 3 FES B 302 S2 104.8 93.6
REMARK 620 4 CYS B 60 SG 103.6 124.4 125.5
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 ASP B 63 OD1
REMARK 620 2 FES B 302 S1 107.9
REMARK 620 3 FES B 302 S2 112.9 92.6
REMARK 620 4 CYS B 75 SG 120.7 99.4 117.2
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 149 SG
REMARK 620 2 SF4 B 303 S1 131.8
REMARK 620 3 SF4 B 303 S2 97.8 106.1
REMARK 620 4 SF4 B 303 S4 110.4 104.2 102.8
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 152 SG
REMARK 620 2 SF4 B 303 S1 111.2
REMARK 620 3 SF4 B 303 S2 119.6 106.2
REMARK 620 4 SF4 B 303 S3 106.4 104.2 108.1
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 155 SG
REMARK 620 2 SF4 B 303 S2 109.3
REMARK 620 3 SF4 B 303 S3 104.9 108.5
REMARK 620 4 SF4 B 303 S4 126.2 102.2 104.9
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 159 SG
REMARK 620 2 F3S B 304 S1 105.6
REMARK 620 3 F3S B 304 S2 117.7 115.4
REMARK 620 4 F3S B 304 S3 116.2 99.8 101.1
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 206 SG
REMARK 620 2 F3S B 304 S1 125.0
REMARK 620 3 F3S B 304 S3 122.4 99.7
REMARK 620 4 F3S B 304 S4 94.9 109.5 102.9
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 212 SG
REMARK 620 2 F3S B 304 S2 82.9
REMARK 620 3 F3S B 304 S3 99.2 105.5
REMARK 620 4 F3S B 304 S4 98.1 145.8 108.1
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 216 SG
REMARK 620 2 SF4 B 303 S1 115.1
REMARK 620 3 SF4 B 303 S3 102.2 104.6
REMARK 620 4 SF4 B 303 S4 123.8 104.0 105.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM C1130 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 84 NE2
REMARK 620 2 HEM C1130 NA 97.4
REMARK 620 3 HEM C1130 NB 87.3 86.8
REMARK 620 4 HEM C1130 NC 86.0 175.5 90.4
REMARK 620 5 HEM C1130 ND 89.1 91.8 176.0 91.2
REMARK 620 6 HIS D 71 NE2 177.7 84.8 92.4 91.8 91.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA E1589 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET E 356 O
REMARK 620 2 MET E 357 O 78.4
REMARK 620 3 GLY E 358 O 79.8 66.5
REMARK 620 4 GLU E 388 O 93.3 158.9 93.1
REMARK 620 5 ALA E 390 O 177.1 99.0 98.0 88.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES F 302 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 55 SG
REMARK 620 2 FES F 302 S1 93.9
REMARK 620 3 FES F 302 S2 117.4 93.9
REMARK 620 4 CYS F 60 SG 102.3 115.2 128.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES F 302 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 63 OD1
REMARK 620 2 FES F 302 S1 118.4
REMARK 620 3 FES F 302 S2 103.1 94.3
REMARK 620 4 CYS F 75 SG 119.9 103.6 114.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 F 303 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 149 SG
REMARK 620 2 SF4 F 303 S1 124.7
REMARK 620 3 SF4 F 303 S2 98.2 102.7
REMARK 620 4 SF4 F 303 S4 117.3 102.9 109.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 F 303 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 152 SG
REMARK 620 2 SF4 F 303 S1 130.0
REMARK 620 3 SF4 F 303 S2 111.8 103.8
REMARK 620 4 SF4 F 303 S3 98.8 105.0 104.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 F 303 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 155 SG
REMARK 620 2 SF4 F 303 S2 123.7
REMARK 620 3 SF4 F 303 S3 106.5 102.9
REMARK 620 4 SF4 F 303 S4 107.9 106.9 108.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S F 304 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 159 SG
REMARK 620 2 F3S F 304 S1 103.9
REMARK 620 3 F3S F 304 S2 113.6 125.0
REMARK 620 4 F3S F 304 S3 123.3 97.8 93.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S F 304 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 206 SG
REMARK 620 2 F3S F 304 S1 120.9
REMARK 620 3 F3S F 304 S3 122.6 98.3
REMARK 620 4 F3S F 304 S4 98.9 115.6 99.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S F 304 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 212 SG
REMARK 620 2 F3S F 304 S2 82.5
REMARK 620 3 F3S F 304 S3 98.5 96.1
REMARK 620 4 F3S F 304 S4 100.4 159.7 103.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 F 303 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F 216 SG
REMARK 620 2 SF4 F 303 S1 105.6
REMARK 620 3 SF4 F 303 S3 111.7 105.8
REMARK 620 4 SF4 F 303 S4 122.3 102.7 107.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM G1130 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS G 84 NE2
REMARK 620 2 HEM G1130 NA 87.9
REMARK 620 3 HEM G1130 NB 88.2 87.5
REMARK 620 4 HEM G1130 NC 88.6 174.7 88.4
REMARK 620 5 HEM G1130 ND 84.6 89.5 172.3 94.2
REMARK 620 6 HIS H 71 NE2 172.5 86.7 86.2 96.3 100.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA I1589 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET I 356 O
REMARK 620 2 MET I 357 O 72.4
REMARK 620 3 GLY I 358 O 71.2 59.8
REMARK 620 4 GLU I 388 O 90.5 140.8 81.4
REMARK 620 5 ALA I 390 O 160.2 94.3 89.5 91.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES J 302 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 55 SG
REMARK 620 2 FES J 302 S1 90.1
REMARK 620 3 FES J 302 S2 111.3 92.9
REMARK 620 4 CYS J 60 SG 100.6 125.4 129.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 FES J 302 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP J 63 OD1
REMARK 620 2 FES J 302 S1 116.9
REMARK 620 3 FES J 302 S2 102.0 93.1
REMARK 620 4 CYS J 75 SG 126.3 97.0 117.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 J 303 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 149 SG
REMARK 620 2 SF4 J 303 S1 114.4
REMARK 620 3 SF4 J 303 S2 100.6 104.3
REMARK 620 4 SF4 J 303 S4 124.4 102.8 108.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 J 303 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 152 SG
REMARK 620 2 SF4 J 303 S1 125.8
REMARK 620 3 SF4 J 303 S2 115.0 105.3
REMARK 620 4 SF4 J 303 S3 97.3 107.0 103.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 J 303 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 155 SG
REMARK 620 2 SF4 J 303 S2 103.2
REMARK 620 3 SF4 J 303 S3 115.6 104.0
REMARK 620 4 SF4 J 303 S4 120.1 108.3 104.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S J 304 FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 159 SG
REMARK 620 2 F3S J 304 S1 120.1
REMARK 620 3 F3S J 304 S2 105.8 115.8
REMARK 620 4 F3S J 304 S3 121.3 97.2 94.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S J 304 FE3
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 206 SG
REMARK 620 2 F3S J 304 S1 125.0
REMARK 620 3 F3S J 304 S3 114.6 96.0
REMARK 620 4 F3S J 304 S4 103.9 116.9 97.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 F3S J 304 FE4
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 212 SG
REMARK 620 2 F3S J 304 S2 98.1
REMARK 620 3 F3S J 304 S3 95.2 93.6
REMARK 620 4 F3S J 304 S4 83.1 167.5 98.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 SF4 J 303 FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J 216 SG
REMARK 620 2 SF4 J 303 S1 127.3
REMARK 620 3 SF4 J 303 S3 110.6 107.5
REMARK 620 4 SF4 J 303 S4 100.4 103.1 105.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 HEM K1130 FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS K 84 NE2
REMARK 620 2 HEM K1130 NA 92.5
REMARK 620 3 HEM K1130 NB 83.7 87.5
REMARK 620 4 HEM K1130 NC 80.1 171.0 86.8
REMARK 620 5 HEM K1130 ND 85.3 91.0 168.8 93.3
REMARK 620 6 HIS L 71 NE2 171.7 95.8 95.6 91.6 95.6
REMARK 620 N 1 2 3 4 5
REMARK 700
REMARK 700 SHEET
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,
REMARK 700 TWO SHEETS ARE DEFINED.
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 601
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 FAD E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES F 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 F 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S F 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD I 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES J 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 J 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F3S J 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1589
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA E 1589
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA I 1589
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE C 1129
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE G 1129
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CBE K 1129
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 1130
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO A 1590
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM G 1130
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO E 1590
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM K 1130
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEO I 1590
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WP9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE OXIDOREDUCTASE
REMARK 900 (SQR) SDHB HIS207THR MUTANT
REMARK 900 RELATED ID: 2WDQ RELATED DB: PDB
REMARK 900 E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH CARBOXIN BOUND
REMARK 900 RELATED ID: 2WDR RELATED DB: PDB
REMARK 900 E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH
REMARK 900 PENTACHLOROPHENOL BOUND
REMARK 900 RELATED ID: 1NEK RELATED DB: PDB
REMARK 900 SUCCINATE DEHYDOGENASE FROM E.COLI
REMARK 900 RELATED ID: 1NEN RELATED DB: PDB
REMARK 900 MOLECULAR ARCHITECTURE OF SUCCINATE DEHYDROGENASE (COMPLEXII)
REMARK 900 PREVENTS REACTIVE OXYGEN SPECIES GENERATION
REMARK 900 RELATED ID: 2WU2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE OXIDOREDUCTASE
REMARK 900 (SQR) SDHC HIS84MET MUTANT
REMARK 900 RELATED ID: 2ACZ RELATED DB: PDB
REMARK 900 COMPLEX II (SUCCINATE DEHYDROGENASE) FROM E. COLI WITHATPENIN A5
REMARK 900 INHIBITOR CO-CRYSTALLIZED AT THE UBIQUINONEBINDING SITE
REMARK 900 RELATED ID: 2WU5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE E. COLI SUCCINATE: QUINONE OXIDOREDUCTASE
REMARK 900 (SQR) SDHD HIS71MET MUTANT
REMARK 900 RELATED ID: 2WDV RELATED DB: PDB
REMARK 900 E. COLI SUCCINATE:QUINONE OXIDOREDUCTASE (SQR ) WITH AN EMPTY
REMARK 900 QUINONE-BINDING POCKET
DBREF 2WS3 A 1 588 UNP P0AC41 DHSA_ECOLI 1 588
DBREF 2WS3 B 1 238 UNP P07014 DHSB_ECOLI 1 238
DBREF 2WS3 C 1 129 UNP P69054 DHSC_ECOLI 1 129
DBREF 2WS3 D 1 115 UNP P0AC44 DHSD_ECOLI 1 115
DBREF 2WS3 E 1 588 UNP P0AC41 DHSA_ECOLI 1 588
DBREF 2WS3 F 1 238 UNP P07014 DHSB_ECOLI 1 238
DBREF 2WS3 G 1 129 UNP P69054 DHSC_ECOLI 1 129
DBREF 2WS3 H 1 115 UNP P0AC44 DHSD_ECOLI 1 115
DBREF 2WS3 I 1 588 UNP P0AC41 DHSA_ECOLI 1 588
DBREF 2WS3 J 1 238 UNP P07014 DHSB_ECOLI 1 238
DBREF 2WS3 K 1 129 UNP P69054 DHSC_ECOLI 1 129
DBREF 2WS3 L 1 115 UNP P0AC44 DHSD_ECOLI 1 115
SEQADV 2WS3 PHE D 83 UNP P0AC44 TYR 83 ENGINEERED MUTATION
SEQADV 2WS3 PHE H 83 UNP P0AC44 TYR 83 ENGINEERED MUTATION
SEQADV 2WS3 PHE L 83 UNP P0AC44 TYR 83 ENGINEERED MUTATION
SEQRES 1 A 588 MET LYS LEU PRO VAL ARG GLU PHE ASP ALA VAL VAL ILE
SEQRES 2 A 588 GLY ALA GLY GLY ALA GLY MET ARG ALA ALA LEU GLN ILE
SEQRES 3 A 588 SER GLN SER GLY GLN THR CYS ALA LEU LEU SER LYS VAL
SEQRES 4 A 588 PHE PRO THR ARG SER HIS THR VAL SER ALA GLN GLY GLY
SEQRES 5 A 588 ILE THR VAL ALA LEU GLY ASN THR HIS GLU ASP ASN TRP
SEQRES 6 A 588 GLU TRP HIS MET TYR ASP THR VAL LYS GLY SER ASP TYR
SEQRES 7 A 588 ILE GLY ASP GLN ASP ALA ILE GLU TYR MET CYS LYS THR
SEQRES 8 A 588 GLY PRO GLU ALA ILE LEU GLU LEU GLU HIS MET GLY LEU
SEQRES 9 A 588 PRO PHE SER ARG LEU ASP ASP GLY ARG ILE TYR GLN ARG
SEQRES 10 A 588 PRO PHE GLY GLY GLN SER LYS ASN PHE GLY GLY GLU GLN
SEQRES 11 A 588 ALA ALA ARG THR ALA ALA ALA ALA ASP ARG THR GLY HIS
SEQRES 12 A 588 ALA LEU LEU HIS THR LEU TYR GLN GLN ASN LEU LYS ASN
SEQRES 13 A 588 HIS THR THR ILE PHE SER GLU TRP TYR ALA LEU ASP LEU
SEQRES 14 A 588 VAL LYS ASN GLN ASP GLY ALA VAL VAL GLY CYS THR ALA
SEQRES 15 A 588 LEU CYS ILE GLU THR GLY GLU VAL VAL TYR PHE LYS ALA
SEQRES 16 A 588 ARG ALA THR VAL LEU ALA THR GLY GLY ALA GLY ARG ILE
SEQRES 17 A 588 TYR GLN SER THR THR ASN ALA HIS ILE ASN THR GLY ASP
SEQRES 18 A 588 GLY VAL GLY MET ALA ILE ARG ALA GLY VAL PRO VAL GLN
SEQRES 19 A 588 ASP MET GLU MET TRP GLN PHE HIS PRO THR GLY ILE ALA
SEQRES 20 A 588 GLY ALA GLY VAL LEU VAL THR GLU GLY CYS ARG GLY GLU
SEQRES 21 A 588 GLY GLY TYR LEU LEU ASN LYS HIS GLY GLU ARG PHE MET
SEQRES 22 A 588 GLU ARG TYR ALA PRO ASN ALA LYS ASP LEU ALA GLY ARG
SEQRES 23 A 588 ASP VAL VAL ALA ARG SER ILE MET ILE GLU ILE ARG GLU
SEQRES 24 A 588 GLY ARG GLY CYS ASP GLY PRO TRP GLY PRO HIS ALA LYS
SEQRES 25 A 588 LEU LYS LEU ASP HIS LEU GLY LYS GLU VAL LEU GLU SER
SEQRES 26 A 588 ARG LEU PRO GLY ILE LEU GLU LEU SER ARG THR PHE ALA
SEQRES 27 A 588 HIS VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL ILE PRO
SEQRES 28 A 588 THR CYS HIS TYR MET MET GLY GLY ILE PRO THR LYS VAL
SEQRES 29 A 588 THR GLY GLN ALA LEU THR VAL ASN GLU LYS GLY GLU ASP
SEQRES 30 A 588 VAL VAL VAL PRO GLY LEU PHE ALA VAL GLY GLU ILE ALA
SEQRES 31 A 588 CYS VAL SER VAL HIS GLY ALA ASN ARG LEU GLY GLY ASN
SEQRES 32 A 588 SER LEU LEU ASP LEU VAL VAL PHE GLY ARG ALA ALA GLY
SEQRES 33 A 588 LEU HIS LEU GLN GLU SER ILE ALA GLU GLN GLY ALA LEU
SEQRES 34 A 588 ARG ASP ALA SER GLU SER ASP VAL GLU ALA SER LEU ASP
SEQRES 35 A 588 ARG LEU ASN ARG TRP ASN ASN ASN ARG ASN GLY GLU ASP
SEQRES 36 A 588 PRO VAL ALA ILE ARG LYS ALA LEU GLN GLU CYS MET GLN
SEQRES 37 A 588 HIS ASN PHE SER VAL PHE ARG GLU GLY ASP ALA MET ALA
SEQRES 38 A 588 LYS GLY LEU GLU GLN LEU LYS VAL ILE ARG GLU ARG LEU
SEQRES 39 A 588 LYS ASN ALA ARG LEU ASP ASP THR SER SER GLU PHE ASN
SEQRES 40 A 588 THR GLN ARG VAL GLU CYS LEU GLU LEU ASP ASN LEU MET
SEQRES 41 A 588 GLU THR ALA TYR ALA THR ALA VAL SER ALA ASN PHE ARG
SEQRES 42 A 588 THR GLU SER ARG GLY ALA HIS SER ARG PHE ASP PHE PRO
SEQRES 43 A 588 ASP ARG ASP ASP GLU ASN TRP LEU CYS HIS SER LEU TYR
SEQRES 44 A 588 LEU PRO GLU SER GLU SER MET THR ARG ARG SER VAL ASN
SEQRES 45 A 588 MET GLU PRO LYS LEU ARG PRO ALA PHE PRO PRO LYS ILE
SEQRES 46 A 588 ARG THR TYR
SEQRES 1 B 238 MET ARG LEU GLU PHE SER ILE TYR ARG TYR ASN PRO ASP
SEQRES 2 B 238 VAL ASP ASP ALA PRO ARG MET GLN ASP TYR THR LEU GLU
SEQRES 3 B 238 ALA ASP GLU GLY ARG ASP MET MET LEU LEU ASP ALA LEU
SEQRES 4 B 238 ILE GLN LEU LYS GLU LYS ASP PRO SER LEU SER PHE ARG
SEQRES 5 B 238 ARG SER CYS ARG GLU GLY VAL CYS GLY SER ASP GLY LEU
SEQRES 6 B 238 ASN MET ASN GLY LYS ASN GLY LEU ALA CYS ILE THR PRO
SEQRES 7 B 238 ILE SER ALA LEU ASN GLN PRO GLY LYS LYS ILE VAL ILE
SEQRES 8 B 238 ARG PRO LEU PRO GLY LEU PRO VAL ILE ARG ASP LEU VAL
SEQRES 9 B 238 VAL ASP MET GLY GLN PHE TYR ALA GLN TYR GLU LYS ILE
SEQRES 10 B 238 LYS PRO TYR LEU LEU ASN ASN GLY GLN ASN PRO PRO ALA
SEQRES 11 B 238 ARG GLU HIS LEU GLN MET PRO GLU GLN ARG GLU LYS LEU
SEQRES 12 B 238 ASP GLY LEU TYR GLU CYS ILE LEU CYS ALA CYS CYS SER
SEQRES 13 B 238 THR SER CYS PRO SER PHE TRP TRP ASN PRO ASP LYS PHE
SEQRES 14 B 238 ILE GLY PRO ALA GLY LEU LEU ALA ALA TYR ARG PHE LEU
SEQRES 15 B 238 ILE ASP SER ARG ASP THR GLU THR ASP SER ARG LEU ASP
SEQRES 16 B 238 GLY LEU SER ASP ALA PHE SER VAL PHE ARG CYS HIS SER
SEQRES 17 B 238 ILE MET ASN CYS VAL SER VAL CYS PRO LYS GLY LEU ASN
SEQRES 18 B 238 PRO THR ARG ALA ILE GLY HIS ILE LYS SER MET LEU LEU
SEQRES 19 B 238 GLN ARG ASN ALA
SEQRES 1 C 129 MET ILE ARG ASN VAL LYS LYS GLN ARG PRO VAL ASN LEU
SEQRES 2 C 129 ASP LEU GLN THR ILE ARG PHE PRO ILE THR ALA ILE ALA
SEQRES 3 C 129 SER ILE LEU HIS ARG VAL SER GLY VAL ILE THR PHE VAL
SEQRES 4 C 129 ALA VAL GLY ILE LEU LEU TRP LEU LEU GLY THR SER LEU
SEQRES 5 C 129 SER SER PRO GLU GLY PHE GLU GLN ALA SER ALA ILE MET
SEQRES 6 C 129 GLY SER PHE PHE VAL LYS PHE ILE MET TRP GLY ILE LEU
SEQRES 7 C 129 THR ALA LEU ALA TYR HIS VAL VAL VAL GLY ILE ARG HIS
SEQRES 8 C 129 MET MET MET ASP PHE GLY TYR LEU GLU GLU THR PHE GLU
SEQRES 9 C 129 ALA GLY LYS ARG SER ALA LYS ILE SER PHE VAL ILE THR
SEQRES 10 C 129 VAL VAL LEU SER LEU LEU ALA GLY VAL LEU VAL TRP
SEQRES 1 D 115 MET VAL SER ASN ALA SER ALA LEU GLY ARG ASN GLY VAL
SEQRES 2 D 115 HIS ASP PHE ILE LEU VAL ARG ALA THR ALA ILE VAL LEU
SEQRES 3 D 115 THR LEU TYR ILE ILE TYR MET VAL GLY PHE PHE ALA THR
SEQRES 4 D 115 SER GLY GLU LEU THR TYR GLU VAL TRP ILE GLY PHE PHE
SEQRES 5 D 115 ALA SER ALA PHE THR LYS VAL PHE THR LEU LEU ALA LEU
SEQRES 6 D 115 PHE SER ILE LEU ILE HIS ALA TRP ILE GLY MET TRP GLN
SEQRES 7 D 115 VAL LEU THR ASP PHE VAL LYS PRO LEU ALA LEU ARG LEU
SEQRES 8 D 115 MET LEU GLN LEU VAL ILE VAL VAL ALA LEU VAL VAL TYR
SEQRES 9 D 115 VAL ILE TYR GLY PHE VAL VAL VAL TRP GLY VAL
SEQRES 1 E 588 MET LYS LEU PRO VAL ARG GLU PHE ASP ALA VAL VAL ILE
SEQRES 2 E 588 GLY ALA GLY GLY ALA GLY MET ARG ALA ALA LEU GLN ILE
SEQRES 3 E 588 SER GLN SER GLY GLN THR CYS ALA LEU LEU SER LYS VAL
SEQRES 4 E 588 PHE PRO THR ARG SER HIS THR VAL SER ALA GLN GLY GLY
SEQRES 5 E 588 ILE THR VAL ALA LEU GLY ASN THR HIS GLU ASP ASN TRP
SEQRES 6 E 588 GLU TRP HIS MET TYR ASP THR VAL LYS GLY SER ASP TYR
SEQRES 7 E 588 ILE GLY ASP GLN ASP ALA ILE GLU TYR MET CYS LYS THR
SEQRES 8 E 588 GLY PRO GLU ALA ILE LEU GLU LEU GLU HIS MET GLY LEU
SEQRES 9 E 588 PRO PHE SER ARG LEU ASP ASP GLY ARG ILE TYR GLN ARG
SEQRES 10 E 588 PRO PHE GLY GLY GLN SER LYS ASN PHE GLY GLY GLU GLN
SEQRES 11 E 588 ALA ALA ARG THR ALA ALA ALA ALA ASP ARG THR GLY HIS
SEQRES 12 E 588 ALA LEU LEU HIS THR LEU TYR GLN GLN ASN LEU LYS ASN
SEQRES 13 E 588 HIS THR THR ILE PHE SER GLU TRP TYR ALA LEU ASP LEU
SEQRES 14 E 588 VAL LYS ASN GLN ASP GLY ALA VAL VAL GLY CYS THR ALA
SEQRES 15 E 588 LEU CYS ILE GLU THR GLY GLU VAL VAL TYR PHE LYS ALA
SEQRES 16 E 588 ARG ALA THR VAL LEU ALA THR GLY GLY ALA GLY ARG ILE
SEQRES 17 E 588 TYR GLN SER THR THR ASN ALA HIS ILE ASN THR GLY ASP
SEQRES 18 E 588 GLY VAL GLY MET ALA ILE ARG ALA GLY VAL PRO VAL GLN
SEQRES 19 E 588 ASP MET GLU MET TRP GLN PHE HIS PRO THR GLY ILE ALA
SEQRES 20 E 588 GLY ALA GLY VAL LEU VAL THR GLU GLY CYS ARG GLY GLU
SEQRES 21 E 588 GLY GLY TYR LEU LEU ASN LYS HIS GLY GLU ARG PHE MET
SEQRES 22 E 588 GLU ARG TYR ALA PRO ASN ALA LYS ASP LEU ALA GLY ARG
SEQRES 23 E 588 ASP VAL VAL ALA ARG SER ILE MET ILE GLU ILE ARG GLU
SEQRES 24 E 588 GLY ARG GLY CYS ASP GLY PRO TRP GLY PRO HIS ALA LYS
SEQRES 25 E 588 LEU LYS LEU ASP HIS LEU GLY LYS GLU VAL LEU GLU SER
SEQRES 26 E 588 ARG LEU PRO GLY ILE LEU GLU LEU SER ARG THR PHE ALA
SEQRES 27 E 588 HIS VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL ILE PRO
SEQRES 28 E 588 THR CYS HIS TYR MET MET GLY GLY ILE PRO THR LYS VAL
SEQRES 29 E 588 THR GLY GLN ALA LEU THR VAL ASN GLU LYS GLY GLU ASP
SEQRES 30 E 588 VAL VAL VAL PRO GLY LEU PHE ALA VAL GLY GLU ILE ALA
SEQRES 31 E 588 CYS VAL SER VAL HIS GLY ALA ASN ARG LEU GLY GLY ASN
SEQRES 32 E 588 SER LEU LEU ASP LEU VAL VAL PHE GLY ARG ALA ALA GLY
SEQRES 33 E 588 LEU HIS LEU GLN GLU SER ILE ALA GLU GLN GLY ALA LEU
SEQRES 34 E 588 ARG ASP ALA SER GLU SER ASP VAL GLU ALA SER LEU ASP
SEQRES 35 E 588 ARG LEU ASN ARG TRP ASN ASN ASN ARG ASN GLY GLU ASP
SEQRES 36 E 588 PRO VAL ALA ILE ARG LYS ALA LEU GLN GLU CYS MET GLN
SEQRES 37 E 588 HIS ASN PHE SER VAL PHE ARG GLU GLY ASP ALA MET ALA
SEQRES 38 E 588 LYS GLY LEU GLU GLN LEU LYS VAL ILE ARG GLU ARG LEU
SEQRES 39 E 588 LYS ASN ALA ARG LEU ASP ASP THR SER SER GLU PHE ASN
SEQRES 40 E 588 THR GLN ARG VAL GLU CYS LEU GLU LEU ASP ASN LEU MET
SEQRES 41 E 588 GLU THR ALA TYR ALA THR ALA VAL SER ALA ASN PHE ARG
SEQRES 42 E 588 THR GLU SER ARG GLY ALA HIS SER ARG PHE ASP PHE PRO
SEQRES 43 E 588 ASP ARG ASP ASP GLU ASN TRP LEU CYS HIS SER LEU TYR
SEQRES 44 E 588 LEU PRO GLU SER GLU SER MET THR ARG ARG SER VAL ASN
SEQRES 45 E 588 MET GLU PRO LYS LEU ARG PRO ALA PHE PRO PRO LYS ILE
SEQRES 46 E 588 ARG THR TYR
SEQRES 1 F 238 MET ARG LEU GLU PHE SER ILE TYR ARG TYR ASN PRO ASP
SEQRES 2 F 238 VAL ASP ASP ALA PRO ARG MET GLN ASP TYR THR LEU GLU
SEQRES 3 F 238 ALA ASP GLU GLY ARG ASP MET MET LEU LEU ASP ALA LEU
SEQRES 4 F 238 ILE GLN LEU LYS GLU LYS ASP PRO SER LEU SER PHE ARG
SEQRES 5 F 238 ARG SER CYS ARG GLU GLY VAL CYS GLY SER ASP GLY LEU
SEQRES 6 F 238 ASN MET ASN GLY LYS ASN GLY LEU ALA CYS ILE THR PRO
SEQRES 7 F 238 ILE SER ALA LEU ASN GLN PRO GLY LYS LYS ILE VAL ILE
SEQRES 8 F 238 ARG PRO LEU PRO GLY LEU PRO VAL ILE ARG ASP LEU VAL
SEQRES 9 F 238 VAL ASP MET GLY GLN PHE TYR ALA GLN TYR GLU LYS ILE
SEQRES 10 F 238 LYS PRO TYR LEU LEU ASN ASN GLY GLN ASN PRO PRO ALA
SEQRES 11 F 238 ARG GLU HIS LEU GLN MET PRO GLU GLN ARG GLU LYS LEU
SEQRES 12 F 238 ASP GLY LEU TYR GLU CYS ILE LEU CYS ALA CYS CYS SER
SEQRES 13 F 238 THR SER CYS PRO SER PHE TRP TRP ASN PRO ASP LYS PHE
SEQRES 14 F 238 ILE GLY PRO ALA GLY LEU LEU ALA ALA TYR ARG PHE LEU
SEQRES 15 F 238 ILE ASP SER ARG ASP THR GLU THR ASP SER ARG LEU ASP
SEQRES 16 F 238 GLY LEU SER ASP ALA PHE SER VAL PHE ARG CYS HIS SER
SEQRES 17 F 238 ILE MET ASN CYS VAL SER VAL CYS PRO LYS GLY LEU ASN
SEQRES 18 F 238 PRO THR ARG ALA ILE GLY HIS ILE LYS SER MET LEU LEU
SEQRES 19 F 238 GLN ARG ASN ALA
SEQRES 1 G 129 MET ILE ARG ASN VAL LYS LYS GLN ARG PRO VAL ASN LEU
SEQRES 2 G 129 ASP LEU GLN THR ILE ARG PHE PRO ILE THR ALA ILE ALA
SEQRES 3 G 129 SER ILE LEU HIS ARG VAL SER GLY VAL ILE THR PHE VAL
SEQRES 4 G 129 ALA VAL GLY ILE LEU LEU TRP LEU LEU GLY THR SER LEU
SEQRES 5 G 129 SER SER PRO GLU GLY PHE GLU GLN ALA SER ALA ILE MET
SEQRES 6 G 129 GLY SER PHE PHE VAL LYS PHE ILE MET TRP GLY ILE LEU
SEQRES 7 G 129 THR ALA LEU ALA TYR HIS VAL VAL VAL GLY ILE ARG HIS
SEQRES 8 G 129 MET MET MET ASP PHE GLY TYR LEU GLU GLU THR PHE GLU
SEQRES 9 G 129 ALA GLY LYS ARG SER ALA LYS ILE SER PHE VAL ILE THR
SEQRES 10 G 129 VAL VAL LEU SER LEU LEU ALA GLY VAL LEU VAL TRP
SEQRES 1 H 115 MET VAL SER ASN ALA SER ALA LEU GLY ARG ASN GLY VAL
SEQRES 2 H 115 HIS ASP PHE ILE LEU VAL ARG ALA THR ALA ILE VAL LEU
SEQRES 3 H 115 THR LEU TYR ILE ILE TYR MET VAL GLY PHE PHE ALA THR
SEQRES 4 H 115 SER GLY GLU LEU THR TYR GLU VAL TRP ILE GLY PHE PHE
SEQRES 5 H 115 ALA SER ALA PHE THR LYS VAL PHE THR LEU LEU ALA LEU
SEQRES 6 H 115 PHE SER ILE LEU ILE HIS ALA TRP ILE GLY MET TRP GLN
SEQRES 7 H 115 VAL LEU THR ASP PHE VAL LYS PRO LEU ALA LEU ARG LEU
SEQRES 8 H 115 MET LEU GLN LEU VAL ILE VAL VAL ALA LEU VAL VAL TYR
SEQRES 9 H 115 VAL ILE TYR GLY PHE VAL VAL VAL TRP GLY VAL
SEQRES 1 I 588 MET LYS LEU PRO VAL ARG GLU PHE ASP ALA VAL VAL ILE
SEQRES 2 I 588 GLY ALA GLY GLY ALA GLY MET ARG ALA ALA LEU GLN ILE
SEQRES 3 I 588 SER GLN SER GLY GLN THR CYS ALA LEU LEU SER LYS VAL
SEQRES 4 I 588 PHE PRO THR ARG SER HIS THR VAL SER ALA GLN GLY GLY
SEQRES 5 I 588 ILE THR VAL ALA LEU GLY ASN THR HIS GLU ASP ASN TRP
SEQRES 6 I 588 GLU TRP HIS MET TYR ASP THR VAL LYS GLY SER ASP TYR
SEQRES 7 I 588 ILE GLY ASP GLN ASP ALA ILE GLU TYR MET CYS LYS THR
SEQRES 8 I 588 GLY PRO GLU ALA ILE LEU GLU LEU GLU HIS MET GLY LEU
SEQRES 9 I 588 PRO PHE SER ARG LEU ASP ASP GLY ARG ILE TYR GLN ARG
SEQRES 10 I 588 PRO PHE GLY GLY GLN SER LYS ASN PHE GLY GLY GLU GLN
SEQRES 11 I 588 ALA ALA ARG THR ALA ALA ALA ALA ASP ARG THR GLY HIS
SEQRES 12 I 588 ALA LEU LEU HIS THR LEU TYR GLN GLN ASN LEU LYS ASN
SEQRES 13 I 588 HIS THR THR ILE PHE SER GLU TRP TYR ALA LEU ASP LEU
SEQRES 14 I 588 VAL LYS ASN GLN ASP GLY ALA VAL VAL GLY CYS THR ALA
SEQRES 15 I 588 LEU CYS ILE GLU THR GLY GLU VAL VAL TYR PHE LYS ALA
SEQRES 16 I 588 ARG ALA THR VAL LEU ALA THR GLY GLY ALA GLY ARG ILE
SEQRES 17 I 588 TYR GLN SER THR THR ASN ALA HIS ILE ASN THR GLY ASP
SEQRES 18 I 588 GLY VAL GLY MET ALA ILE ARG ALA GLY VAL PRO VAL GLN
SEQRES 19 I 588 ASP MET GLU MET TRP GLN PHE HIS PRO THR GLY ILE ALA
SEQRES 20 I 588 GLY ALA GLY VAL LEU VAL THR GLU GLY CYS ARG GLY GLU
SEQRES 21 I 588 GLY GLY TYR LEU LEU ASN LYS HIS GLY GLU ARG PHE MET
SEQRES 22 I 588 GLU ARG TYR ALA PRO ASN ALA LYS ASP LEU ALA GLY ARG
SEQRES 23 I 588 ASP VAL VAL ALA ARG SER ILE MET ILE GLU ILE ARG GLU
SEQRES 24 I 588 GLY ARG GLY CYS ASP GLY PRO TRP GLY PRO HIS ALA LYS
SEQRES 25 I 588 LEU LYS LEU ASP HIS LEU GLY LYS GLU VAL LEU GLU SER
SEQRES 26 I 588 ARG LEU PRO GLY ILE LEU GLU LEU SER ARG THR PHE ALA
SEQRES 27 I 588 HIS VAL ASP PRO VAL LYS GLU PRO ILE PRO VAL ILE PRO
SEQRES 28 I 588 THR CYS HIS TYR MET MET GLY GLY ILE PRO THR LYS VAL
SEQRES 29 I 588 THR GLY GLN ALA LEU THR VAL ASN GLU LYS GLY GLU ASP
SEQRES 30 I 588 VAL VAL VAL PRO GLY LEU PHE ALA VAL GLY GLU ILE ALA
SEQRES 31 I 588 CYS VAL SER VAL HIS GLY ALA ASN ARG LEU GLY GLY ASN
SEQRES 32 I 588 SER LEU LEU ASP LEU VAL VAL PHE GLY ARG ALA ALA GLY
SEQRES 33 I 588 LEU HIS LEU GLN GLU SER ILE ALA GLU GLN GLY ALA LEU
SEQRES 34 I 588 ARG ASP ALA SER GLU SER ASP VAL GLU ALA SER LEU ASP
SEQRES 35 I 588 ARG LEU ASN ARG TRP ASN ASN ASN ARG ASN GLY GLU ASP
SEQRES 36 I 588 PRO VAL ALA ILE ARG LYS ALA LEU GLN GLU CYS MET GLN
SEQRES 37 I 588 HIS ASN PHE SER VAL PHE ARG GLU GLY ASP ALA MET ALA
SEQRES 38 I 588 LYS GLY LEU GLU GLN LEU LYS VAL ILE ARG GLU ARG LEU
SEQRES 39 I 588 LYS ASN ALA ARG LEU ASP ASP THR SER SER GLU PHE ASN
SEQRES 40 I 588 THR GLN ARG VAL GLU CYS LEU GLU LEU ASP ASN LEU MET
SEQRES 41 I 588 GLU THR ALA TYR ALA THR ALA VAL SER ALA ASN PHE ARG
SEQRES 42 I 588 THR GLU SER ARG GLY ALA HIS SER ARG PHE ASP PHE PRO
SEQRES 43 I 588 ASP ARG ASP ASP GLU ASN TRP LEU CYS HIS SER LEU TYR
SEQRES 44 I 588 LEU PRO GLU SER GLU SER MET THR ARG ARG SER VAL ASN
SEQRES 45 I 588 MET GLU PRO LYS LEU ARG PRO ALA PHE PRO PRO LYS ILE
SEQRES 46 I 588 ARG THR TYR
SEQRES 1 J 238 MET ARG LEU GLU PHE SER ILE TYR ARG TYR ASN PRO ASP
SEQRES 2 J 238 VAL ASP ASP ALA PRO ARG MET GLN ASP TYR THR LEU GLU
SEQRES 3 J 238 ALA ASP GLU GLY ARG ASP MET MET LEU LEU ASP ALA LEU
SEQRES 4 J 238 ILE GLN LEU LYS GLU LYS ASP PRO SER LEU SER PHE ARG
SEQRES 5 J 238 ARG SER CYS ARG GLU GLY VAL CYS GLY SER ASP GLY LEU
SEQRES 6 J 238 ASN MET ASN GLY LYS ASN GLY LEU ALA CYS ILE THR PRO
SEQRES 7 J 238 ILE SER ALA LEU ASN GLN PRO GLY LYS LYS ILE VAL ILE
SEQRES 8 J 238 ARG PRO LEU PRO GLY LEU PRO VAL ILE ARG ASP LEU VAL
SEQRES 9 J 238 VAL ASP MET GLY GLN PHE TYR ALA GLN TYR GLU LYS ILE
SEQRES 10 J 238 LYS PRO TYR LEU LEU ASN ASN GLY GLN ASN PRO PRO ALA
SEQRES 11 J 238 ARG GLU HIS LEU GLN MET PRO GLU GLN ARG GLU LYS LEU
SEQRES 12 J 238 ASP GLY LEU TYR GLU CYS ILE LEU CYS ALA CYS CYS SER
SEQRES 13 J 238 THR SER CYS PRO SER PHE TRP TRP ASN PRO ASP LYS PHE
SEQRES 14 J 238 ILE GLY PRO ALA GLY LEU LEU ALA ALA TYR ARG PHE LEU
SEQRES 15 J 238 ILE ASP SER ARG ASP THR GLU THR ASP SER ARG LEU ASP
SEQRES 16 J 238 GLY LEU SER ASP ALA PHE SER VAL PHE ARG CYS HIS SER
SEQRES 17 J 238 ILE MET ASN CYS VAL SER VAL CYS PRO LYS GLY LEU ASN
SEQRES 18 J 238 PRO THR ARG ALA ILE GLY HIS ILE LYS SER MET LEU LEU
SEQRES 19 J 238 GLN ARG ASN ALA
SEQRES 1 K 129 MET ILE ARG ASN VAL LYS LYS GLN ARG PRO VAL ASN LEU
SEQRES 2 K 129 ASP LEU GLN THR ILE ARG PHE PRO ILE THR ALA ILE ALA
SEQRES 3 K 129 SER ILE LEU HIS ARG VAL SER GLY VAL ILE THR PHE VAL
SEQRES 4 K 129 ALA VAL GLY ILE LEU LEU TRP LEU LEU GLY THR SER LEU
SEQRES 5 K 129 SER SER PRO GLU GLY PHE GLU GLN ALA SER ALA ILE MET
SEQRES 6 K 129 GLY SER PHE PHE VAL LYS PHE ILE MET TRP GLY ILE LEU
SEQRES 7 K 129 THR ALA LEU ALA TYR HIS VAL VAL VAL GLY ILE ARG HIS
SEQRES 8 K 129 MET MET MET ASP PHE GLY TYR LEU GLU GLU THR PHE GLU
SEQRES 9 K 129 ALA GLY LYS ARG SER ALA LYS ILE SER PHE VAL ILE THR
SEQRES 10 K 129 VAL VAL LEU SER LEU LEU ALA GLY VAL LEU VAL TRP
SEQRES 1 L 115 MET VAL SER ASN ALA SER ALA LEU GLY ARG ASN GLY VAL
SEQRES 2 L 115 HIS ASP PHE ILE LEU VAL ARG ALA THR ALA ILE VAL LEU
SEQRES 3 L 115 THR LEU TYR ILE ILE TYR MET VAL GLY PHE PHE ALA THR
SEQRES 4 L 115 SER GLY GLU LEU THR TYR GLU VAL TRP ILE GLY PHE PHE
SEQRES 5 L 115 ALA SER ALA PHE THR LYS VAL PHE THR LEU LEU ALA LEU
SEQRES 6 L 115 PHE SER ILE LEU ILE HIS ALA TRP ILE GLY MET TRP GLN
SEQRES 7 L 115 VAL LEU THR ASP PHE VAL LYS PRO LEU ALA LEU ARG LEU
SEQRES 8 L 115 MET LEU GLN LEU VAL ILE VAL VAL ALA LEU VAL VAL TYR
SEQRES 9 L 115 VAL ILE TYR GLY PHE VAL VAL VAL TRP GLY VAL
HET FAD A 601 53
HET NA A1589 1
HET TEO A1590 9
HET FES B 302 4
HET SF4 B 303 8
HET F3S B 304 7
HET CBE C1129 16
HET HEM C1130 43
HET FAD E 601 53
HET NA E1589 1
HET TEO E1590 9
HET FES F 302 4
HET SF4 F 303 8
HET F3S F 304 7
HET CBE G1129 16
HET HEM G1130 43
HET FAD I 601 53
HET NA I1589 1
HET TEO I1590 9
HET FES J 302 4
HET SF4 J 303 8
HET F3S J 304 7
HET CBE K1129 16
HET HEM K1130 43
HETNAM FAD FLAVIN-ADENINE DINUCLEOTIDE
HETNAM NA SODIUM ION
HETNAM TEO MALATE LIKE INTERMEDIATE
HETNAM FES FE2/S2 (INORGANIC) CLUSTER
HETNAM SF4 IRON/SULFUR CLUSTER
HETNAM F3S FE3-S4 CLUSTER
HETNAM CBE 2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-
HETNAM 2 CBE CARBOXAMIDE
HETNAM HEM PROTOPORPHYRIN IX CONTAINING FE
HETSYN CBE 5,6-DIHYDRO-2-METHYL-1,4-OXATHIIN-3-CARBOXANILID;
HETSYN 2 CBE CARBOXIN; CBX
HETSYN HEM HEME
FORMUL 13 FAD 3(C27 H33 N9 O15 P2)
FORMUL 14 NA 3(NA 1+)
FORMUL 15 TEO 3(C4 H4 O5 2-)
FORMUL 16 FES 3(FE2 S2)
FORMUL 17 SF4 3(FE4 S4)
FORMUL 18 F3S 3(FE3 S4)
FORMUL 19 CBE 3(C12 H13 N O2 S)
FORMUL 20 HEM 3(C34 H32 FE N4 O4)
HELIX 1 1 GLY A 16 SER A 29 1 14
HELIX 2 2 PHE A 40 SER A 44 5 5
HELIX 3 3 SER A 44 ALA A 49 5 6
HELIX 4 4 ASN A 64 SER A 76 1 13
HELIX 5 5 ASP A 81 GLY A 103 1 23
HELIX 6 6 ARG A 140 ASN A 156 1 17
HELIX 7 7 ALA A 205 TYR A 209 5 5
HELIX 8 8 GLY A 220 ALA A 229 1 10
HELIX 9 9 GLU A 255 GLU A 260 1 6
HELIX 10 10 PHE A 272 ALA A 277 1 6
HELIX 11 11 ALA A 280 ALA A 284 5 5
HELIX 12 12 GLY A 285 GLU A 299 1 15
HELIX 13 13 LEU A 315 LEU A 318 5 4
HELIX 14 14 GLY A 319 LEU A 327 1 9
HELIX 15 15 LEU A 327 ALA A 338 1 12
HELIX 16 16 GLY A 402 HIS A 418 1 17
HELIX 17 17 HIS A 418 GLY A 427 1 10
HELIX 18 18 SER A 433 ASN A 450 1 18
HELIX 19 19 ASP A 455 PHE A 471 1 17
HELIX 20 20 GLU A 476 LYS A 495 1 20
HELIX 21 21 ASN A 507 ARG A 533 1 27
HELIX 22 22 MET B 34 ASP B 46 1 13
HELIX 23 23 CYS B 75 THR B 77 5 3
HELIX 24 24 PRO B 78 ASN B 83 1 6
HELIX 25 25 MET B 107 ILE B 117 1 11
HELIX 26 26 MET B 136 GLU B 141 1 6
HELIX 27 27 LYS B 142 ASP B 144 5 3
HELIX 28 28 CYS B 155 SER B 158 5 4
HELIX 29 29 CYS B 159 ASN B 165 1 7
HELIX 30 30 GLY B 171 ILE B 183 1 13
HELIX 31 31 GLU B 189 GLY B 196 1 8
HELIX 32 32 MET B 210 CYS B 216 1 7
HELIX 33 33 ASN B 221 ALA B 238 1 18
HELIX 34 34 ASP C 14 ILE C 18 5 5
HELIX 35 35 PRO C 21 SER C 54 1 34
HELIX 36 36 SER C 54 SER C 67 1 14
HELIX 37 37 SER C 67 PHE C 96 1 30
HELIX 38 38 THR C 102 VAL C 128 1 27
HELIX 39 39 ASN D 11 ALA D 38 1 28
HELIX 40 40 THR D 44 SER D 54 1 11
HELIX 41 41 SER D 54 VAL D 84 1 31
HELIX 42 42 PRO D 86 GLY D 114 1 29
HELIX 43 43 GLY E 16 SER E 29 1 14
HELIX 44 44 PHE E 40 SER E 44 5 5
HELIX 45 45 SER E 44 ALA E 49 5 6
HELIX 46 46 ASN E 64 SER E 76 1 13
HELIX 47 47 ASP E 81 MET E 102 1 22
HELIX 48 48 ARG E 140 ASN E 156 1 17
HELIX 49 49 ALA E 205 TYR E 209 5 5
HELIX 50 50 GLY E 220 ALA E 229 1 10
HELIX 51 51 GLU E 255 GLU E 260 1 6
HELIX 52 52 PHE E 272 ALA E 277 1 6
HELIX 53 53 ALA E 280 ALA E 284 5 5
HELIX 54 54 GLY E 285 GLU E 299 1 15
HELIX 55 55 LEU E 315 LEU E 318 5 4
HELIX 56 56 GLY E 319 LEU E 327 1 9
HELIX 57 57 LEU E 327 HIS E 339 1 13
HELIX 58 58 GLY E 402 GLY E 427 1 26
HELIX 59 59 SER E 433 ASN E 450 1 18
HELIX 60 60 ASP E 455 PHE E 471 1 17
HELIX 61 61 GLU E 476 LYS E 495 1 20
HELIX 62 62 ASN E 507 ARG E 533 1 27
HELIX 63 63 MET F 34 ASP F 46 1 13
HELIX 64 64 PRO F 78 ASN F 83 1 6
HELIX 65 65 MET F 107 ILE F 117 1 11
HELIX 66 66 MET F 136 GLU F 141 1 6
HELIX 67 67 LYS F 142 ASP F 144 5 3
HELIX 68 68 CYS F 155 SER F 158 5 4
HELIX 69 69 CYS F 159 ASN F 165 1 7
HELIX 70 70 GLY F 171 ILE F 183 1 13
HELIX 71 71 GLU F 189 GLY F 196 1 8
HELIX 72 72 MET F 210 CYS F 216 1 7
HELIX 73 73 ASN F 221 ALA F 238 1 18
HELIX 74 74 ASP G 14 ILE G 18 5 5
HELIX 75 75 PRO G 21 SER G 54 1 34
HELIX 76 76 SER G 54 SER G 67 1 14
HELIX 77 77 SER G 67 PHE G 96 1 30
HELIX 78 78 THR G 102 VAL G 128 1 27
HELIX 79 79 ASN H 11 THR H 39 1 29
HELIX 80 80 THR H 44 SER H 54 1 11
HELIX 81 81 SER H 54 VAL H 84 1 31
HELIX 82 82 PRO H 86 GLY H 114 1 29
HELIX 83 83 GLY I 16 SER I 29 1 14
HELIX 84 84 PHE I 40 SER I 44 5 5
HELIX 85 85 SER I 44 ALA I 49 5 6
HELIX 86 86 ASN I 64 SER I 76 1 13
HELIX 87 87 ASP I 81 MET I 102 1 22
HELIX 88 88 ARG I 140 ASN I 156 1 17
HELIX 89 89 ALA I 205 TYR I 209 5 5
HELIX 90 90 GLY I 220 ALA I 229 1 10
HELIX 91 91 GLU I 255 GLU I 260 1 6
HELIX 92 92 PHE I 272 ALA I 277 1 6
HELIX 93 93 ALA I 280 ALA I 284 5 5
HELIX 94 94 GLY I 285 GLU I 299 1 15
HELIX 95 95 LEU I 315 LEU I 318 5 4
HELIX 96 96 GLY I 319 LEU I 327 1 9
HELIX 97 97 LEU I 327 ALA I 338 1 12
HELIX 98 98 GLY I 402 HIS I 418 1 17
HELIX 99 99 HIS I 418 GLY I 427 1 10
HELIX 100 100 SER I 433 ASN I 450 1 18
HELIX 101 101 ASP I 455 PHE I 471 1 17
HELIX 102 102 GLU I 476 LYS I 495 1 20
HELIX 103 103 ASN I 507 ARG I 533 1 27
HELIX 104 104 MET J 34 ASP J 46 1 13
HELIX 105 105 CYS J 75 THR J 77 5 3
HELIX 106 106 PRO J 78 ASN J 83 1 6
HELIX 107 107 MET J 107 ILE J 117 1 11
HELIX 108 108 MET J 136 LYS J 142 1 7
HELIX 109 109 CYS J 155 SER J 158 5 4
HELIX 110 110 CYS J 159 ASN J 165 1 7
HELIX 111 111 GLY J 171 ILE J 183 1 13
HELIX 112 112 GLU J 189 GLY J 196 1 8
HELIX 113 113 MET J 210 CYS J 216 1 7
HELIX 114 114 ASN J 221 ALA J 238 1 18
HELIX 115 115 ASP K 14 ILE K 18 5 5
HELIX 116 116 PRO K 21 SER K 54 1 34
HELIX 117 117 SER K 54 SER K 67 1 14
HELIX 118 118 SER K 67 PHE K 96 1 30
HELIX 119 119 THR K 102 VAL K 128 1 27
HELIX 120 120 ASN L 11 THR L 39 1 29
HELIX 121 121 THR L 44 SER L 54 1 11
HELIX 122 122 SER L 54 VAL L 84 1 31
HELIX 123 123 PRO L 86 GLY L 114 1 29
SHEET 1 AA 4 VAL A 5 GLU A 7 0
SHEET 2 AA 4 VAL A 190 LYS A 194 1 O TYR A 192 N ARG A 6
SHEET 3 AA 4 VAL A 177 CYS A 184 -1 O CYS A 180 N PHE A 193
SHEET 4 AA 4 TRP A 164 LYS A 171 -1 O TYR A 165 N LEU A 183
SHEET 1 AB 6 THR A 159 SER A 162 0
SHEET 2 AB 6 CYS A 33 SER A 37 1 O CYS A 33 N THR A 159
SHEET 3 AB 6 ALA A 10 ILE A 13 1 O ALA A 10 N ALA A 34
SHEET 4 AB 6 ALA A 197 LEU A 200 1 O ALA A 197 N VAL A 11
SHEET 5 AB 6 ASP A 377 ALA A 385 1 O GLY A 382 N THR A 198
SHEET 6 AB 6 GLN A 367 VAL A 371 -1 O ALA A 368 N VAL A 380
SHEET 1 AC 3 ILE A 53 THR A 54 0
SHEET 2 AC 3 GLN A 130 ALA A 135 -1 O ALA A 135 N ILE A 53
SHEET 3 AC 3 GLN A 116 SER A 123 -1 O ARG A 117 N THR A 134
SHEET 1 AD 3 VAL A 233 GLN A 234 0
SHEET 2 AD 3 CYS A 555 LEU A 560 -1 O TYR A 559 N VAL A 233
SHEET 3 AD 3 SER A 565 SER A 570 -1 O SER A 565 N LEU A 560
SHEET 1 AE 4 TRP A 239 ILE A 246 0
SHEET 2 AE 4 ILE A 347 MET A 356 -1 O ILE A 350 N GLY A 245
SHEET 3 AE 4 ALA A 311 LYS A 314 -1 O ALA A 311 N VAL A 349
SHEET 4 AE 4 TYR A 263 LEU A 265 -1 O TYR A 263 N LYS A 314
SHEET 1 AF 2 ILE A 360 PRO A 361 0
SHEET 2 AF 2 ALA A 390 CYS A 391 1 N CYS A 391 O ILE A 360
SHEET 1 BA 5 ARG B 19 GLU B 26 0
SHEET 2 BA 5 ARG B 2 ARG B 9 -1 O LEU B 3 N LEU B 25
SHEET 3 BA 5 ILE B 89 ARG B 92 1 O ILE B 89 N SER B 6
SHEET 4 BA 5 GLY B 64 MET B 67 -1 O ASN B 66 N ARG B 92
SHEET 5 BA 5 LYS B 70 LEU B 73 -1 O LYS B 70 N MET B 67
SHEET 1 BB 2 VAL B 99 ARG B 101 0
SHEET 2 BB 2 VAL B 104 VAL B 105 -1 O VAL B 104 N ILE B 100
SHEET 1 EA 4 VAL E 5 GLU E 7 0
SHEET 2 EA 4 VAL E 190 LYS E 194 1 O TYR E 192 N ARG E 6
SHEET 3 EA 4 VAL E 177 CYS E 184 -1 O CYS E 180 N PHE E 193
SHEET 4 EA 4 TRP E 164 LYS E 171 -1 O TYR E 165 N LEU E 183
SHEET 1 EB 6 THR E 159 SER E 162 0
SHEET 2 EB 6 CYS E 33 SER E 37 1 O CYS E 33 N THR E 159
SHEET 3 EB 6 ALA E 10 ILE E 13 1 O ALA E 10 N ALA E 34
SHEET 4 EB 6 ALA E 197 LEU E 200 1 O ALA E 197 N VAL E 11
SHEET 5 EB 6 ASP E 377 ALA E 385 1 O GLY E 382 N THR E 198
SHEET 6 EB 6 GLN E 367 VAL E 371 -1 O ALA E 368 N VAL E 380
SHEET 1 EC 3 ILE E 53 THR E 54 0
SHEET 2 EC 3 THR E 134 ALA E 135 -1 O ALA E 135 N ILE E 53
SHEET 3 EC 3 GLN E 116 ARG E 117 -1 O ARG E 117 N THR E 134
SHEET 1 ED 3 VAL E 233 GLN E 234 0
SHEET 2 ED 3 CYS E 555 LEU E 560 -1 O TYR E 559 N VAL E 233
SHEET 3 ED 3 SER E 565 SER E 570 -1 O SER E 565 N LEU E 560
SHEET 1 EE 4 TRP E 239 ILE E 246 0
SHEET 2 EE 4 ILE E 347 MET E 356 -1 O ILE E 350 N GLY E 245
SHEET 3 EE 4 ALA E 311 LYS E 314 -1 O ALA E 311 N VAL E 349
SHEET 4 EE 4 TYR E 263 LEU E 265 -1 O TYR E 263 N LYS E 314
SHEET 1 EF 2 ILE E 360 PRO E 361 0
SHEET 2 EF 2 ALA E 390 CYS E 391 1 N CYS E 391 O ILE E 360
SHEET 1 FA 5 ARG F 19 GLU F 26 0
SHEET 2 FA 5 ARG F 2 ARG F 9 -1 O LEU F 3 N LEU F 25
SHEET 3 FA 5 ILE F 89 ARG F 92 1 O ILE F 89 N SER F 6
SHEET 4 FA 5 GLY F 64 MET F 67 -1 O ASN F 66 N ARG F 92
SHEET 5 FA 5 LYS F 70 LEU F 73 -1 O LYS F 70 N MET F 67
SHEET 1 FB 2 VAL F 99 ARG F 101 0
SHEET 2 FB 2 VAL F 104 VAL F 105 -1 O VAL F 104 N ILE F 100
SHEET 1 IA 6 THR I 159 SER I 162 0
SHEET 2 IA 6 CYS I 33 SER I 37 1 O CYS I 33 N THR I 159
SHEET 3 IA 6 VAL I 5 ILE I 13 1 O ALA I 10 N ALA I 34
SHEET 4 IA 6 VAL I 190 LEU I 200 1 O TYR I 192 N ARG I 6
SHEET 5 IA 6 ASP I 377 ALA I 385 -1 O GLY I 382 N THR I 198
SHEET 6 IA 6 GLN I 367 VAL I 371 1 O ALA I 368 N VAL I 380
SHEET 1 IB 6 THR I 159 SER I 162 0
SHEET 2 IB 6 CYS I 33 SER I 37 1 O CYS I 33 N THR I 159
SHEET 3 IB 6 VAL I 5 ILE I 13 1 O ALA I 10 N ALA I 34
SHEET 4 IB 6 VAL I 190 LEU I 200 1 O TYR I 192 N ARG I 6
SHEET 5 IB 6 VAL I 177 CYS I 184 -1 O VAL I 178 N ALA I 195
SHEET 6 IB 6 TRP I 164 LYS I 171 -1 O TYR I 165 N LEU I 183
SHEET 1 IC 3 ILE I 53 THR I 54 0
SHEET 2 IC 3 GLN I 130 ALA I 135 -1 O ALA I 135 N ILE I 53
SHEET 3 IC 3 GLN I 116 SER I 123 -1 O ARG I 117 N THR I 134
SHEET 1 ID 3 VAL I 233 GLN I 234 0
SHEET 2 ID 3 CYS I 555 LEU I 560 -1 O TYR I 559 N VAL I 233
SHEET 3 ID 3 SER I 565 SER I 570 -1 O SER I 565 N LEU I 560
SHEET 1 IE 4 TRP I 239 ILE I 246 0
SHEET 2 IE 4 ILE I 347 MET I 356 -1 O ILE I 350 N GLY I 245
SHEET 3 IE 4 ALA I 311 LYS I 314 -1 O ALA I 311 N VAL I 349
SHEET 4 IE 4 TYR I 263 LEU I 265 -1 O TYR I 263 N LYS I 314
SHEET 1 IF 2 ILE I 360 PRO I 361 0
SHEET 2 IF 2 ALA I 390 CYS I 391 1 N CYS I 391 O ILE I 360
SHEET 1 JA 5 ARG J 19 GLU J 26 0
SHEET 2 JA 5 ARG J 2 ARG J 9 -1 O LEU J 3 N LEU J 25
SHEET 3 JA 5 ILE J 89 ARG J 92 1 O ILE J 89 N SER J 6
SHEET 4 JA 5 GLY J 64 MET J 67 -1 O ASN J 66 N ARG J 92
SHEET 5 JA 5 LYS J 70 LEU J 73 -1 O LYS J 70 N MET J 67
SHEET 1 JB 2 VAL J 99 ARG J 101 0
SHEET 2 JB 2 VAL J 104 VAL J 105 -1 O VAL J 104 N ILE J 100
LINK O MET A 356 NA NA A1589 1555 1555 2.65
LINK O MET A 357 NA NA A1589 1555 1555 2.92
LINK O GLY A 358 NA NA A1589 1555 1555 2.51
LINK O GLU A 388 NA NA A1589 1555 1555 2.32
LINK O ALA A 390 NA NA A1589 1555 1555 2.60
LINK SG CYS B 55 FE1 FES B 302 1555 1555 2.32
LINK SG CYS B 60 FE1 FES B 302 1555 1555 2.25
LINK OD1 ASP B 63 FE2 FES B 302 1555 1555 1.82
LINK SG CYS B 75 FE2 FES B 302 1555 1555 2.29
LINK SG CYS B 149 FE3 SF4 B 303 1555 1555 2.27
LINK SG CYS B 152 FE4 SF4 B 303 1555 1555 2.33
LINK SG CYS B 155 FE1 SF4 B 303 1555 1555 2.30
LINK SG CYS B 159 FE1 F3S B 304 1555 1555 2.28
LINK SG CYS B 206 FE3 F3S B 304 1555 1555 2.29
LINK SG CYS B 212 FE4 F3S B 304 1555 1555 2.32
LINK SG CYS B 216 FE2 SF4 B 303 1555 1555 2.26
LINK NE2 HIS C 84 FE HEM C1130 1555 1555 1.93
LINK FE HEM C1130 NE2 HIS D 71 1555 1555 1.95
LINK O MET E 356 NA NA E1589 1555 1555 2.67
LINK O MET E 357 NA NA E1589 1555 1555 2.96
LINK O GLY E 358 NA NA E1589 1555 1555 2.39
LINK O GLU E 388 NA NA E1589 1555 1555 2.36
LINK O ALA E 390 NA NA E1589 1555 1555 2.60
LINK SG CYS F 55 FE1 FES F 302 1555 1555 2.30
LINK SG CYS F 60 FE1 FES F 302 1555 1555 2.28
LINK OD1 ASP F 63 FE2 FES F 302 1555 1555 1.82
LINK SG CYS F 75 FE2 FES F 302 1555 1555 2.25
LINK SG CYS F 149 FE3 SF4 F 303 1555 1555 2.30
LINK SG CYS F 152 FE4 SF4 F 303 1555 1555 2.28
LINK SG CYS F 155 FE1 SF4 F 303 1555 1555 2.32
LINK SG CYS F 159 FE1 F3S F 304 1555 1555 2.27
LINK SG CYS F 206 FE3 F3S F 304 1555 1555 2.26
LINK SG CYS F 212 FE4 F3S F 304 1555 1555 2.32
LINK SG CYS F 216 FE2 SF4 F 303 1555 1555 2.27
LINK NE2 HIS G 84 FE HEM G1130 1555 1555 1.93
LINK FE HEM G1130 NE2 HIS H 71 1555 1555 1.93
LINK O MET I 356 NA NA I1589 1555 1555 2.81
LINK O MET I 357 NA NA I1589 1555 1555 3.17
LINK O GLY I 358 NA NA I1589 1555 1555 2.82
LINK O GLU I 388 NA NA I1589 1555 1555 2.31
LINK O ALA I 390 NA NA I1589 1555 1555 2.51
LINK SG CYS J 55 FE1 FES J 302 1555 1555 2.50
LINK SG CYS J 60 FE1 FES J 302 1555 1555 2.29
LINK OD1 ASP J 63 FE2 FES J 302 1555 1555 1.82
LINK SG CYS J 75 FE2 FES J 302 1555 1555 2.28
LINK SG CYS J 149 FE3 SF4 J 303 1555 1555 2.34
LINK SG CYS J 152 FE4 SF4 J 303 1555 1555 2.29
LINK SG CYS J 155 FE1 SF4 J 303 1555 1555 2.30
LINK SG CYS J 159 FE1 F3S J 304 1555 1555 2.29
LINK SG CYS J 206 FE3 F3S J 304 1555 1555 2.32
LINK SG CYS J 212 FE4 F3S J 304 1555 1555 2.60
LINK SG CYS J 216 FE2 SF4 J 303 1555 1555 2.29
LINK NE2 HIS K 84 FE HEM K1130 1555 1555 1.98
LINK FE HEM K1130 NE2 HIS L 71 1555 1555 1.95
CISPEP 1 VAL A 392 SER A 393 0 9.17
CISPEP 2 VAL E 392 SER E 393 0 7.23
CISPEP 3 VAL I 392 SER I 393 0 7.44
SITE 1 AC1 35 GLY A 14 ALA A 15 GLY A 16 GLY A 17
SITE 2 AC1 35 ALA A 18 SER A 37 LYS A 38 VAL A 39
SITE 3 AC1 35 SER A 44 HIS A 45 THR A 46 SER A 48
SITE 4 AC1 35 ALA A 49 GLN A 50 GLY A 51 GLY A 52
SITE 5 AC1 35 TRP A 164 ALA A 166 ALA A 201 THR A 202
SITE 6 AC1 35 GLY A 203 THR A 213 ASP A 221 LEU A 252
SITE 7 AC1 35 HIS A 354 TYR A 355 GLY A 387 GLU A 388
SITE 8 AC1 35 ARG A 399 GLY A 402 ASN A 403 SER A 404
SITE 9 AC1 35 LEU A 405 LEU A 408 TEO A1590
SITE 1 AC2 8 SER B 54 CYS B 55 ARG B 56 GLY B 58
SITE 2 AC2 8 CYS B 60 GLY B 61 ASP B 63 CYS B 75
SITE 1 AC3 8 CYS B 149 ILE B 150 CYS B 152 ALA B 153
SITE 2 AC3 8 CYS B 155 ALA B 173 CYS B 216 PRO B 217
SITE 1 AC4 9 CYS B 159 CYS B 206 HIS B 207 SER B 208
SITE 2 AC4 9 ILE B 209 MET B 210 ASN B 211 CYS B 212
SITE 3 AC4 9 THR B 223
SITE 1 AC5 37 GLY E 14 ALA E 15 GLY E 16 GLY E 17
SITE 2 AC5 37 ALA E 18 SER E 37 LYS E 38 VAL E 39
SITE 3 AC5 37 SER E 44 HIS E 45 THR E 46 SER E 48
SITE 4 AC5 37 ALA E 49 GLN E 50 GLY E 51 GLY E 52
SITE 5 AC5 37 TRP E 164 TYR E 165 ALA E 166 ALA E 201
SITE 6 AC5 37 THR E 202 GLY E 203 THR E 213 ASN E 214
SITE 7 AC5 37 ASP E 221 LEU E 252 HIS E 354 TYR E 355
SITE 8 AC5 37 GLY E 387 GLU E 388 ARG E 399 GLY E 402
SITE 9 AC5 37 ASN E 403 SER E 404 LEU E 405 LEU E 408
SITE 10 AC5 37 TEO E1590
SITE 1 AC6 9 SER F 54 CYS F 55 ARG F 56 GLY F 58
SITE 2 AC6 9 VAL F 59 CYS F 60 GLY F 61 ASP F 63
SITE 3 AC6 9 CYS F 75
SITE 1 AC7 7 CYS F 149 ILE F 150 CYS F 152 ALA F 153
SITE 2 AC7 7 CYS F 155 CYS F 216 PRO F 217
SITE 1 AC8 9 CYS F 159 CYS F 206 HIS F 207 SER F 208
SITE 2 AC8 9 ILE F 209 MET F 210 ASN F 211 CYS F 212
SITE 3 AC8 9 THR F 223
SITE 1 AC9 37 ILE I 13 GLY I 14 ALA I 15 GLY I 16
SITE 2 AC9 37 GLY I 17 ALA I 18 SER I 37 LYS I 38
SITE 3 AC9 37 VAL I 39 SER I 44 HIS I 45 THR I 46
SITE 4 AC9 37 SER I 48 ALA I 49 GLN I 50 GLY I 51
SITE 5 AC9 37 GLY I 52 TRP I 164 TYR I 165 ALA I 166
SITE 6 AC9 37 ALA I 201 THR I 202 GLY I 203 THR I 213
SITE 7 AC9 37 ASP I 221 LEU I 252 HIS I 354 TYR I 355
SITE 8 AC9 37 GLY I 387 GLU I 388 ARG I 399 GLY I 402
SITE 9 AC9 37 ASN I 403 SER I 404 LEU I 405 LEU I 408
SITE 10 AC9 37 TEO I1590
SITE 1 BC1 9 SER J 54 CYS J 55 ARG J 56 GLY J 58
SITE 2 BC1 9 VAL J 59 CYS J 60 GLY J 61 ASP J 63
SITE 3 BC1 9 CYS J 75
SITE 1 BC2 9 CYS J 149 ILE J 150 CYS J 152 ALA J 153
SITE 2 BC2 9 CYS J 154 CYS J 155 CYS J 216 PRO J 217
SITE 3 BC2 9 LEU J 220
SITE 1 BC3 8 CYS J 159 CYS J 206 HIS J 207 SER J 208
SITE 2 BC3 8 ILE J 209 MET J 210 CYS J 212 THR J 223
SITE 1 BC4 5 MET A 356 MET A 357 GLY A 358 GLU A 388
SITE 2 BC4 5 ALA A 390
SITE 1 BC5 5 MET E 356 MET E 357 GLY E 358 GLU E 388
SITE 2 BC5 5 ALA E 390
SITE 1 BC6 6 TYR I 355 MET I 356 MET I 357 GLY I 358
SITE 2 BC6 6 GLU I 388 ALA I 390
SITE 1 BC7 9 SER B 161 TRP B 164 HIS B 207 PHE C 20
SITE 2 BC7 9 SER C 27 ILE C 28 ARG C 31 HEM C1130
SITE 3 BC7 9 ASP D 82
SITE 1 BC8 10 PRO F 160 SER F 161 TRP F 164 HIS F 207
SITE 2 BC8 10 PHE G 20 SER G 27 ILE G 28 ARG G 31
SITE 3 BC8 10 HEM G1130 ASP H 82
SITE 1 BC9 10 PRO J 160 SER J 161 TRP J 164 HIS J 207
SITE 2 BC9 10 ILE J 209 SER K 27 ILE K 28 ARG K 31
SITE 3 BC9 10 HEM K1130 ASP L 82
SITE 1 CC1 17 HIS B 207 HIS C 30 ARG C 31 GLY C 34
SITE 2 CC1 17 THR C 37 PHE C 38 HIS C 84 VAL C 85
SITE 3 CC1 17 GLY C 88 HIS C 91 CBE C1129 ALA D 23
SITE 4 CC1 17 THR D 27 HIS D 71 ALA D 72 GLY D 75
SITE 5 CC1 17 GLN D 78
SITE 1 CC2 11 GLN A 50 GLY A 51 HIS A 242 THR A 254
SITE 2 CC2 11 GLU A 255 ARG A 286 HIS A 354 ARG A 399
SITE 3 CC2 11 GLY A 401 GLY A 402 FAD A 601
SITE 1 CC3 18 HIS F 207 HIS G 30 ARG G 31 THR G 37
SITE 2 CC3 18 PHE G 38 HIS G 84 VAL G 85 GLY G 88
SITE 3 CC3 18 HIS G 91 CBE G1129 ARG H 20 ALA H 23
SITE 4 CC3 18 LEU H 26 THR H 27 HIS H 71 GLY H 75
SITE 5 CC3 18 GLN H 78 VAL H 79
SITE 1 CC4 11 GLN E 50 GLY E 51 HIS E 242 THR E 254
SITE 2 CC4 11 GLU E 255 ARG E 286 HIS E 354 ARG E 399
SITE 3 CC4 11 GLY E 401 GLY E 402 FAD E 601
SITE 1 CC5 16 HIS J 207 HIS K 30 ARG K 31 GLY K 34
SITE 2 CC5 16 HIS K 84 GLY K 88 ILE K 89 HIS K 91
SITE 3 CC5 16 CBE K1129 ARG L 20 ALA L 23 THR L 27
SITE 4 CC5 16 HIS L 71 GLY L 75 MET L 76 VAL L 79
SITE 1 CC6 12 GLN I 50 GLY I 51 HIS I 242 LEU I 252
SITE 2 CC6 12 THR I 254 GLU I 255 ARG I 286 HIS I 354
SITE 3 CC6 12 ARG I 399 GLY I 401 GLY I 402 FAD I 601
CRYST1 119.850 184.710 203.310 90.00 90.00 90.00 P 21 21 21 12
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.008344 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005414 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004919 0.00000
MTRIX1 1 0.944920 0.286190 0.158790 18.50396 1
MTRIX2 1 0.280930 -0.460290 -0.842150 -97.15851 1
MTRIX3 1 -0.167930 0.840380 -0.515330 -30.96337 1
MTRIX1 2 0.947030 0.281600 -0.154360 4.53321 1
MTRIX2 2 0.271360 -0.444710 0.853580 -22.49522 1
MTRIX3 2 0.171720 -0.850260 -0.497570 -101.68967 1
MTRIX1 3 0.948050 0.280950 0.149250 18.16462 1
MTRIX2 3 0.269630 -0.460630 -0.845650 -97.08932 1
MTRIX3 3 -0.168830 0.841960 -0.512450 -30.90920 1
MTRIX1 4 0.944650 0.281700 -0.168170 4.26520 1
MTRIX2 4 0.284180 -0.446440 0.848490 -23.09317 1
MTRIX3 4 0.163940 -0.849320 -0.501780 -101.58215 1
MTRIX1 5 0.947330 0.284720 0.146660 18.24940 1
MTRIX2 5 0.268410 -0.455980 -0.848550 -97.04973 1
MTRIX3 5 -0.174720 0.843220 -0.508380 -30.63527 1
MTRIX1 6 0.942310 0.283180 -0.178510 4.07432 1
MTRIX2 6 0.294860 -0.449710 0.843100 -23.69032 1
MTRIX3 6 0.158470 -0.847100 -0.507260 -101.56531 1
MTRIX1 7 0.946190 0.286880 0.149750 18.46492 1
MTRIX2 7 0.271140 -0.450210 -0.850760 -97.26530 1
MTRIX3 7 -0.176650 0.845580 -0.503770 -30.37287 1
MTRIX1 8 0.944100 0.276930 -0.178820 3.82943 1
MTRIX2 8 0.290680 -0.443530 0.847810 -23.20065 1
MTRIX3 8 0.155480 -0.852400 -0.499240 -101.13769 1
(ATOM LINES ARE NOT SHOWN.)
END
