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PDBsum entry 1sqv

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Top Page protein ligands Protein-protein interface(s) links
Oxidoreductase PDB id
1sqv
Jmol
Contents
Protein chains
446 a.a.
423 a.a.
378 a.a.
241 a.a.
196 a.a.
105 a.a.
75 a.a.
67 a.a.
57 a.a.
61 a.a.
51 a.a.
Ligands
HEM ×3
UHD
UQ2
FES
Waters ×291
HEADER    OXIDOREDUCTASE                          19-MAR-04   1SQV
TITLE     CRYSTAL STRUCTURE ANALYSIS OF BOVINE BC1 WITH UHDBT
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I,
COMPND   3 MITOCHONDRIAL;
COMPND   4 CHAIN: A;
COMPND   5 SYNONYM: COMPLEX III SUBUNIT I;
COMPND   6 EC: 1.10.2.2;
COMPND   7 MOL_ID: 2;
COMPND   8 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2,
COMPND   9 MITOCHONDRIAL;
COMPND  10 CHAIN: B;
COMPND  11 SYNONYM: COMPLEX III SUBUNIT II;
COMPND  12 EC: 1.10.2.2;
COMPND  13 MOL_ID: 3;
COMPND  14 MOLECULE: CYTOCHROME B;
COMPND  15 CHAIN: C;
COMPND  16 EC: 1.10.2.2;
COMPND  17 MOL_ID: 4;
COMPND  18 MOLECULE: CYTOCHROME C1, HEME PROTEIN, MITOCHONDRIAL;
COMPND  19 CHAIN: D;
COMPND  20 SYNONYM: CYTOCHROME C-1;
COMPND  21 EC: 1.10.2.2;
COMPND  22 MOL_ID: 5;
COMPND  23 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT;
COMPND  24 CHAIN: E;
COMPND  25 SYNONYM: COMPLEX III SUBUNIT IX;
COMPND  26 EC: 1.10.2.2;
COMPND  27 MOL_ID: 6;
COMPND  28 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 14 KDA PROTEIN;
COMPND  29 CHAIN: F;
COMPND  30 SYNONYM: COMPLEX III SUBUNIT VI;
COMPND  31 EC: 1.10.2.2;
COMPND  32 MOL_ID: 7;
COMPND  33 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX UBIQUINONE-BINDING
COMPND  34 PROTEIN QP-C;
COMPND  35 CHAIN: G;
COMPND  36 SYNONYM: COMPLEX III SUBUNIT VII;
COMPND  37 EC: 1.10.2.2;
COMPND  38 MOL_ID: 8;
COMPND  39 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 11 KDA PROTEIN;
COMPND  40 CHAIN: H;
COMPND  41 SYNONYM: COMPLEX III SUBUNIT VIII;
COMPND  42 EC: 1.10.2.2;
COMPND  43 MOL_ID: 9;
COMPND  44 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 8 KDA PROTEIN;
COMPND  45 CHAIN: I;
COMPND  46 SYNONYM: COMPLEX III SUBUNIT IX;
COMPND  47 EC: 1.10.2.2;
COMPND  48 MOL_ID: 10;
COMPND  49 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 7.2 KDA PROTEIN;
COMPND  50 CHAIN: J;
COMPND  51 SYNONYM: COMPLEX III SUBUNIT X;
COMPND  52 EC: 1.10.2.2;
COMPND  53 MOL_ID: 11;
COMPND  54 MOLECULE: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX 6.4 KDA PROTEIN;
COMPND  55 CHAIN: K;
COMPND  56 SYNONYM: COMPLEX III SUBUNIT XI;
COMPND  57 EC: 1.10.2.2
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   3 ORGANISM_COMMON: CATTLE;
SOURCE   4 ORGANISM_TAXID: 9913;
SOURCE   5 MOL_ID: 2;
SOURCE   6 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   7 ORGANISM_COMMON: CATTLE;
SOURCE   8 ORGANISM_TAXID: 9913;
SOURCE   9 MOL_ID: 3;
SOURCE  10 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  11 ORGANISM_COMMON: CATTLE;
SOURCE  12 ORGANISM_TAXID: 9913;
SOURCE  13 MOL_ID: 4;
SOURCE  14 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  15 ORGANISM_COMMON: CATTLE;
SOURCE  16 ORGANISM_TAXID: 9913;
SOURCE  17 MOL_ID: 5;
SOURCE  18 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  19 ORGANISM_COMMON: CATTLE;
SOURCE  20 ORGANISM_TAXID: 9913;
SOURCE  21 MOL_ID: 6;
SOURCE  22 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  23 ORGANISM_COMMON: CATTLE;
SOURCE  24 ORGANISM_TAXID: 9913;
SOURCE  25 MOL_ID: 7;
SOURCE  26 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  27 ORGANISM_COMMON: CATTLE;
SOURCE  28 ORGANISM_TAXID: 9913;
SOURCE  29 MOL_ID: 8;
SOURCE  30 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  31 ORGANISM_COMMON: CATTLE;
SOURCE  32 ORGANISM_TAXID: 9913;
SOURCE  33 MOL_ID: 9;
SOURCE  34 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  35 ORGANISM_COMMON: CATTLE;
SOURCE  36 ORGANISM_TAXID: 9913;
SOURCE  37 MOL_ID: 10;
SOURCE  38 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  39 ORGANISM_COMMON: CATTLE;
SOURCE  40 ORGANISM_TAXID: 9913;
SOURCE  41 MOL_ID: 11;
SOURCE  42 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  43 ORGANISM_COMMON: CATTLE;
SOURCE  44 ORGANISM_TAXID: 9913
KEYWDS    CYTOCHROME BC1, QO INHIBITOR, MEMBRANE PROTEIN, ELECTRON TRANSPORT,
KEYWDS   2 OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    L.ESSER,B.QUINN,Y.F.LI,M.ZHANG,M.ELBERRY,L.YU,C.A.YU,D.XIA
REVDAT   3   13-JUL-11 1SQV    1       VERSN
REVDAT   2   24-FEB-09 1SQV    1       VERSN
REVDAT   1   06-SEP-05 1SQV    0
JRNL        AUTH   L.ESSER,B.QUINN,Y.F.LI,M.ZHANG,M.ELBERRY,L.YU,C.A.YU,D.XIA
JRNL        TITL   CRYSTALLOGRAPHIC STUDIES OF QUINOL OXIDATION SITE
JRNL        TITL 2 INHIBITORS: A MODIFIED CLASSIFICATION OF INHIBITORS FOR THE
JRNL        TITL 3 CYTOCHROME BC(1) COMPLEX.
JRNL        REF    J.MOL.BIOL.                   V. 341   281 2004
JRNL        REFN                   ISSN 0022-2836
JRNL        PMID   15312779
JRNL        DOI    10.1016/J.JMB.2004.05.065
REMARK   1
REMARK   1 REFERENCE 1
REMARK   1  AUTH   D.XIA,C.A.YU,H.KIM,J.Z.XIA,A.M.KACHURIN,L.ZHANG,L.YU,
REMARK   1  AUTH 2 J.DEISENHOFER
REMARK   1  TITL   CRYSTAL STRUCTURE OF THE CYTOCHROME BC1 COMPLEX FROM BOVINE
REMARK   1  TITL 2 HEART MITOCHONDRIA
REMARK   1  REF    SCIENCE                       V. 277    60 1997
REMARK   1  REFN                   ISSN 0036-8075
REMARK   1  PMID   9204897
REMARK   1  DOI    10.1126/SCIENCE.277.5322.60
REMARK   1 REFERENCE 2
REMARK   1  AUTH   X.GAO,X.WEN,C.YU,L.ESSER,S.TSAO,B.QUINN,L.ZHANG,L.YU,D.XIA
REMARK   1  TITL   THE CRYSTAL STRUCTURE OF MITOCHONDRIAL CYTOCHROME BC1 IN
REMARK   1  TITL 2 COMPLEX WITH FAMOXADONE: THE ROLE OF AROMATIC-AROMATIC
REMARK   1  TITL 3 INTERACTION IN INHIBITION
REMARK   1  REF    BIOCHEMISTRY                  V.  41 11692 2002
REMARK   1  REFN                   ISSN 0006-2960
REMARK   1  PMID   12269811
REMARK   1  DOI    10.1021/BI026252P
REMARK   2
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.1.24
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : ENGH & HUBER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   COMPLETENESS FOR RANGE        (%) : 85.5
REMARK   3   NUMBER OF REFLECTIONS             : 68441
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) : 0.219
REMARK   3   R VALUE            (WORKING SET) : 0.217
REMARK   3   FREE R VALUE                     : 0.285
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000
REMARK   3   FREE R VALUE TEST SET COUNT      : 2124
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) : 2.85
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.92
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 973
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3450
REMARK   3   BIN FREE R VALUE SET COUNT          : 30
REMARK   3   BIN FREE R VALUE                    : 0.4120
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 16483
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 179
REMARK   3   SOLVENT ATOMS            : 291
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.74
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 2.22000
REMARK   3    B22 (A**2) : 2.22000
REMARK   3    B33 (A**2) : -4.43000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.435
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.377
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.576
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.918
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.873
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 17473 ; 0.010 ; 0.021
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 23681 ; 1.870 ; 1.985
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2089 ;12.404 ;10.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2579 ; 0.191 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 13018 ; 0.020 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  8913 ; 0.185 ; 0.200
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):   752 ; 0.144 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.011 ; 0.200
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):   106 ; 0.163 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.170 ; 0.200
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): 10466 ; 0.512 ; 0.400
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 16841 ; 2.447 ; 3.801
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7004 ; 5.120 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6832 ; 7.545 ; 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  : 22
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     1        A   231
REMARK   3    ORIGIN FOR THE GROUP (A):  31.6523  87.0146  92.6812
REMARK   3    T TENSOR
REMARK   3      T11:   0.4384 T22:   0.5735
REMARK   3      T33:   0.7267 T12:  -0.0682
REMARK   3      T13:   0.0308 T23:   0.0016
REMARK   3    L TENSOR
REMARK   3      L11:   0.9617 L22:   1.3571
REMARK   3      L33:   2.0247 L12:   0.1033
REMARK   3      L13:   0.5363 L23:  -0.8539
REMARK   3    S TENSOR
REMARK   3      S11:   0.0645 S12:  -0.0273 S13:   0.0618
REMARK   3      S21:  -0.1048 S22:   0.0639 S23:   0.7553
REMARK   3      S31:  -0.0019 S32:  -0.7274 S33:  -0.1284
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   232        A   446
REMARK   3    ORIGIN FOR THE GROUP (A):  48.6192  93.1821 114.6354
REMARK   3    T TENSOR
REMARK   3      T11:   0.4310 T22:   0.2894
REMARK   3      T33:   0.4440 T12:  -0.1076
REMARK   3      T13:   0.1297 T23:  -0.0009
REMARK   3    L TENSOR
REMARK   3      L11:   0.0979 L22:   1.5950
REMARK   3      L33:   0.9050 L12:  -0.3140
REMARK   3      L13:   0.1305 L23:   0.1259
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0338 S12:  -0.0979 S13:   0.1153
REMARK   3      S21:   0.2448 S22:   0.0010 S23:   0.2777
REMARK   3      S31:  -0.1174 S32:  -0.3809 S33:   0.0328
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 :   B    17        B   235
REMARK   3    ORIGIN FOR THE GROUP (A):  68.6117 104.2109  91.7620
REMARK   3    T TENSOR
REMARK   3      T11:   0.2729 T22:   0.0364
REMARK   3      T33:   0.2542 T12:  -0.0934
REMARK   3      T13:   0.0151 T23:   0.0108
REMARK   3    L TENSOR
REMARK   3      L11:   1.0945 L22:   1.8843
REMARK   3      L33:   2.3134 L12:  -0.3345
REMARK   3      L13:  -0.0147 L23:   0.2534
REMARK   3    S TENSOR
REMARK   3      S11:   0.0519 S12:   0.0460 S13:   0.2165
REMARK   3      S21:  -0.0379 S22:  -0.0053 S23:   0.1481
REMARK   3      S31:  -0.3489 S32:  -0.1268 S33:  -0.0465
REMARK   3
REMARK   3   TLS GROUP : 4
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   B   236        B   439
REMARK   3    ORIGIN FOR THE GROUP (A):  56.9134  86.2218  73.1542
REMARK   3    T TENSOR
REMARK   3      T11:   0.2716 T22:   0.1559
REMARK   3      T33:   0.3101 T12:  -0.0875
REMARK   3      T13:  -0.0520 T23:  -0.0096
REMARK   3    L TENSOR
REMARK   3      L11:   1.1329 L22:   3.1785
REMARK   3      L33:   1.6066 L12:  -0.7567
REMARK   3      L13:   0.0424 L23:  -0.0888
REMARK   3    S TENSOR
REMARK   3      S11:   0.0158 S12:   0.0169 S13:  -0.1175
REMARK   3      S21:  -0.1848 S22:   0.0394 S23:   0.4353
REMARK   3      S31:   0.0693 S32:  -0.2717 S33:  -0.0552
REMARK   3
REMARK   3   TLS GROUP : 5
REMARK   3    NUMBER OF COMPONENTS GROUP : 3
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C     3        C   133
REMARK   3    RESIDUE RANGE :   C   173        C   264
REMARK   3    RESIDUE RANGE :   C   381        C   382
REMARK   3    ORIGIN FOR THE GROUP (A):  64.6313  68.4054 153.7852
REMARK   3    T TENSOR
REMARK   3      T11:   0.8294 T22:   0.4125
REMARK   3      T33:   0.4335 T12:  -0.2549
REMARK   3      T13:   0.0729 T23:   0.0400
REMARK   3    L TENSOR
REMARK   3      L11:   1.0942 L22:   0.3333
REMARK   3      L33:   0.8100 L12:  -0.0201
REMARK   3      L13:   0.2932 L23:   0.6438
REMARK   3    S TENSOR
REMARK   3      S11:   0.0379 S12:  -0.3208 S13:   0.0302
REMARK   3      S21:   0.3628 S22:  -0.0129 S23:  -0.0193
REMARK   3      S31:  -0.0025 S32:  -0.0591 S33:  -0.0250
REMARK   3
REMARK   3   TLS GROUP : 6
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   134        C   172
REMARK   3    ORIGIN FOR THE GROUP (A):  81.3168  56.8636 171.5416
REMARK   3    T TENSOR
REMARK   3      T11:   1.1787 T22:   0.6975
REMARK   3      T33:   0.5277 T12:  -0.2007
REMARK   3      T13:  -0.0651 T23:   0.2057
REMARK   3    L TENSOR
REMARK   3      L11:   2.1086 L22:   2.9333
REMARK   3      L33:   2.5608 L12:   0.9977
REMARK   3      L13:  -1.4226 L23:   2.0332
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1856 S12:  -0.2069 S13:   0.2378
REMARK   3      S21:   0.9306 S22:   0.3471 S23:  -0.5292
REMARK   3      S31:   0.1582 S32:   0.3169 S33:  -0.1615
REMARK   3
REMARK   3   TLS GROUP : 7
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   C   265        C   379
REMARK   3    ORIGIN FOR THE GROUP (A):  64.6448  44.7772 152.7457
REMARK   3    T TENSOR
REMARK   3      T11:   0.8006 T22:   0.3907
REMARK   3      T33:   0.5149 T12:  -0.2700
REMARK   3      T13:   0.0635 T23:   0.0979
REMARK   3    L TENSOR
REMARK   3      L11:   1.1947 L22:   1.1577
REMARK   3      L33:   4.1045 L12:  -0.0579
REMARK   3      L13:   1.0775 L23:  -0.5222
REMARK   3    S TENSOR
REMARK   3      S11:   0.0506 S12:  -0.3474 S13:  -0.1325
REMARK   3      S21:   0.4074 S22:  -0.0621 S23:  -0.0765
REMARK   3      S31:   0.2215 S32:   0.2212 S33:   0.0115
REMARK   3
REMARK   3   TLS GROUP : 8
REMARK   3    NUMBER OF COMPONENTS GROUP : 0
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0000   0.0000   0.0000
REMARK   3    T TENSOR
REMARK   3      T11:   0.5761 T22:   0.5761
REMARK   3      T33:   0.5761 T12:   0.0000
REMARK   3      T13:   0.0000 T23:   0.0000
REMARK   3    L TENSOR
REMARK   3      L11:   0.0000 L22:   0.0000
REMARK   3      L33:   0.0000 L12:   0.0000
REMARK   3      L13:   0.0000 L23:   0.0000
REMARK   3    S TENSOR
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000
REMARK   3      S31:   0.0000 S32:   0.0000 S33:   0.0000
REMARK   3
REMARK   3   TLS GROUP : 9
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   D   173        D   241
REMARK   3    ORIGIN FOR THE GROUP (A):  45.0705  70.9570 158.6773
REMARK   3    T TENSOR
REMARK   3      T11:   0.8842 T22:   0.5290
REMARK   3      T33:   0.5429 T12:  -0.2441
REMARK   3      T13:   0.2194 T23:   0.0349
REMARK   3    L TENSOR
REMARK   3      L11:   0.9065 L22:  -0.0133
REMARK   3      L33:   7.6573 L12:  -0.0660
REMARK   3      L13:  -1.3157 L23:  -0.5442
REMARK   3    S TENSOR
REMARK   3      S11:   0.0534 S12:  -0.4007 S13:   0.0534
REMARK   3      S21:   0.3696 S22:   0.0280 S23:   0.1297
REMARK   3      S31:   0.3711 S32:  -0.7086 S33:  -0.0814
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 :   D     1        D   172
REMARK   3    RESIDUE RANGE :   D   242        D   242
REMARK   3    ORIGIN FOR THE GROUP (A):  54.3206  66.9101 192.0144
REMARK   3    T TENSOR
REMARK   3      T11:   1.4741 T22:   1.2523
REMARK   3      T33:   0.6901 T12:  -0.2208
REMARK   3      T13:   0.2372 T23:   0.0988
REMARK   3    L TENSOR
REMARK   3      L11:   1.2915 L22:   2.6320
REMARK   3      L33:   1.1686 L12:   0.5460
REMARK   3      L13:   0.6321 L23:   1.0015
REMARK   3    S TENSOR
REMARK   3      S11:   0.0246 S12:  -0.5346 S13:  -0.1615
REMARK   3      S21:   0.5716 S22:   0.1549 S23:  -0.0404
REMARK   3      S31:   0.0138 S32:  -0.0212 S33:  -0.1795
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 :   E     1        E    71
REMARK   3    ORIGIN FOR THE GROUP (A):  43.0206  81.8827 141.4039
REMARK   3    T TENSOR
REMARK   3      T11:   0.6724 T22:   0.5099
REMARK   3      T33:   0.6507 T12:  -0.2014
REMARK   3      T13:   0.2588 T23:   0.0493
REMARK   3    L TENSOR
REMARK   3      L11:   1.5174 L22:   1.1075
REMARK   3      L33:   3.8782 L12:   0.3911
REMARK   3      L13:   1.2343 L23:   1.2834
REMARK   3    S TENSOR
REMARK   3      S11:   0.0919 S12:  -0.4524 S13:  -0.0389
REMARK   3      S21:   0.3169 S22:  -0.1623 S23:   0.1721
REMARK   3      S31:  -0.2116 S32:  -0.8222 S33:   0.0704
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 :   E    72        E   197
REMARK   3    ORIGIN FOR THE GROUP (A):  73.6699 112.4094 187.7514
REMARK   3    T TENSOR
REMARK   3      T11:   1.6894 T22:   1.2326
REMARK   3      T33:   0.8904 T12:  -0.3044
REMARK   3      T13:   0.0805 T23:  -0.3411
REMARK   3    L TENSOR
REMARK   3      L11:   4.0512 L22:   1.3487
REMARK   3      L33:   5.6210 L12:  -1.4241
REMARK   3      L13:  -1.4639 L23:   0.3390
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0233 S12:  -1.1607 S13:   0.3983
REMARK   3      S21:   0.7874 S22:   0.0175 S23:   0.0637
REMARK   3      S31:  -0.1579 S32:  -0.3689 S33:   0.0059
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 :   F     6        F   110
REMARK   3    ORIGIN FOR THE GROUP (A):  58.7487  46.8256 121.9518
REMARK   3    T TENSOR
REMARK   3      T11:   0.6363 T22:   0.2804
REMARK   3      T33:   0.3684 T12:  -0.2708
REMARK   3      T13:   0.0597 T23:   0.0117
REMARK   3    L TENSOR
REMARK   3      L11:   3.3611 L22:   1.7826
REMARK   3      L33:   1.7138 L12:  -1.3454
REMARK   3      L13:  -1.4021 L23:  -0.0991
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0760 S12:  -0.2382 S13:  -0.4505
REMARK   3      S21:   0.3012 S22:   0.0247 S23:   0.3042
REMARK   3      S31:   0.4789 S32:  -0.2912 S33:   0.0513
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 :   G     1        G    75
REMARK   3    ORIGIN FOR THE GROUP (A):  47.8646  54.3432 144.2213
REMARK   3    T TENSOR
REMARK   3      T11:   0.7554 T22:   0.5595
REMARK   3      T33:   0.5575 T12:  -0.2646
REMARK   3      T13:   0.1397 T23:   0.0344
REMARK   3    L TENSOR
REMARK   3      L11:   0.2831 L22:   1.3510
REMARK   3      L33:   3.6325 L12:   0.1417
REMARK   3      L13:  -0.2138 L23:  -1.7765
REMARK   3    S TENSOR
REMARK   3      S11:   0.0458 S12:  -0.4582 S13:  -0.1165
REMARK   3      S21:   0.3419 S22:   0.0137 S23:   0.1586
REMARK   3      S31:   0.2117 S32:  -0.2779 S33:  -0.0596
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 :   H    12        H    52
REMARK   3    ORIGIN FOR THE GROUP (A):  39.3441  40.2349 193.3021
REMARK   3    T TENSOR
REMARK   3      T11:   0.9237 T22:   1.0366
REMARK   3      T33:   0.9524 T12:  -0.3705
REMARK   3      T13:   0.0378 T23:   0.1365
REMARK   3    L TENSOR
REMARK   3      L11:   5.6836 L22:   7.4753
REMARK   3      L33:  12.4047 L12:  -3.5537
REMARK   3      L13:  -3.4751 L23:   0.0025
REMARK   3    S TENSOR
REMARK   3      S11:   0.3136 S12:  -0.1573 S13:  -0.5178
REMARK   3      S21:  -0.8672 S22:  -0.2529 S23:   0.1411
REMARK   3      S31:   0.3954 S32:  -0.3455 S33:  -0.0607
REMARK   3
REMARK   3   TLS GROUP : 16
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   H    53        H    78
REMARK   3    ORIGIN FOR THE GROUP (A):  39.6601  49.3723 186.6306
REMARK   3    T TENSOR
REMARK   3      T11:   0.9075 T22:   1.0089
REMARK   3      T33:   0.7600 T12:  -0.4030
REMARK   3      T13:   0.0057 T23:   0.0202
REMARK   3    L TENSOR
REMARK   3      L11:  10.7765 L22:  35.6893
REMARK   3      L33:   6.8147 L12: -15.2241
REMARK   3      L13:  -7.8263 L23:   0.7140
REMARK   3    S TENSOR
REMARK   3      S11:   0.1664 S12:   0.4350 S13:   0.1838
REMARK   3      S21:   0.1242 S22:  -0.7638 S23:  -0.2671
REMARK   3      S31:   0.3498 S32:  -0.6846 S33:   0.5974
REMARK   3
REMARK   3   TLS GROUP : 17
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   H    49        H    78
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0000   0.0000   0.0000
REMARK   3    T TENSOR
REMARK   3      T11:   0.5761 T22:   0.5761
REMARK   3      T33:   0.5761 T12:   0.0000
REMARK   3      T13:   0.0000 T23:   0.0000
REMARK   3    L TENSOR
REMARK   3      L11:   0.0000 L22:   0.0000
REMARK   3      L33:   0.0000 L12:   0.0000
REMARK   3      L13:   0.0000 L23:   0.0000
REMARK   3    S TENSOR
REMARK   3      S11:   0.0000 S12:   0.0000 S13:   0.0000
REMARK   3      S21:   0.0000 S22:   0.0000 S23:   0.0000
REMARK   3      S31:   0.0000 S32:   0.0000 S33:   0.0000
REMARK   3
REMARK   3   TLS GROUP : 18
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   I     2        I    26
REMARK   3    ORIGIN FOR THE GROUP (A):  60.3233  94.5408  88.4712
REMARK   3    T TENSOR
REMARK   3      T11:   0.6077 T22:   0.5936
REMARK   3      T33:   0.6349 T12:  -0.1012
REMARK   3      T13:   0.1389 T23:  -0.0573
REMARK   3    L TENSOR
REMARK   3      L11:   0.8502 L22:  11.7642
REMARK   3      L33: -13.3594 L12:  -0.3860
REMARK   3      L13:   3.8189 L23:   2.4944
REMARK   3    S TENSOR
REMARK   3      S11:  -0.1306 S12:   0.2219 S13:   0.1007
REMARK   3      S21:  -0.3404 S22:  -0.4691 S23:   0.2438
REMARK   3      S31:   0.7344 S32:  -1.4715 S33:   0.5997
REMARK   3
REMARK   3   TLS GROUP : 19
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   I    27        I    51
REMARK   3    ORIGIN FOR THE GROUP (A):  54.4746  80.6013  93.6741
REMARK   3    T TENSOR
REMARK   3      T11:   0.6455 T22:   0.7813
REMARK   3      T33:   0.8096 T12:  -0.0376
REMARK   3      T13:   0.1101 T23:  -0.0433
REMARK   3    L TENSOR
REMARK   3      L11:   9.2931 L22:  12.2507
REMARK   3      L33:  21.6711 L12:   4.5871
REMARK   3      L13:   5.7204 L23:   4.8799
REMARK   3    S TENSOR
REMARK   3      S11:   0.5921 S12:  -0.6230 S13:   0.0576
REMARK   3      S21:   0.1378 S22:  -0.1364 S23:   0.7821
REMARK   3      S31:   0.7617 S32:  -0.9942 S33:  -0.4557
REMARK   3
REMARK   3   TLS GROUP : 20
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   I    52        I    57
REMARK   3    ORIGIN FOR THE GROUP (A):  46.8601  97.8409 104.1184
REMARK   3    T TENSOR
REMARK   3      T11:   0.5770 T22:   0.5790
REMARK   3      T33:   0.5790 T12:  -0.0025
REMARK   3      T13:   0.0002 T23:  -0.0038
REMARK   3    L TENSOR
REMARK   3      L11: 159.4970 L22:  58.6451
REMARK   3      L33:  59.0070 L12:  40.9357
REMARK   3      L13:  -0.1502 L23:  19.1401
REMARK   3    S TENSOR
REMARK   3      S11:  -0.7787 S12:   4.7042 S13:  -0.4789
REMARK   3      S21:  -0.3142 S22:   1.1071 S23:  -0.5736
REMARK   3      S31:  -0.8090 S32:  -1.2483 S33:  -0.3284
REMARK   3
REMARK   3   TLS GROUP : 21
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   J     2        J    61
REMARK   3    ORIGIN FOR THE GROUP (A):  38.4152  88.2708 160.3650
REMARK   3    T TENSOR
REMARK   3      T11:   0.9234 T22:   0.9938
REMARK   3      T33:   0.7134 T12:  -0.1317
REMARK   3      T13:   0.2868 T23:  -0.0815
REMARK   3    L TENSOR
REMARK   3      L11:   1.4755 L22:   2.7992
REMARK   3      L33:   0.7435 L12:   0.4130
REMARK   3      L13:  -1.0584 L23:   0.2740
REMARK   3    S TENSOR
REMARK   3      S11:  -0.0644 S12:  -0.3202 S13:  -0.0677
REMARK   3      S21:   0.6579 S22:   0.1752 S23:   0.3293
REMARK   3      S31:  -0.2612 S32:  -1.2502 S33:  -0.1108
REMARK   3
REMARK   3   TLS GROUP : 22
REMARK   3    NUMBER OF COMPONENTS GROUP : 1
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI
REMARK   3    RESIDUE RANGE :   K     1        K    51
REMARK   3    ORIGIN FOR THE GROUP (A):  52.6112 104.3757 146.0771
REMARK   3    T TENSOR
REMARK   3      T11:   0.8210 T22:   0.5893
REMARK   3      T33:   0.6965 T12:  -0.0470
REMARK   3      T13:   0.0805 T23:  -0.1989
REMARK   3    L TENSOR
REMARK   3      L11:   2.2600 L22:   4.9854
REMARK   3      L33:  16.3470 L12:   2.2148
REMARK   3      L13:  -4.4810 L23:  -5.9000
REMARK   3    S TENSOR
REMARK   3      S11:   0.2224 S12:  -0.3816 S13:   0.0537
REMARK   3      S21:   0.5226 S22:   0.0779 S23:   0.1852
REMARK   3      S31:  -0.5953 S32:  -0.3863 S33:  -0.3003
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: NULL
REMARK   4
REMARK   4 1SQV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-04.
REMARK 100 THE RCSB ID CODE IS RCSB021932.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 08-JAN-02
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               : APS
REMARK 200  BEAMLINE                       : 17-ID
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2
REMARK 200  MONOCHROMATOR                  : SAGITTALLY FOCUSED SI(111)
REMARK 200  OPTICS                         : MIRRORS
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 68441
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 65.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20MM AMMONIUM ACETATE, 20% GLYCEROL,
REMARK 280  12% PEG4000, 0.5M KCL, 0.1% DIHEPTANOYL-PHOSPHATIDYLCHOLINE, PH
REMARK 280  7.2, VAPOR DIFFUSION, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       3555   -Y,X+1/2,Z+1/4
REMARK 290       4555   Y+1/2,-X,Z+3/4
REMARK 290       5555   -X+1/2,Y,-Z+3/4
REMARK 290       6555   X,-Y+1/2,-Z+1/4
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2
REMARK 290       8555   -Y,-X,-Z
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2
REMARK 290      10555   -X,-Y,Z
REMARK 290      11555   -Y+1/2,X,Z+3/4
REMARK 290      12555   Y,-X+1/2,Z+1/4
REMARK 290      13555   -X,Y+1/2,-Z+1/4
REMARK 290      14555   X+1/2,-Y,-Z+3/4
REMARK 290      15555   Y,X,-Z
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2
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       76.83600
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       76.83600
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      294.60950
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       76.83600
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      147.30475
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       76.83600
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      441.91425
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       76.83600
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      441.91425
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       76.83600
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      147.30475
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       76.83600
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       76.83600
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      294.60950
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       76.83600
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       76.83600
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      294.60950
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       76.83600
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      441.91425
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       76.83600
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000      147.30475
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       76.83600
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000      147.30475
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       76.83600
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      441.91425
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       76.83600
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       76.83600
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      294.60950
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: 22-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 22-MERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 101840 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 162040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -690.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350                    AND CHAINS: J, K
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   BIOMT1   2 -1.000000  0.000000  0.000000      153.67200
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      153.67200
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
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 B     1
REMARK 465     LEU B     2
REMARK 465     LYS B     3
REMARK 465     VAL B     4
REMARK 465     ALA B     5
REMARK 465     PRO B     6
REMARK 465     LYS B     7
REMARK 465     VAL B     8
REMARK 465     LYS B     9
REMARK 465     ALA B    10
REMARK 465     THR B    11
REMARK 465     GLU B    12
REMARK 465     ALA B    13
REMARK 465     PRO B    14
REMARK 465     ALA B    15
REMARK 465     GLY B    16
REMARK 465     MET C     1
REMARK 465     ALA F     1
REMARK 465     GLY F     2
REMARK 465     ARG F     3
REMARK 465     PRO F     4
REMARK 465     ALA F     5
REMARK 465     ALA G    76
REMARK 465     TYR G    77
REMARK 465     GLU G    78
REMARK 465     ASN G    79
REMARK 465     ASP G    80
REMARK 465     ARG G    81
REMARK 465     GLY H     1
REMARK 465     ASP H     2
REMARK 465     PRO H     3
REMARK 465     LYS H     4
REMARK 465     GLU H     5
REMARK 465     GLU H     6
REMARK 465     GLU H     7
REMARK 465     GLU H     8
REMARK 465     GLU H     9
REMARK 465     GLU H    10
REMARK 465     GLU H    11
REMARK 465     GLN I    58
REMARK 465     ALA I    59
REMARK 465     ALA I    60
REMARK 465     GLY I    61
REMARK 465     ARG I    62
REMARK 465     PRO I    63
REMARK 465     LEU I    64
REMARK 465     VAL I    65
REMARK 465     ALA I    66
REMARK 465     SER I    67
REMARK 465     VAL I    68
REMARK 465     SER I    69
REMARK 465     LEU I    70
REMARK 465     ASN I    71
REMARK 465     VAL I    72
REMARK 465     PRO I    73
REMARK 465     ALA I    74
REMARK 465     SER I    75
REMARK 465     VAL I    76
REMARK 465     ARG I    77
REMARK 465     TYR I    78
REMARK 465     LYS J    62
REMARK 465     PHE K    52
REMARK 465     LYS K    53
REMARK 465     LYS K    54
REMARK 465     ASP K    55
REMARK 465     ASP K    56
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   NH2  ARG A   244     O    HOH A   514              2.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    ASP A 105   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES
REMARK 500    LEU A 203   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES
REMARK 500    ASP B 180   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES
REMARK 500    LEU I  45   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES
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    ASN A  21      -53.24   -174.37
REMARK 500    THR A  34      144.98   -176.41
REMARK 500    ASP A  42       30.13    -78.48
REMARK 500    SER A  45      -20.16   -140.46
REMARK 500    ARG A  92       -4.98    -59.42
REMARK 500    GLU A  93      -19.07   -144.33
REMARK 500    PRO A 107      -75.16    -40.33
REMARK 500    GLN A 118      -63.71   -109.17
REMARK 500    ASN A 119       40.83    -88.49
REMARK 500    SER A 125      -57.98    -16.35
REMARK 500    GLN A 159       93.67     11.63
REMARK 500    LEU A 219      -68.04    -94.47
REMARK 500    SER A 220       34.82    -94.23
REMARK 500    TYR A 223     -129.78   -157.20
REMARK 500    ASP A 224      -56.23     56.40
REMARK 500    THR A 237      -76.87    -85.39
REMARK 500    SER A 239      169.48    161.38
REMARK 500    CYS A 304     -172.53   -174.07
REMARK 500    ASP A 327      145.54    -37.55
REMARK 500    SER A 348       38.17   -147.81
REMARK 500    HIS B  20      114.36    -35.73
REMARK 500    TYR B  41       38.90    -85.28
REMARK 500    LYS B  52       71.51    -56.65
REMARK 500    ALA B  53       27.21   -143.09
REMARK 500    ASN B  62       30.59   -147.88
REMARK 500    PRO B 155      -34.71    -36.93
REMARK 500    ASN B 170      139.77    175.01
REMARK 500    ALA B 171      -87.52     65.77
REMARK 500    PHE B 199       48.99    -93.68
REMARK 500    LEU B 232      123.43     -3.37
REMARK 500    LYS B 236      116.72     66.72
REMARK 500    HIS B 240      -42.27   -145.10
REMARK 500    SER B 251      -35.30     69.14
REMARK 500    SER B 261     -109.76    -94.56
REMARK 500    SER B 266      150.26    -39.65
REMARK 500    ALA B 281     -133.59    -96.26
REMARK 500    ALA B 291      -34.58    -37.41
REMARK 500    ASP B 318       19.46   -143.37
REMARK 500    ASP B 407      -38.82    -36.01
REMARK 500    PRO B 434     -168.63    -67.03
REMARK 500    ILE B 436      -81.46     80.92
REMARK 500    ASP B 437      -55.62     -1.95
REMARK 500    ILE C   4      -37.85    -36.71
REMARK 500    SER C   7      -31.58   -130.85
REMARK 500    LYS C  12      -65.75    -22.70
REMARK 500    SER C  25        5.94    -65.67
REMARK 500    ASN C  26      -41.51   -149.74
REMARK 500    HIS C  54      -30.15   -132.94
REMARK 500    TYR C 155      -27.44     75.30
REMARK 500    ASP C 171     -153.84   -147.59
REMARK 500
REMARK 500 THIS ENTRY HAS     140 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 ASP A   20     ASN A   21                 -146.85
REMARK 500 SER A   45     ARG A   46                  146.32
REMARK 500 ASN A   52     ASN A   53                 -149.47
REMARK 500 ASP A  124     SER A  125                  149.97
REMARK 500 PHE A  158     GLN A  159                  145.36
REMARK 500 GLY A  238     SER A  239                 -126.52
REMARK 500 ARG A  388     ARG A  389                  140.26
REMARK 500 PRO B   19     HIS B   20                  143.98
REMARK 500 GLU B   39     ASN B   40                  139.13
REMARK 500 GLY B   79     ALA B   80                  129.67
REMARK 500 ARG B  169     ASN B  170                 -135.27
REMARK 500 GLY B  228     GLY B  229                  142.32
REMARK 500 GLY B  231     LEU B  232                  146.54
REMARK 500 SER B  233     GLY B  234                 -135.84
REMARK 500 GLY B  234     ALA B  235                  124.80
REMARK 500 ASN B  248     GLY B  249                 -135.31
REMARK 500 ILE B  436     ASP B  437                  143.94
REMARK 500 SER C   25     ASN C   26                 -120.76
REMARK 500 GLY C  167     PHE C  168                 -143.12
REMARK 500 GLU C  344     HIS C  345                 -142.25
REMARK 500 SER D    1     ASP D    2                  147.20
REMARK 500 GLY D   53     VAL D   54                 -140.69
REMARK 500 GLY D   73     PRO D   74                 -137.88
REMARK 500 GLY D   85     LYS D   86                 -149.18
REMARK 500 LYS D   86     LEU D   87                 -146.32
REMARK 500 TYR D   90     PHE D   91                  143.28
REMARK 500 LYS D   93     PRO D   94                 -120.91
REMARK 500 ASN D   97     PRO D   98                  148.33
REMARK 500 GLY D  107     ALA D  108                  145.79
REMARK 500 HIS D  121     GLY D  122                 -139.03
REMARK 500 PRO D  137     PRO D  138                 -149.02
REMARK 500 LEU D  143     ARG D  144                  147.02
REMARK 500 ARG D  144     GLU D  145                 -144.32
REMARK 500 GLU D  145     GLY D  146                  147.58
REMARK 500 ALA D  157     ILE D  158                  138.70
REMARK 500 ILE D  158     GLY D  159                 -140.75
REMARK 500 PRO D  162     PRO D  163                 -132.37
REMARK 500 TYR D  165     ASN D  166                  148.98
REMARK 500 VAL D  168     LEU D  169                 -145.81
REMARK 500 ASP D  172     ASP D  173                  146.43
REMARK 500 PRO D  240     LYS D  241                 -149.32
REMARK 500 SER E   63     ALA E   64                  137.97
REMARK 500 ALA E   64     SER E   65                  117.51
REMARK 500 VAL E   68     LEU E   69                  137.02
REMARK 500 ALA E   70     MET E   71                 -141.54
REMARK 500 LYS E   94     PRO E   95                 -144.17
REMARK 500 VAL F    6     SER F    7                 -145.15
REMARK 500 GLN H   26     LEU H   27                 -148.67
REMARK 500 LEU H   27     GLU H   28                 -138.75
REMARK 500 ARG H   43     VAL H   44                 -149.05
REMARK 500
REMARK 500 THIS ENTRY HAS      72 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    GLU A 137        -10.26
REMARK 500    PRO B  30        -10.98
REMARK 500    THR B 108        -10.26
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    ARG A 131        24.3      L          L   OUTSIDE RANGE
REMARK 500    ASP A 224        21.2      L          L   OUTSIDE RANGE
REMARK 500    ILE B 118        19.6      L          L   OUTSIDE RANGE
REMARK 500    VAL B 189        24.7      L          L   OUTSIDE RANGE
REMARK 500    THR B 397        24.1      L          L   OUTSIDE RANGE
REMARK 500    ILE C  42        24.1      L          L   OUTSIDE RANGE
REMARK 500    PHE C  91        24.7      L          L   OUTSIDE RANGE
REMARK 500    TYR C 131        24.5      L          L   OUTSIDE RANGE
REMARK 500    ILE C 226        23.3      L          L   OUTSIDE RANGE
REMARK 500    VAL C 243        23.8      L          L   OUTSIDE RANGE
REMARK 500    ARG C 318        24.2      L          L   OUTSIDE RANGE
REMARK 500    HIS C 345        20.7      L          L   OUTSIDE RANGE
REMARK 500    GLU D  76        23.8      L          L   OUTSIDE RANGE
REMARK 500    ALA D 108        24.9      L          L   OUTSIDE RANGE
REMARK 500    ARG D 201        24.3      L          L   OUTSIDE RANGE
REMARK 500    SER E  65        18.0      L          L   OUTSIDE RANGE
REMARK 500    ASN E 149        24.2      L          L   OUTSIDE RANGE
REMARK 500    ILE G  34        20.9      L          L   OUTSIDE RANGE
REMARK 500    PHE I  11        24.4      L          L   OUTSIDE RANGE
REMARK 500    LEU I  26        23.8      L          L   OUTSIDE RANGE
REMARK 500    VAL I  30        23.7      L          L   OUTSIDE RANGE
REMARK 500    VAL I  42        13.0      L          L   OUTSIDE RANGE
REMARK 500    LEU I  43        16.5      L          L   OUTSIDE RANGE
REMARK 500    LEU I  45        22.4      L          L   OUTSIDE RANGE
REMARK 500    VAL K  18        17.6      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH B 632        DISTANCE =  5.57 ANGSTROMS
REMARK 525    HOH D 715        DISTANCE =  5.62 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM C 382  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C  97   NE2
REMARK 620 2 HEM C 382   NA   86.8
REMARK 620 3 HEM C 382   NB   95.5  89.7
REMARK 620 4 HEM C 382   NC   88.8 175.5  90.2
REMARK 620 5 HEM C 382   ND   82.9  91.2 178.1  88.8
REMARK 620 6 HIS C 196   NE2 170.3  91.0  93.9  93.4  87.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM C 381  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C  83   NE2
REMARK 620 2 HEM C 381   NA   90.4
REMARK 620 3 HEM C 381   NB   95.1  89.2
REMARK 620 4 HEM C 381   NC   89.3 178.4  89.3
REMARK 620 5 HEM C 381   ND   86.3  91.5 178.4  90.0
REMARK 620 6 HIS C 182   NE2 176.8  88.6  88.0  91.8  90.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEM D 242  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET D 160   SD
REMARK 620 2 HEM D 242   NA   72.7
REMARK 620 3 HEM D 242   NB   86.8  90.4
REMARK 620 4 HEM D 242   NC  107.5 179.6  89.4
REMARK 620 5 HEM D 242   ND   92.7  89.8 179.4  90.5
REMARK 620 6 HIS D  41   NE2 157.3  84.9  90.0  94.8  90.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             FES E 197  FE1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 139   SG
REMARK 620 2 FES E 197   S1  103.9
REMARK 620 3 FES E 197   S2  104.6 103.9
REMARK 620 4 CYS E 158   SG  103.0 119.2 120.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             FES E 197  FE2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS E 161   ND1
REMARK 620 2 FES E 197   S1  125.3
REMARK 620 3 FES E 197   S2  105.5 103.7
REMARK 620 4 HIS E 141   ND1  94.7 108.2 121.0
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 HEM C 381
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM C 382
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM D 242
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FES E 197
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UHD C 383
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UQ2 C 384
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QCR   RELATED DB: PDB
REMARK 900 NATIVE
REMARK 900 RELATED ID: 1LOL   RELATED DB: PDB
REMARK 900 WITH FAMOXADONE
REMARK 900 RELATED ID: 1SQP   RELATED DB: PDB
REMARK 900 WITH MYXOTHIAZOL
REMARK 900 RELATED ID: 1SQQ   RELATED DB: PDB
REMARK 900 WITH MOASTILBENE
REMARK 900 RELATED ID: 1SQB   RELATED DB: PDB
REMARK 900 WITH AZOXYSTROBIN
REMARK 900 RELATED ID: 1SQX   RELATED DB: PDB
REMARK 900 WITH STIGMATELLIN A
DBREF  1SQV A    1   446  UNP    P31800   UQCR1_BOVIN     34    480
DBREF  1SQV B    1   439  UNP    P23004   UQCR2_BOVIN     15    453
DBREF  1SQV C    1   379  UNP    P00157   CYB_BOVIN        1    379
DBREF  1SQV D    1   241  UNP    P00125   CY1_BOVIN        1    241
DBREF  1SQV E    1   196  UNP    P13272   UCRI_BOVIN      79    274
DBREF  1SQV F    1   110  UNP    P00129   UCR6_BOVIN       1    110
DBREF  1SQV G    1    81  UNP    P13271   UCRQ_BOVIN       1     81
DBREF  1SQV H    1    78  UNP    P00126   UCRH_BOVIN       1     78
DBREF  1SQV I    1    78  UNP    P13272   UCRI_BOVIN       1     78
DBREF  1SQV J    1    62  UNP    P00130   UCR10_BOVIN      1     62
DBREF  1SQV K    1    56  UNP    P07552   UCR11_BOVIN      1     56
SEQRES   1 A  446  THR ALA THR TYR ALA GLN ALA LEU GLN SER VAL PRO GLU
SEQRES   2 A  446  THR GLN VAL SER GLN LEU ASP ASN GLY LEU ARG VAL ALA
SEQRES   3 A  446  SER GLU GLN SER SER GLN PRO THR CYS THR VAL GLY VAL
SEQRES   4 A  446  TRP ILE ASP ALA GLY SER ARG TYR GLU SER GLU LYS ASN
SEQRES   5 A  446  ASN GLY ALA GLY TYR PHE VAL GLU HIS LEU ALA PHE LYS
SEQRES   6 A  446  GLY THR LYS ASN ARG PRO GLY ASN ALA LEU GLU LYS GLU
SEQRES   7 A  446  VAL GLU SER MET GLY ALA HIS LEU ASN ALA TYR SER THR
SEQRES   8 A  446  ARG GLU HIS THR ALA TYR TYR ILE LYS ALA LEU SER LYS
SEQRES   9 A  446  ASP LEU PRO LYS ALA VAL GLU LEU LEU ALA ASP ILE VAL
SEQRES  10 A  446  GLN ASN CYS SER LEU GLU ASP SER GLN ILE GLU LYS GLU
SEQRES  11 A  446  ARG ASP VAL ILE LEU GLN GLU LEU GLN GLU ASN ASP THR
SEQRES  12 A  446  SER MET ARG ASP VAL VAL PHE ASN TYR LEU HIS ALA THR
SEQRES  13 A  446  ALA PHE GLN GLY THR PRO LEU ALA GLN SER VAL GLU GLY
SEQRES  14 A  446  PRO SER GLU ASN VAL ARG LYS LEU SER ARG ALA ASP LEU
SEQRES  15 A  446  THR GLU TYR LEU SER ARG HIS TYR LYS ALA PRO ARG MET
SEQRES  16 A  446  VAL LEU ALA ALA ALA GLY GLY LEU GLU HIS ARG GLN LEU
SEQRES  17 A  446  LEU ASP LEU ALA GLN LYS HIS PHE SER GLY LEU SER GLY
SEQRES  18 A  446  THR TYR ASP GLU ASP ALA VAL PRO THR LEU SER PRO CYS
SEQRES  19 A  446  ARG PHE THR GLY SER GLN ILE CYS HIS ARG GLU ASP GLY
SEQRES  20 A  446  LEU PRO LEU ALA HIS VAL ALA ILE ALA VAL GLU GLY PRO
SEQRES  21 A  446  GLY TRP ALA HIS PRO ASP ASN VAL ALA LEU GLN VAL ALA
SEQRES  22 A  446  ASN ALA ILE ILE GLY HIS TYR ASP CYS THR TYR GLY GLY
SEQRES  23 A  446  GLY ALA HIS LEU SER SER PRO LEU ALA SER ILE ALA ALA
SEQRES  24 A  446  THR ASN LYS LEU CYS GLN SER PHE GLN THR PHE ASN ILE
SEQRES  25 A  446  CYS TYR ALA ASP THR GLY LEU LEU GLY ALA HIS PHE VAL
SEQRES  26 A  446  CYS ASP HIS MET SER ILE ASP ASP MET MET PHE VAL LEU
SEQRES  27 A  446  GLN GLY GLN TRP MET ARG LEU CYS THR SER ALA THR GLU
SEQRES  28 A  446  SER GLU VAL LEU ARG GLY LYS ASN LEU LEU ARG ASN ALA
SEQRES  29 A  446  LEU VAL SER HIS LEU ASP GLY THR THR PRO VAL CYS GLU
SEQRES  30 A  446  ASP ILE GLY ARG SER LEU LEU THR TYR GLY ARG ARG ILE
SEQRES  31 A  446  PRO LEU ALA GLU TRP GLU SER ARG ILE ALA GLU VAL ASP
SEQRES  32 A  446  ALA ARG VAL VAL ARG GLU VAL CYS SER LYS TYR PHE TYR
SEQRES  33 A  446  ASP GLN CYS PRO ALA VAL ALA GLY PHE GLY PRO ILE GLU
SEQRES  34 A  446  GLN LEU PRO ASP TYR ASN ARG ILE ARG SER GLY MET PHE
SEQRES  35 A  446  TRP LEU ARG PHE
SEQRES   1 B  439  SER LEU LYS VAL ALA PRO LYS VAL LYS ALA THR GLU ALA
SEQRES   2 B  439  PRO ALA GLY VAL PRO PRO HIS PRO GLN ASP LEU GLU PHE
SEQRES   3 B  439  THR ARG LEU PRO ASN GLY LEU VAL ILE ALA SER LEU GLU
SEQRES   4 B  439  ASN TYR ALA PRO ALA SER ARG ILE GLY LEU PHE ILE LYS
SEQRES   5 B  439  ALA GLY SER ARG TYR GLU ASN SER ASN ASN LEU GLY THR
SEQRES   6 B  439  SER HIS LEU LEU ARG LEU ALA SER SER LEU THR THR LYS
SEQRES   7 B  439  GLY ALA SER SER PHE LYS ILE THR ARG GLY ILE GLU ALA
SEQRES   8 B  439  VAL GLY GLY LYS LEU SER VAL THR SER THR ARG GLU ASN
SEQRES   9 B  439  MET ALA TYR THR VAL GLU CYS LEU ARG ASP ASP VAL ASP
SEQRES  10 B  439  ILE LEU MET GLU PHE LEU LEU ASN VAL THR THR ALA PRO
SEQRES  11 B  439  GLU PHE ARG ARG TRP GLU VAL ALA ALA LEU GLN PRO GLN
SEQRES  12 B  439  LEU ARG ILE ASP LYS ALA VAL ALA LEU GLN ASN PRO GLN
SEQRES  13 B  439  ALA HIS VAL ILE GLU ASN LEU HIS ALA ALA ALA TYR ARG
SEQRES  14 B  439  ASN ALA LEU ALA ASN SER LEU TYR CYS PRO ASP TYR ARG
SEQRES  15 B  439  ILE GLY LYS VAL THR PRO VAL GLU LEU HIS ASP TYR VAL
SEQRES  16 B  439  GLN ASN HIS PHE THR SER ALA ARG MET ALA LEU ILE GLY
SEQRES  17 B  439  LEU GLY VAL SER HIS PRO VAL LEU LYS GLN VAL ALA GLU
SEQRES  18 B  439  GLN PHE LEU ASN ILE ARG GLY GLY LEU GLY LEU SER GLY
SEQRES  19 B  439  ALA LYS ALA LYS TYR HIS GLY GLY GLU ILE ARG GLU GLN
SEQRES  20 B  439  ASN GLY ASP SER LEU VAL HIS ALA ALA LEU VAL ALA GLU
SEQRES  21 B  439  SER ALA ALA ILE GLY SER ALA GLU ALA ASN ALA PHE SER
SEQRES  22 B  439  VAL LEU GLN HIS VAL LEU GLY ALA GLY PRO HIS VAL LYS
SEQRES  23 B  439  ARG GLY SER ASN ALA THR SER SER LEU TYR GLN ALA VAL
SEQRES  24 B  439  ALA LYS GLY VAL HIS GLN PRO PHE ASP VAL SER ALA PHE
SEQRES  25 B  439  ASN ALA SER TYR SER ASP SER GLY LEU PHE GLY PHE TYR
SEQRES  26 B  439  THR ILE SER GLN ALA ALA SER ALA GLY ASP VAL ILE LYS
SEQRES  27 B  439  ALA ALA TYR ASN GLN VAL LYS THR ILE ALA GLN GLY ASN
SEQRES  28 B  439  LEU SER ASN PRO ASP VAL GLN ALA ALA LYS ASN LYS LEU
SEQRES  29 B  439  LYS ALA GLY TYR LEU MET SER VAL GLU SER SER GLU GLY
SEQRES  30 B  439  PHE LEU ASP GLU VAL GLY SER GLN ALA LEU ALA ALA GLY
SEQRES  31 B  439  SER TYR THR PRO PRO SER THR VAL LEU GLN GLN ILE ASP
SEQRES  32 B  439  ALA VAL ALA ASP ALA ASP VAL ILE ASN ALA ALA LYS LYS
SEQRES  33 B  439  PHE VAL SER GLY ARG LYS SER MET ALA ALA SER GLY ASN
SEQRES  34 B  439  LEU GLY HIS THR PRO PHE ILE ASP GLU LEU
SEQRES   1 C  379  MET THR ASN ILE ARG LYS SER HIS PRO LEU MET LYS ILE
SEQRES   2 C  379  VAL ASN ASN ALA PHE ILE ASP LEU PRO ALA PRO SER ASN
SEQRES   3 C  379  ILE SER SER TRP TRP ASN PHE GLY SER LEU LEU GLY ILE
SEQRES   4 C  379  CYS LEU ILE LEU GLN ILE LEU THR GLY LEU PHE LEU ALA
SEQRES   5 C  379  MET HIS TYR THR SER ASP THR THR THR ALA PHE SER SER
SEQRES   6 C  379  VAL THR HIS ILE CYS ARG ASP VAL ASN TYR GLY TRP ILE
SEQRES   7 C  379  ILE ARG TYR MET HIS ALA ASN GLY ALA SER MET PHE PHE
SEQRES   8 C  379  ILE CYS LEU TYR MET HIS VAL GLY ARG GLY LEU TYR TYR
SEQRES   9 C  379  GLY SER TYR THR PHE LEU GLU THR TRP ASN ILE GLY VAL
SEQRES  10 C  379  ILE LEU LEU LEU THR VAL MET ALA THR ALA PHE MET GLY
SEQRES  11 C  379  TYR VAL LEU PRO TRP GLY GLN MET SER PHE TRP GLY ALA
SEQRES  12 C  379  THR VAL ILE THR ASN LEU LEU SER ALA ILE PRO TYR ILE
SEQRES  13 C  379  GLY THR ASN LEU VAL GLU TRP ILE TRP GLY GLY PHE SER
SEQRES  14 C  379  VAL ASP LYS ALA THR LEU THR ARG PHE PHE ALA PHE HIS
SEQRES  15 C  379  PHE ILE LEU PRO PHE ILE ILE MET ALA ILE ALA MET VAL
SEQRES  16 C  379  HIS LEU LEU PHE LEU HIS GLU THR GLY SER ASN ASN PRO
SEQRES  17 C  379  THR GLY ILE SER SER ASP VAL ASP LYS ILE PRO PHE HIS
SEQRES  18 C  379  PRO TYR TYR THR ILE LYS ASP ILE LEU GLY ALA LEU LEU
SEQRES  19 C  379  LEU ILE LEU ALA LEU MET LEU LEU VAL LEU PHE ALA PRO
SEQRES  20 C  379  ASP LEU LEU GLY ASP PRO ASP ASN TYR THR PRO ALA ASN
SEQRES  21 C  379  PRO LEU ASN THR PRO PRO HIS ILE LYS PRO GLU TRP TYR
SEQRES  22 C  379  PHE LEU PHE ALA TYR ALA ILE LEU ARG SER ILE PRO ASN
SEQRES  23 C  379  LYS LEU GLY GLY VAL LEU ALA LEU ALA PHE SER ILE LEU
SEQRES  24 C  379  ILE LEU ALA LEU ILE PRO LEU LEU HIS THR SER LYS GLN
SEQRES  25 C  379  ARG SER MET MET PHE ARG PRO LEU SER GLN CYS LEU PHE
SEQRES  26 C  379  TRP ALA LEU VAL ALA ASP LEU LEU THR LEU THR TRP ILE
SEQRES  27 C  379  GLY GLY GLN PRO VAL GLU HIS PRO TYR ILE THR ILE GLY
SEQRES  28 C  379  GLN LEU ALA SER VAL LEU TYR PHE LEU LEU ILE LEU VAL
SEQRES  29 C  379  LEU MET PRO THR ALA GLY THR ILE GLU ASN LYS LEU LEU
SEQRES  30 C  379  LYS TRP
SEQRES   1 D  241  SER ASP LEU GLU LEU HIS PRO PRO SER TYR PRO TRP SER
SEQRES   2 D  241  HIS ARG GLY LEU LEU SER SER LEU ASP HIS THR SER ILE
SEQRES   3 D  241  ARG ARG GLY PHE GLN VAL TYR LYS GLN VAL CYS SER SER
SEQRES   4 D  241  CYS HIS SER MET ASP TYR VAL ALA TYR ARG HIS LEU VAL
SEQRES   5 D  241  GLY VAL CYS TYR THR GLU ASP GLU ALA LYS ALA LEU ALA
SEQRES   6 D  241  GLU GLU VAL GLU VAL GLN ASP GLY PRO ASN GLU ASP GLY
SEQRES   7 D  241  GLU MET PHE MET ARG PRO GLY LYS LEU SER ASP TYR PHE
SEQRES   8 D  241  PRO LYS PRO TYR PRO ASN PRO GLU ALA ALA ARG ALA ALA
SEQRES   9 D  241  ASN ASN GLY ALA LEU PRO PRO ASP LEU SER TYR ILE VAL
SEQRES  10 D  241  ARG ALA ARG HIS GLY GLY GLU ASP TYR VAL PHE SER LEU
SEQRES  11 D  241  LEU THR GLY TYR CYS GLU PRO PRO THR GLY VAL SER LEU
SEQRES  12 D  241  ARG GLU GLY LEU TYR PHE ASN PRO TYR PHE PRO GLY GLN
SEQRES  13 D  241  ALA ILE GLY MET ALA PRO PRO ILE TYR ASN GLU VAL LEU
SEQRES  14 D  241  GLU PHE ASP ASP GLY THR PRO ALA THR MET SER GLN VAL
SEQRES  15 D  241  ALA LYS ASP VAL CYS THR PHE LEU ARG TRP ALA ALA GLU
SEQRES  16 D  241  PRO GLU HIS ASP HIS ARG LYS ARG MET GLY LEU LYS MET
SEQRES  17 D  241  LEU LEU MET MET GLY LEU LEU LEU PRO LEU VAL TYR ALA
SEQRES  18 D  241  MET LYS ARG HIS LYS TRP SER VAL LEU LYS SER ARG LYS
SEQRES  19 D  241  LEU ALA TYR ARG PRO PRO LYS
SEQRES   1 E  196  SER HIS THR ASP ILE LYS VAL PRO ASP PHE SER ASP TYR
SEQRES   2 E  196  ARG ARG PRO GLU VAL LEU ASP SER THR LYS SER SER LYS
SEQRES   3 E  196  GLU SER SER GLU ALA ARG LYS GLY PHE SER TYR LEU VAL
SEQRES   4 E  196  THR ALA THR THR THR VAL GLY VAL ALA TYR ALA ALA LYS
SEQRES   5 E  196  ASN VAL VAL SER GLN PHE VAL SER SER MET SER ALA SER
SEQRES   6 E  196  ALA ASP VAL LEU ALA MET SER LYS ILE GLU ILE LYS LEU
SEQRES   7 E  196  SER ASP ILE PRO GLU GLY LYS ASN MET ALA PHE LYS TRP
SEQRES   8 E  196  ARG GLY LYS PRO LEU PHE VAL ARG HIS ARG THR LYS LYS
SEQRES   9 E  196  GLU ILE ASP GLN GLU ALA ALA VAL GLU VAL SER GLN LEU
SEQRES  10 E  196  ARG ASP PRO GLN HIS ASP LEU GLU ARG VAL LYS LYS PRO
SEQRES  11 E  196  GLU TRP VAL ILE LEU ILE GLY VAL CYS THR HIS LEU GLY
SEQRES  12 E  196  CYS VAL PRO ILE ALA ASN ALA GLY ASP PHE GLY GLY TYR
SEQRES  13 E  196  TYR CYS PRO CYS HIS GLY SER HIS TYR ASP ALA SER GLY
SEQRES  14 E  196  ARG ILE ARG LYS GLY PRO ALA PRO LEU ASN LEU GLU VAL
SEQRES  15 E  196  PRO SER TYR GLU PHE THR SER ASP ASP MET VAL ILE VAL
SEQRES  16 E  196  GLY
SEQRES   1 F  110  ALA GLY ARG PRO ALA VAL SER ALA SER SER ARG TRP LEU
SEQRES   2 F  110  GLU GLY ILE ARG LYS TRP TYR TYR ASN ALA ALA GLY PHE
SEQRES   3 F  110  ASN LYS LEU GLY LEU MET ARG ASP ASP THR ILE HIS GLU
SEQRES   4 F  110  ASN ASP ASP VAL LYS GLU ALA ILE ARG ARG LEU PRO GLU
SEQRES   5 F  110  ASN LEU TYR ASP ASP ARG VAL PHE ARG ILE LYS ARG ALA
SEQRES   6 F  110  LEU ASP LEU SER MET ARG GLN GLN ILE LEU PRO LYS GLU
SEQRES   7 F  110  GLN TRP THR LYS TYR GLU GLU ASP LYS SER TYR LEU GLU
SEQRES   8 F  110  PRO TYR LEU LYS GLU VAL ILE ARG GLU ARG LYS GLU ARG
SEQRES   9 F  110  GLU GLU TRP ALA LYS LYS
SEQRES   1 G   81  GLY ARG GLN PHE GLY HIS LEU THR ARG VAL ARG HIS VAL
SEQRES   2 G   81  ILE THR TYR SER LEU SER PRO PHE GLU GLN ARG ALA PHE
SEQRES   3 G   81  PRO HIS TYR PHE SER LYS GLY ILE PRO ASN VAL LEU ARG
SEQRES   4 G   81  ARG THR ARG ALA CYS ILE LEU ARG VAL ALA PRO PRO PHE
SEQRES   5 G   81  VAL ALA PHE TYR LEU VAL TYR THR TRP GLY THR GLN GLU
SEQRES   6 G   81  PHE GLU LYS SER LYS ARG LYS ASN PRO ALA ALA TYR GLU
SEQRES   7 G   81  ASN ASP ARG
SEQRES   1 H   78  GLY ASP PRO LYS GLU GLU GLU GLU GLU GLU GLU GLU LEU
SEQRES   2 H   78  VAL ASP PRO LEU THR THR VAL ARG GLU GLN CYS GLU GLN
SEQRES   3 H   78  LEU GLU LYS CYS VAL LYS ALA ARG GLU ARG LEU GLU LEU
SEQRES   4 H   78  CYS ASP GLU ARG VAL SER SER ARG SER GLN THR GLU GLU
SEQRES   5 H   78  ASP CYS THR GLU GLU LEU LEU ASP PHE LEU HIS ALA ARG
SEQRES   6 H   78  ASP HIS CYS VAL ALA HIS LYS LEU PHE ASN SER LEU LYS
SEQRES   1 I   78  MET LEU SER VAL ALA ALA ARG SER GLY PRO PHE ALA PRO
SEQRES   2 I   78  VAL LEU SER ALA THR SER ARG GLY VAL ALA GLY ALA LEU
SEQRES   3 I   78  ARG PRO LEU VAL GLN ALA ALA VAL PRO ALA THR SER GLU
SEQRES   4 I   78  SER PRO VAL LEU ASP LEU LYS ARG SER VAL LEU CYS ARG
SEQRES   5 I   78  GLU SER LEU ARG GLY GLN ALA ALA GLY ARG PRO LEU VAL
SEQRES   6 I   78  ALA SER VAL SER LEU ASN VAL PRO ALA SER VAL ARG TYR
SEQRES   1 J   62  VAL ALA PRO THR LEU THR ALA ARG LEU TYR SER LEU LEU
SEQRES   2 J   62  PHE ARG ARG THR SER THR PHE ALA LEU THR ILE VAL VAL
SEQRES   3 J   62  GLY ALA LEU PHE PHE GLU ARG ALA PHE ASP GLN GLY ALA
SEQRES   4 J   62  ASP ALA ILE TYR GLU HIS ILE ASN GLU GLY LYS LEU TRP
SEQRES   5 J   62  LYS HIS ILE LYS HIS LYS TYR GLU ASN LYS
SEQRES   1 K   56  MET LEU THR ARG PHE LEU GLY PRO ARG TYR ARG GLN LEU
SEQRES   2 K   56  ALA ARG ASN TRP VAL PRO THR ALA SER LEU TRP GLY ALA
SEQRES   3 K   56  VAL GLY ALA VAL GLY LEU VAL TRP ALA THR ASP TRP ARG
SEQRES   4 K   56  LEU ILE LEU ASP TRP VAL PRO TYR ILE ASN GLY LYS PHE
SEQRES   5 K   56  LYS LYS ASP ASP
HET    HEM  C 381      43
HET    HEM  C 382      43
HET    HEM  D 242      43
HET    FES  E 197       4
HET    UHD  C 383      23
HET    UQ2  C 384      23
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER
HETNAM     UHD 6-HYDROXY-5-UNDECYL-1,3-BENZOTHIAZOLE-4,7-DIONE
HETNAM     UQ2 UBIQUINONE-2
HETSYN     HEM HEME
HETSYN     UHD 3-UNDECYL-2-HYDROXYDIOXOBENZOTHIAZOL; UHDBT
FORMUL  12  HEM    3(C34 H32 FE N4 O4)
FORMUL  15  FES    FE2 S2
FORMUL  16  UHD    C18 H25 N O3 S
FORMUL  17  UQ2    C19 H26 O4
FORMUL  18  HOH   *291(H2 O)
HELIX    1   1 THR A    3  SER A   10  1                                   8
HELIX    2   2 GLY A   54  PHE A   64  1                                  11
HELIX    3   3 ASN A   73  MET A   82  1                                  10
HELIX    4   4 ASP A  105  GLN A  118  1                                  14
HELIX    5   5 GLU A  123  ASP A  142  1                                  20
HELIX    6   6 SER A  144  PHE A  158  1                                  15
HELIX    7   7 THR A  161  GLN A  165  5                                   5
HELIX    8   8 PRO A  170  LEU A  177  1                                   8
HELIX    9   9 SER A  178  TYR A  190  1                                  13
HELIX   10  10 LYS A  191  PRO A  193  5                                   3
HELIX   11  11 GLU A  204  PHE A  216  1                                  13
HELIX   12  12 PRO A  265  GLY A  278  1                                  14
HELIX   13  13 SER A  292  ASN A  301  1                                  10
HELIX   14  14 SER A  330  ALA A  349  1                                  20
HELIX   15  15 THR A  350  LEU A  369  1                                  20
HELIX   16  16 GLY A  371  TYR A  386  1                                  16
HELIX   17  17 PRO A  391  VAL A  402  1                                  12
HELIX   18  18 ASP A  403  TYR A  416  1                                  14
HELIX   19  19 ASP A  433  GLY A  440  1                                   8
HELIX   20  20 GLY B   54  GLU B   58  5                                   5
HELIX   21  21 GLY B   64  ALA B   72  1                                   9
HELIX   22  22 SER B   81  ALA B   91  1                                  11
HELIX   23  23 ASP B  115  ALA B  129  1                                  15
HELIX   24  24 ARG B  133  LEU B  152  1                                  20
HELIX   25  25 ASN B  154  TYR B  168  1                                  15
HELIX   26  26 ASN B  170  ASN B  174  5                                   5
HELIX   27  27 PRO B  179  ILE B  183  5                                   5
HELIX   28  28 THR B  187  PHE B  199  1                                  13
HELIX   29  29 THR B  200  ALA B  202  5                                   3
HELIX   30  30 SER B  212  LEU B  224  1                                  13
HELIX   31  31 ALA B  267  GLY B  280  1                                  14
HELIX   32  32 SER B  293  VAL B  303  1                                  11
HELIX   33  33 SER B  332  GLN B  349  1                                  18
HELIX   34  34 SER B  353  VAL B  372  1                                  20
HELIX   35  35 SER B  374  GLY B  390  1                                  17
HELIX   36  36 PRO B  394  ALA B  404  1                                  11
HELIX   37  37 ALA B  406  GLY B  420  1                                  15
HELIX   38  38 ASN B  429  THR B  433  5                                   5
HELIX   39  39 ASN C    3  HIS C    8  1                                   6
HELIX   40  40 HIS C    8  ILE C   19  1                                  12
HELIX   41  41 SER C   28  TRP C   31  5                                   4
HELIX   42  42 ASN C   32  MET C   53  1                                  22
HELIX   43  43 ASP C   58  ASP C   72  1                                  15
HELIX   44  44 TYR C   75  TYR C  104  1                                  30
HELIX   45  45 GLY C  105  THR C  108  5                                   4
HELIX   46  46 PHE C  109  LEU C  133  1                                  25
HELIX   47  47 GLY C  136  LEU C  149  1                                  14
HELIX   48  48 LEU C  150  ILE C  153  5                                   4
HELIX   49  49 ILE C  156  GLY C  166  1                                  11
HELIX   50  50 ASP C  171  GLY C  204  1                                  34
HELIX   51  51 SER C  213  VAL C  215  5                                   3
HELIX   52  52 PHE C  220  ALA C  246  1                                  27
HELIX   53  53 PRO C  253  THR C  257  5                                   5
HELIX   54  54 GLU C  271  TYR C  273  5                                   3
HELIX   55  55 PHE C  274  SER C  283  1                                  10
HELIX   56  56 ASN C  286  ILE C  300  1                                  15
HELIX   57  57 LEU C  301  HIS C  308  5                                   8
HELIX   58  58 ARG C  318  GLY C  340  1                                  23
HELIX   59  59 GLU C  344  VAL C  364  1                                  21
HELIX   60  60 VAL C  364  LEU C  377  1                                  14
HELIX   61  61 ASP D   22  VAL D   36  1                                  15
HELIX   62  62 CYS D   37  CYS D   40  5                                   4
HELIX   63  63 HIS D   50  CYS D   55  1                                   6
HELIX   64  64 THR D   57  GLU D   66  1                                  10
HELIX   65  65 TYR D  115  ARG D  120  1                                   6
HELIX   66  66 GLY D  123  GLY D  133  1                                  11
HELIX   67  67 THR D  178  GLU D  195  1                                  18
HELIX   68  68 GLU D  197  SER D  232  1                                  36
HELIX   69  69 SER E    1  ILE E    5  5                                   5
HELIX   70  70 SER E   25  SER E   61  1                                  37
HELIX   71  71 SER E   79  ILE E   81  5                                   3
HELIX   72  72 THR E  102  VAL E  112  1                                  11
HELIX   73  73 HIS E  122  ARG E  126  5                                   5
HELIX   74  74 SER F    9  GLY F   25  1                                  17
HELIX   75  75 PHE F   26  GLY F   30  5                                   5
HELIX   76  76 MET F   32  ILE F   37  1                                   6
HELIX   77  77 ASN F   40  ARG F   49  1                                  10
HELIX   78  78 PRO F   51  GLN F   72  1                                  22
HELIX   79  79 LEU F   90  ALA F  108  1                                  19
HELIX   80  80 LYS G   32  SER G   69  1                                  38
HELIX   81  81 ASP H   15  GLU H   25  1                                  11
HELIX   82  82 LEU H   27  SER H   45  1                                  19
HELIX   83  83 CYS H   54  PHE H   74  1                                  21
HELIX   84  84 ASN H   75  LEU H   77  5                                   3
HELIX   85  85 SER I    3  SER I    8  5                                   6
HELIX   86  86 THR J    4  PHE J   14  1                                  11
HELIX   87  87 ARG J   16  ILE J   46  1                                  31
HELIX   88  88 LEU J   51  LYS J   56  1                                   6
HELIX   89  89 GLY K    7  TRP K   17  1                                  11
HELIX   90  90 TRP K   17  ASP K   37  1                                  21
HELIX   91  91 TRP K   38  ASP K   43  1                                   6
SHEET    1   A 6 GLN A  15  GLN A  18  0
SHEET    2   A 6 ARG A  24  GLN A  29 -1  O  VAL A  25   N  SER A  17
SHEET    3   A 6 MET A 195  GLY A 201  1  O  LEU A 197   N  ALA A  26
SHEET    4   A 6 THR A  34  ILE A  41 -1  N  GLY A  38   O  ALA A 198
SHEET    5   A 6 THR A  95  LEU A 102 -1  O  ILE A  99   N  VAL A  37
SHEET    6   A 6 HIS A  85  SER A  90 -1  N  HIS A  85   O  LYS A 100
SHEET    1   B 8 HIS A 279  ASP A 281  0
SHEET    2   B 8 SER A 306  TYR A 314 -1  O  PHE A 307   N  TYR A 280
SHEET    3   B 8 THR A 317  CYS A 326 -1  O  THR A 317   N  TYR A 314
SHEET    4   B 8 ALA A 251  GLY A 259 -1  N  GLY A 259   O  GLY A 318
SHEET    5   B 8 ALA A 421  GLY A 426 -1  O  ALA A 421   N  ALA A 256
SHEET    6   B 8 SER A 239  GLU A 245  1  N  HIS A 243   O  GLY A 424
SHEET    7   B 8 ARG G  11  LEU G  18 -1  O  THR G  15   N  CYS A 242
SHEET    8   B 8 LYS D 234  TYR D 237 -1  N  LYS D 234   O  TYR G  16
SHEET    1   C 8 GLU B  25  ARG B  28  0
SHEET    2   C 8 VAL B  34  LEU B  38 -1  O  ILE B  35   N  THR B  27
SHEET    3   C 8 MET B 204  LEU B 209  1  O  LEU B 206   N  VAL B  34
SHEET    4   C 8 ALA B  44  ILE B  51 -1  N  ARG B  46   O  LEU B 209
SHEET    5   C 8 MET B 105  LEU B 112 -1  O  TYR B 107   N  LEU B  49
SHEET    6   C 8 LYS B  95  SER B 100 -1  N  SER B  97   O  THR B 108
SHEET    7   C 8 PRO I  13  SER I  16 -1  O  LEU I  15   N  VAL B  98
SHEET    8   C 8 VAL I  22  ALA I  23 -1  O  VAL I  22   N  VAL I  14
SHEET    1   D 5 GLY B 242  GLN B 247  0
SHEET    2   D 5 LYS B 422  GLY B 428  1  O  MET B 424   N  ILE B 244
SHEET    3   D 5 LEU B 252  GLU B 260 -1  N  ALA B 256   O  ALA B 425
SHEET    4   D 5 SER B 319  GLN B 329 -1  O  THR B 326   N  ALA B 255
SHEET    5   D 5 PHE B 307  TYR B 316 -1  N  SER B 310   O  TYR B 325
SHEET    1   E 2 PRO C  22  PRO C  24  0
SHEET    2   E 2 LYS C 217  PRO C 219 -1  O  ILE C 218   N  ALA C  23
SHEET    1   F 2 MET D  43  ALA D  47  0
SHEET    2   F 2 TYR D  90  PHE D  91 -1  O  PHE D  91   N  VAL D  46
SHEET    1   G 3 ILE E  74  LYS E  77  0
SHEET    2   G 3 MET E 192  VAL E 195 -1  O  VAL E 193   N  ILE E  76
SHEET    3   G 3 TYR E 185  PHE E 187 -1  N  GLU E 186   O  ILE E 194
SHEET    1   H 3 ASN E  86  PHE E  89  0
SHEET    2   H 3 LEU E  96  HIS E 100 -1  O  LEU E  96   N  PHE E  89
SHEET    3   H 3 TRP E 132  ILE E 136 -1  O  LEU E 135   N  PHE E  97
SHEET    1   I 4 ILE E 147  ALA E 148  0
SHEET    2   I 4 TYR E 156  CYS E 158 -1  O  TYR E 157   N  ILE E 147
SHEET    3   I 4 SER E 163  TYR E 165 -1  O  TYR E 165   N  TYR E 156
SHEET    4   I 4 ILE E 171  LYS E 173 -1  O  ARG E 172   N  HIS E 164
SSBOND   1 CYS E  144    CYS E  160                          1555   1555  2.03
SSBOND   2 CYS H   24    CYS H   68                          1555   1555  2.04
SSBOND   3 CYS H   40    CYS H   54                          1555   1555  2.03
LINK         NE2 HIS C  97                FE   HEM C 382     1555   1555  2.35
LINK         NE2 HIS C 196                FE   HEM C 382     1555   1555  2.22
LINK         NE2 HIS C  83                FE   HEM C 381     1555   1555  2.20
LINK         NE2 HIS C 182                FE   HEM C 381     1555   1555  2.18
LINK         SD  MET D 160                FE   HEM D 242     1555   1555  2.96
LINK         NE2 HIS D  41                FE   HEM D 242     1555   1555  2.29
LINK         SG  CYS D  37                 CAB HEM D 242     1555   1555  3.23
LINK         SG  CYS D  40                 CAC HEM D 242     1555   1555  3.19
LINK         SG  CYS E 139                FE1  FES E 197     1555   1555  2.64
LINK         SG  CYS E 158                FE1  FES E 197     1555   1555  1.99
LINK         ND1 HIS E 161                FE2  FES E 197     1555   1555  1.99
LINK         ND1 HIS E 141                FE2  FES E 197     1555   1555  2.18
CISPEP   1 HIS C  221    PRO C  222          0         6.05
SITE     1 AC1 16 GLN C  44  GLY C  48  LEU C  51  ARG C  80
SITE     2 AC1 16 HIS C  83  ALA C  84  ALA C  87  PHE C  90
SITE     3 AC1 16 THR C 126  ALA C 127  GLY C 130  TYR C 131
SITE     4 AC1 16 PRO C 134  HIS C 182  PHE C 183  PRO C 186
SITE     1 AC2 16 TRP C  31  GLY C  34  LEU C  37  HIS C  97
SITE     2 AC2 16 ARG C 100  SER C 106  PHE C 109  TRP C 113
SITE     3 AC2 16 GLY C 116  VAL C 117  LEU C 119  LEU C 120
SITE     4 AC2 16 HIS C 196  SER C 205  ASN C 206  UQ2 C 384
SITE     1 AC3 15 CYS D  37  CYS D  40  HIS D  41  ASN D 105
SITE     2 AC3 15 ALA D 108  LEU D 109  PRO D 110  ARG D 120
SITE     3 AC3 15 TYR D 126  PHE D 153  ILE D 158  GLY D 159
SITE     4 AC3 15 MET D 160  ALA D 161  ILE D 164
SITE     1 AC4  9 CYS E 139  HIS E 141  LEU E 142  GLY E 143
SITE     2 AC4  9 CYS E 158  CYS E 160  HIS E 161  GLY E 162
SITE     3 AC4  9 SER E 163
SITE     1 AC5 11 LEU C 121  TYR C 131  MET C 138  GLY C 142
SITE     2 AC5 11 VAL C 145  ILE C 146  LYS C 269  PRO C 270
SITE     3 AC5 11 PHE C 274  TYR C 278  HIS E 161
SITE     1 AC6 11 PHE C  18  TRP C  31  SER C  35  LEU C 197
SITE     2 AC6 11 LEU C 200  HIS C 201  SER C 205  PHE C 220
SITE     3 AC6 11 ASP C 228  HEM C 382  HOH C 707
CRYST1  153.672  153.672  589.219  90.00  90.00  90.00 I 41 2 2     16
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      0.006507  0.000000  0.000000        0.00000
SCALE2      0.000000  0.006507  0.000000        0.00000
SCALE3      0.000000  0.000000  0.001697        0.00000
      
PROCHECK
Go to PROCHECK summary
 References