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PDBsum entry 1v54

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Top Page protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
1v54
Jmol
Contents
Protein chains
514 a.a. *
227 a.a. *
259 a.a. *
144 a.a. *
105 a.a. *
98 a.a. *
84 a.a. *
79 a.a. *
73 a.a. *
58 a.a. *
49 a.a. *
46 a.a. *
43 a.a. *
Ligands
HEA ×4
TGL ×6
PGV ×8
CUA ×2
CHD ×8
CDL ×4
PEK ×6
UNX ×2
PSC ×2
DMU ×2
Metals
_ZN ×2
_CU ×2
_MG ×2
_NA ×2
Waters ×1970
* Residue conservation analysis
HEADER    OXIDOREDUCTASE                          21-NOV-03   1V54
TITLE     BOVINE HEART CYTOCHROME C OXIDASE AT THE FULLY OXIDIZED STATE
CAVEAT     1V54    THERE ARE SEVERAL CHIRALITY ERRORS IN CHD.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE I;
COMPND   3 CHAIN: A, N;
COMPND   4 EC: 1.9.3.1;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE II;
COMPND   7 CHAIN: B, O;
COMPND   8 EC: 1.9.3.1;
COMPND   9 MOL_ID: 3;
COMPND  10 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE III;
COMPND  11 CHAIN: C, P;
COMPND  12 EC: 1.9.3.1;
COMPND  13 MOL_ID: 4;
COMPND  14 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT IV ISOFORM 1;
COMPND  15 CHAIN: D, Q;
COMPND  16 SYNONYM: COX IV-1, CYTOCHROME C OXIDASE POLYPEPTIDE IV;
COMPND  17 EC: 1.9.3.1;
COMPND  18 MOL_ID: 5;
COMPND  19 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VA;
COMPND  20 CHAIN: E, R;
COMPND  21 EC: 1.9.3.1;
COMPND  22 MOL_ID: 6;
COMPND  23 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VB;
COMPND  24 CHAIN: F, S;
COMPND  25 SYNONYM: VI;
COMPND  26 EC: 1.9.3.1;
COMPND  27 MOL_ID: 7;
COMPND  28 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIA-HEART;
COMPND  29 CHAIN: G, T;
COMPND  30 SYNONYM: COXVIAH, POLYPEPTIDE VIB;
COMPND  31 EC: 1.9.3.1;
COMPND  32 MOL_ID: 8;
COMPND  33 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIB;
COMPND  34 CHAIN: H, U;
COMPND  35 SYNONYM: AED;
COMPND  36 EC: 1.9.3.1;
COMPND  37 MOL_ID: 9;
COMPND  38 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIC;
COMPND  39 CHAIN: I, V;
COMPND  40 SYNONYM: STA;
COMPND  41 EC: 1.9.3.1;
COMPND  42 MOL_ID: 10;
COMPND  43 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA-HEART;
COMPND  44 CHAIN: J, W;
COMPND  45 SYNONYM: CYTOCHROME C OXIDASE SUBUNIT VIIA-H, COX VIIA-M, VIIIC;
COMPND  46 EC: 1.9.3.1;
COMPND  47 MOL_ID: 11;
COMPND  48 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIIB;
COMPND  49 CHAIN: K, X;
COMPND  50 SYNONYM: IHQ;
COMPND  51 EC: 1.9.3.1;
COMPND  52 MOL_ID: 12;
COMPND  53 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIIC;
COMPND  54 CHAIN: L, Y;
COMPND  55 SYNONYM: VIIIA;
COMPND  56 EC: 1.9.3.1;
COMPND  57 MOL_ID: 13;
COMPND  58 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIII-HEART;
COMPND  59 CHAIN: M, Z;
COMPND  60 SYNONYM: VIIIB, IX;
COMPND  61 EC: 1.9.3.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   3 ORGANISM_COMMON: CATTLE;
SOURCE   4 ORGANISM_TAXID: 9913;
SOURCE   5 TISSUE: HEART;
SOURCE   6 MOL_ID: 2;
SOURCE   7 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   8 ORGANISM_COMMON: CATTLE;
SOURCE   9 ORGANISM_TAXID: 9913;
SOURCE  10 TISSUE: HEART;
SOURCE  11 MOL_ID: 3;
SOURCE  12 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  13 ORGANISM_COMMON: CATTLE;
SOURCE  14 ORGANISM_TAXID: 9913;
SOURCE  15 TISSUE: HEART;
SOURCE  16 MOL_ID: 4;
SOURCE  17 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  18 ORGANISM_COMMON: CATTLE;
SOURCE  19 ORGANISM_TAXID: 9913;
SOURCE  20 TISSUE: HEART;
SOURCE  21 MOL_ID: 5;
SOURCE  22 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  23 ORGANISM_COMMON: CATTLE;
SOURCE  24 ORGANISM_TAXID: 9913;
SOURCE  25 TISSUE: HEART;
SOURCE  26 MOL_ID: 6;
SOURCE  27 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  28 ORGANISM_COMMON: CATTLE;
SOURCE  29 ORGANISM_TAXID: 9913;
SOURCE  30 TISSUE: HEART;
SOURCE  31 MOL_ID: 7;
SOURCE  32 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  33 ORGANISM_COMMON: CATTLE;
SOURCE  34 ORGANISM_TAXID: 9913;
SOURCE  35 TISSUE: HEART;
SOURCE  36 MOL_ID: 8;
SOURCE  37 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  38 ORGANISM_COMMON: CATTLE;
SOURCE  39 ORGANISM_TAXID: 9913;
SOURCE  40 TISSUE: HEART;
SOURCE  41 MOL_ID: 9;
SOURCE  42 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  43 ORGANISM_COMMON: CATTLE;
SOURCE  44 ORGANISM_TAXID: 9913;
SOURCE  45 TISSUE: HEART;
SOURCE  46 MOL_ID: 10;
SOURCE  47 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  48 ORGANISM_COMMON: CATTLE;
SOURCE  49 ORGANISM_TAXID: 9913;
SOURCE  50 TISSUE: HEART;
SOURCE  51 MOL_ID: 11;
SOURCE  52 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  53 ORGANISM_COMMON: CATTLE;
SOURCE  54 ORGANISM_TAXID: 9913;
SOURCE  55 TISSUE: HEART;
SOURCE  56 MOL_ID: 12;
SOURCE  57 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  58 ORGANISM_COMMON: CATTLE;
SOURCE  59 ORGANISM_TAXID: 9913;
SOURCE  60 TISSUE: HEART;
SOURCE  61 MOL_ID: 13;
SOURCE  62 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  63 ORGANISM_COMMON: CATTLE;
SOURCE  64 ORGANISM_TAXID: 9913;
SOURCE  65 TISSUE: HEART
KEYWDS    OXIDOREDUCTASE
EXPDTA    X-RAY DIFFRACTION
AUTHOR    T.TSUKIHARA,K.SHIMOKATA,Y.KATAYAMA,H.SHIMADA,K.MURAMOTO,H.AOYAMA,
AUTHOR   2 M.MOCHIZUKI,K.SHINZAWA-ITOH,E.YAMASHITA,M.YAO,Y.ISHIMURA,S.YOSHIKAWA
REVDAT   3   13-JUL-11 1V54    1       VERSN
REVDAT   2   24-FEB-09 1V54    1       VERSN
REVDAT   1   23-DEC-03 1V54    0
JRNL        AUTH   T.TSUKIHARA,K.SHIMOKATA,Y.KATAYAMA,H.SHIMADA,K.MURAMOTO,
JRNL        AUTH 2 H.AOYAMA,M.MOCHIZUKI,K.SHINZAWA-ITOH,E.YAMASHITA,M.YAO,
JRNL        AUTH 3 Y.ISHIMURA,S.YOSHIKAWA
JRNL        TITL   THE LOW-SPIN HEME OF CYTOCHROME C OXIDASE AS THE DRIVING
JRNL        TITL 2 ELEMENT OF THE PROTON-PUMPING PROCESS.
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 100 15304 2003
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   14673090
JRNL        DOI    10.1073/PNAS.2635097100
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 604170
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.202
REMARK   3   FREE R VALUE                     : 0.227
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 28506
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 2160
REMARK   3   SOLVENT ATOMS            : 1970
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: THE (FO-FC) DIFFERENCE FOURIER MAP
REMARK   3  SHOWS A RESIDUAL DENSITY BETWEEN HEME A3 IRON AND CUB.
REMARK   4
REMARK   4 1V54 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-DEC-03.
REMARK 100 THE RCSB ID CODE IS RCSB006217.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : NULL
REMARK 200  TEMPERATURE           (KELVIN) : NULL
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : NULL
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SPRING-8
REMARK 200  BEAMLINE                       : BL44XU
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : NULL
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 69.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
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       91.29500
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       89.12500
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      102.57000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       89.12500
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       91.29500
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      102.57000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 26-MERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 26-MERIC
REMARK 350 SOFTWARE USED: PISA,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 172140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 109890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1366.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350                    AND CHAINS: J, K, L, M, N, O, P, Q, R,
REMARK 350                    AND CHAINS: S, T, U, V, W, X, Y, Z
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 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     THR C     2
REMARK 465     ALA D     1
REMARK 465     HIS D     2
REMARK 465     GLY D     3
REMARK 465     SER E     1
REMARK 465     HIS E     2
REMARK 465     GLY E     3
REMARK 465     SER E     4
REMARK 465     PRO G    85
REMARK 465     ALA H     1
REMARK 465     GLU H     2
REMARK 465     ASP H     3
REMARK 465     ILE H     4
REMARK 465     GLN H     5
REMARK 465     ALA H     6
REMARK 465     LYS J    59
REMARK 465     ILE K     1
REMARK 465     HIS K     2
REMARK 465     GLN K     3
REMARK 465     LYS K     4
REMARK 465     ARG K     5
REMARK 465     GLU K    55
REMARK 465     GLN K    56
REMARK 465     SER L     1
REMARK 465     SER M    44
REMARK 465     ALA M    45
REMARK 465     ALA M    46
REMARK 465     MET P     1
REMARK 465     THR P     2
REMARK 465     ALA Q     1
REMARK 465     HIS Q     2
REMARK 465     GLY Q     3
REMARK 465     SER R     1
REMARK 465     HIS R     2
REMARK 465     GLY R     3
REMARK 465     SER R     4
REMARK 465     PRO T    85
REMARK 465     ALA U     1
REMARK 465     GLU U     2
REMARK 465     ASP U     3
REMARK 465     ILE U     4
REMARK 465     GLN U     5
REMARK 465     ALA U     6
REMARK 465     LYS W    59
REMARK 465     ILE X     1
REMARK 465     HIS X     2
REMARK 465     GLN X     3
REMARK 465     LYS X     4
REMARK 465     ARG X     5
REMARK 465     GLU X    55
REMARK 465     GLN X    56
REMARK 465     SER Y     1
REMARK 465     SER Z    44
REMARK 465     ALA Z    45
REMARK 465     ALA Z    46
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    HIS A  61   CB  -  CG  -  CD2 ANGL. DEV. = -10.5 DEGREES
REMARK 500    GLN B 103   CA  -  C   -  N   ANGL. DEV. = -13.6 DEGREES
REMARK 500    HIS S  94   N   -  CA  -  C   ANGL. DEV. =  16.9 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    ASP A  50     -167.86    -78.24
REMARK 500    MET A  69      -65.12   -108.80
REMARK 500    ASP A  91     -166.90    178.35
REMARK 500    GLU A 119     -134.73     48.18
REMARK 500    THR A 218       47.46   -141.86
REMARK 500    LEU A 483      -75.91   -109.65
REMARK 500    GLU B  60      -44.36   -174.21
REMARK 500    ASN B  92       92.23     61.31
REMARK 500    GLN B 103       88.58    -67.90
REMARK 500    TRP B 104       44.09     85.28
REMARK 500    TYR B 105      163.78    178.18
REMARK 500    LEU B 135       -8.78     69.97
REMARK 500    ASP B 158     -102.14   -144.97
REMARK 500    LYS B 171      107.93   -169.51
REMARK 500    MET B 185      101.90   -161.45
REMARK 500    ASN C  38       59.90     31.58
REMARK 500    SER C  65      -66.20    -99.70
REMARK 500    GLU C 128     -116.40   -100.21
REMARK 500    HIS C 232       56.49   -162.29
REMARK 500    TRP C 258      -72.02    -94.91
REMARK 500    GLN D 132      -41.57   -148.58
REMARK 500    PHE D 134      -69.20   -140.60
REMARK 500    ASP F  65        0.75     81.62
REMARK 500    HIS F  94      175.03     49.38
REMARK 500    GLN F  95      -98.73     93.27
REMARK 500    LEU F  96      -76.47     62.81
REMARK 500    ALA G   3      -93.16     85.21
REMARK 500    ALA G   4       10.47    162.07
REMARK 500    LYS G   5     -130.54   -110.18
REMARK 500    ASP G   7      -95.92     10.30
REMARK 500    HIS G   8       -3.85     45.29
REMARK 500    LEU G  23      -56.88   -128.55
REMARK 500    LEU G  37      -53.39   -153.55
REMARK 500    SER G  39     -119.35    -65.33
REMARK 500    SER G  61       25.74    -79.17
REMARK 500    LYS H   9     -122.04    -94.16
REMARK 500    ASN H  10       33.45     77.96
REMARK 500    GLN H  12      -64.72    -96.47
REMARK 500    ALA H  45      -75.26    -79.90
REMARK 500    LYS H  46        9.99    -61.81
REMARK 500    LYS I  36       37.88    -76.06
REMARK 500    PHE I  37      -51.96   -154.11
REMARK 500    VAL I  39      -60.80   -130.60
REMARK 500    ASP N  50     -169.60    -77.34
REMARK 500    MET N  69      -66.73   -106.57
REMARK 500    ASP N  91     -167.20    179.73
REMARK 500    GLU N 119     -132.32     46.43
REMARK 500    LEU N 483      -72.13   -108.43
REMARK 500    GLU O  60      -47.73   -172.54
REMARK 500    ASN O  92       92.91     56.46
REMARK 500
REMARK 500 THIS ENTRY HAS      85 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR A  19         0.07    SIDE CHAIN
REMARK 500    HIS A 240         0.14    SIDE CHAIN
REMARK 500    HIS N 240         0.14    SIDE CHAIN
REMARK 500    TYR N 304         0.07    SIDE CHAIN
REMARK 500    TYR U  11         0.07    SIDE CHAIN
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    PHE A 377        24.2      L          L   OUTSIDE RANGE
REMARK 500    TRP B  65        24.0      L          L   OUTSIDE RANGE
REMARK 500    TRP B 104        17.4      L          L   OUTSIDE RANGE
REMARK 500    HIS F  94        23.3      L          L   OUTSIDE RANGE
REMARK 500    GLN F  95        20.0      L          L   OUTSIDE RANGE
REMARK 500    PHE N 377        24.4      L          L   OUTSIDE RANGE
REMARK 500    TRP O  65        23.6      L          L   OUTSIDE RANGE
REMARK 500    TRP O 104        19.4      L          L   OUTSIDE RANGE
REMARK 500    HIS S  94        17.7      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 A3681        DISTANCE =  5.39 ANGSTROMS
REMARK 525    HOH A3741        DISTANCE =  6.71 ANGSTROMS
REMARK 525    HOH E3249        DISTANCE =  5.71 ANGSTROMS
REMARK 525    HOH H 689        DISTANCE =  5.02 ANGSTROMS
REMARK 525    HOH I2599        DISTANCE =  6.27 ANGSTROMS
REMARK 525    HOH J 454        DISTANCE =  5.23 ANGSTROMS
REMARK 525    HOH K  81        DISTANCE =  5.76 ANGSTROMS
REMARK 525    HOH K  91        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH N1443        DISTANCE =  5.10 ANGSTROMS
REMARK 525    HOH P1484        DISTANCE =  5.75 ANGSTROMS
REMARK 525    HOH Q2206        DISTANCE =  5.15 ANGSTROMS
REMARK 525    HOH T2308        DISTANCE =  5.73 ANGSTROMS
REMARK 525    HOH T2532        DISTANCE =  5.53 ANGSTROMS
REMARK 525    HOH X2354        DISTANCE =  5.49 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                              NA A3519  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A  40   O
REMARK 620 2 GLU A  40   OE1  80.3
REMARK 620 3 GLY A  45   O   131.3  90.2
REMARK 620 4 SER A 441   O   115.9  80.2 109.2
REMARK 620 5 HOH A3544   O    90.9 171.1  95.2 104.5
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEA A 515  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  61   NE2
REMARK 620 2 HEA A 515   NA   92.1
REMARK 620 3 HEA A 515   NB   91.6  90.5
REMARK 620 4 HEA A 515   NC   92.1 175.7  90.4
REMARK 620 5 HEA A 515   ND   87.3  89.1 178.8  90.0
REMARK 620 6 HIS A 378   NE2 176.8  91.1  87.9  84.7  93.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CU A 517  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 240   ND1
REMARK 620 2 HIS A 290   NE2 104.5
REMARK 620 3 HIS A 291   NE2 154.9  91.5
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A3518  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 368   NE2
REMARK 620 2 ASP A 369   OD1  91.9
REMARK 620 3 GLU B 198   OE1 174.9  93.0
REMARK 620 4 HOH B4093   O    84.4  92.5  94.3
REMARK 620 5 HOH B4091   O    82.8 173.8  92.3  90.3
REMARK 620 6 HOH B4092   O    93.6  91.4  87.4 175.7  85.7
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEA A 516  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 376   NE2
REMARK 620 2 HEA A 516   NA   93.1
REMARK 620 3 HEA A 516   NB  101.3  88.9
REMARK 620 4 HEA A 516   NC  100.1 166.6  90.3
REMARK 620 5 HEA A 516   ND   90.7  90.6 168.0  87.3
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CUA B 228  CU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 161   ND1
REMARK 620 2 CUA B 228  CU2  133.7
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CUA B 228  CU2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 204   ND1
REMARK 620 2 CUA B 228  CU1  160.0
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN F  99  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS F  60   SG
REMARK 620 2 CYS F  62   SG  118.4
REMARK 620 3 CYS F  82   SG  103.3 109.0
REMARK 620 4 CYS F  85   SG  109.1 108.0 108.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA N4519  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU N  40   O
REMARK 620 2 GLU N  40   OE1  82.2
REMARK 620 3 GLY N  45   O   131.7  93.3
REMARK 620 4 SER N 441   O   115.4  82.3 111.6
REMARK 620 5 HOH N1026   O    90.5 172.5  90.1 102.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEA N 515  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N  61   NE2
REMARK 620 2 HEA N 515   NA   92.8
REMARK 620 3 HEA N 515   NB   88.8  90.3
REMARK 620 4 HEA N 515   NC   90.5 176.7  90.2
REMARK 620 5 HEA N 515   ND   86.9  90.3 175.7  89.5
REMARK 620 6 HIS N 378   NE2 174.3  91.1  87.0  85.7  97.3
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CU N 517  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 240   ND1
REMARK 620 2 HIS N 290   NE2 103.9
REMARK 620 3 HIS N 291   NE2 154.7  93.9
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG N4518  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 368   NE2
REMARK 620 2 ASP N 369   OD1  88.9
REMARK 620 3 GLU O 198   OE1 169.8 101.0
REMARK 620 4 HOH O1033   O    88.4  92.4  88.6
REMARK 620 5 HOH O1032   O    96.1  91.7  86.2 174.0
REMARK 620 6 HOH O1031   O    88.0 176.0  82.3  90.0  86.2
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEA N 516  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 376   NE2
REMARK 620 2 HEA N 516   NA   94.3
REMARK 620 3 HEA N 516   NB   92.7  88.1
REMARK 620 4 HEA N 516   NC   99.5 166.0  89.1
REMARK 620 5 HEA N 516   ND  100.8  90.9 166.4  88.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CUA O 228  CU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 161   ND1
REMARK 620 2 CUA O 228  CU2  132.0
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CUA O 228  CU2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 204   ND1
REMARK 620 2 CUA O 228  CU1  155.5
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN S  99  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS S  60   SG
REMARK 620 2 CYS S  62   SG  115.1
REMARK 620 3 CYS S  82   SG  109.7 107.9
REMARK 620 4 CYS S  85   SG  108.1 106.3 109.6
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 CU A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 3519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL A 3521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV A 3266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV A 3524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA B 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD B 4085
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD C 3525
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD C 3271
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL C 3270
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK C 3264
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK C 3265
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV C 3267
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV C 3268
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX C 3262
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL D 3523
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSC E 3230
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 99
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL G 3269
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK G 4263
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD J 3060
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL L 3522
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU M 3526
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU N 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 4518
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA N 4519
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA N 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA N 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL N 4521
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL N 4522
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV N 4266
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV N 4524
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD O 3085
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSC O 4230
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA O 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD P 4525
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD P 4271
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL P 4270
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK P 4264
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK P 4265
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV P 4267
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV P 4268
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX P 4262
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL Q 4523
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN S 99
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK T 3263
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL T 4269
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD W 4060
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU Z 4526
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1V55   RELATED DB: PDB
REMARK 900 THE SAME PROTEIN AT THE FULLY REDUCED STATE
DBREF  1V54 A    1   514  UNP    P00396   COX1_BOVIN       1    514
DBREF  1V54 B    1   227  UNP    P68530   COX2_BOVIN       1    227
DBREF  1V54 C    1   261  UNP    P00415   COX3_BOVIN       1    261
DBREF  1V54 D    1   147  UNP    P00423   COX41_BOVIN     23    169
DBREF  1V54 E    1   109  UNP    P00426   COX5A_BOVIN     44    152
DBREF  1V54 F    1    98  UNP    P00428   COX5B_BOVIN     32    129
DBREF  1V54 G    1    85  UNP    P07471   CX6A2_BOVIN     13     97
DBREF  1V54 H    1    85  UNP    P00429   CX6B1_BOVIN      2     86
DBREF  1V54 I    1    73  UNP    P04038   COX6C_BOVIN      1     73
DBREF  1V54 J    1    59  UNP    P07470   CX7A1_BOVIN     22     80
DBREF  1V54 K    1    56  UNP    P13183   COX7B_BOVIN     25     80
DBREF  1V54 L    1    47  UNP    P00430   COX7C_BOVIN     17     63
DBREF  1V54 M    1    46  UNP    P10175   COX81_BOVIN     25     70
DBREF  1V54 N    1   514  UNP    P00396   COX1_BOVIN       1    514
DBREF  1V54 O    1   227  UNP    P68530   COX2_BOVIN       1    227
DBREF  1V54 P    1   261  UNP    P00415   COX3_BOVIN       1    261
DBREF  1V54 Q    1   147  UNP    P00423   COX41_BOVIN     23    169
DBREF  1V54 R    1   109  UNP    P00426   COX5A_BOVIN     44    152
DBREF  1V54 S    1    98  UNP    P00428   COX5B_BOVIN     32    129
DBREF  1V54 T    1    85  UNP    P07471   CX6A2_BOVIN     13     97
DBREF  1V54 U    1    85  UNP    P00429   CX6B1_BOVIN      2     86
DBREF  1V54 V    1    73  UNP    P04038   COX6C_BOVIN      1     73
DBREF  1V54 W    1    59  UNP    P07470   CX7A1_BOVIN     22     80
DBREF  1V54 X    1    56  UNP    P13183   COX7B_BOVIN     25     80
DBREF  1V54 Y    1    47  UNP    P00430   COX7C_BOVIN     17     63
DBREF  1V54 Z    1    46  UNP    P10175   COX81_BOVIN     25     70
SEQRES   1 A  514  FME PHE ILE ASN ARG TRP LEU PHE SER THR ASN HIS LYS
SEQRES   2 A  514  ASP ILE GLY THR LEU TYR LEU LEU PHE GLY ALA TRP ALA
SEQRES   3 A  514  GLY MET VAL GLY THR ALA LEU SER LEU LEU ILE ARG ALA
SEQRES   4 A  514  GLU LEU GLY GLN PRO GLY THR LEU LEU GLY ASP ASP GLN
SEQRES   5 A  514  ILE TYR ASN VAL VAL VAL THR ALA HIS ALA PHE VAL MET
SEQRES   6 A  514  ILE PHE PHE MET VAL MET PRO ILE MET ILE GLY GLY PHE
SEQRES   7 A  514  GLY ASN TRP LEU VAL PRO LEU MET ILE GLY ALA PRO ASP
SEQRES   8 A  514  MET ALA PHE PRO ARG MET ASN ASN MET SER PHE TRP LEU
SEQRES   9 A  514  LEU PRO PRO SER PHE LEU LEU LEU LEU ALA SER SER MET
SEQRES  10 A  514  VAL GLU ALA GLY ALA GLY THR GLY TRP THR VAL TYR PRO
SEQRES  11 A  514  PRO LEU ALA GLY ASN LEU ALA HIS ALA GLY ALA SER VAL
SEQRES  12 A  514  ASP LEU THR ILE PHE SER LEU HIS LEU ALA GLY VAL SER
SEQRES  13 A  514  SER ILE LEU GLY ALA ILE ASN PHE ILE THR THR ILE ILE
SEQRES  14 A  514  ASN MET LYS PRO PRO ALA MET SER GLN TYR GLN THR PRO
SEQRES  15 A  514  LEU PHE VAL TRP SER VAL MET ILE THR ALA VAL LEU LEU
SEQRES  16 A  514  LEU LEU SER LEU PRO VAL LEU ALA ALA GLY ILE THR MET
SEQRES  17 A  514  LEU LEU THR ASP ARG ASN LEU ASN THR THR PHE PHE ASP
SEQRES  18 A  514  PRO ALA GLY GLY GLY ASP PRO ILE LEU TYR GLN HIS LEU
SEQRES  19 A  514  PHE TRP PHE PHE GLY HIS PRO GLU VAL TYR ILE LEU ILE
SEQRES  20 A  514  LEU PRO GLY PHE GLY MET ILE SER HIS ILE VAL THR TYR
SEQRES  21 A  514  TYR SER GLY LYS LYS GLU PRO PHE GLY TYR MET GLY MET
SEQRES  22 A  514  VAL TRP ALA MET MET SER ILE GLY PHE LEU GLY PHE ILE
SEQRES  23 A  514  VAL TRP ALA HIS HIS MET PHE THR VAL GLY MET ASP VAL
SEQRES  24 A  514  ASP THR ARG ALA TYR PHE THR SER ALA THR MET ILE ILE
SEQRES  25 A  514  ALA ILE PRO THR GLY VAL LYS VAL PHE SER TRP LEU ALA
SEQRES  26 A  514  THR LEU HIS GLY GLY ASN ILE LYS TRP SER PRO ALA MET
SEQRES  27 A  514  MET TRP ALA LEU GLY PHE ILE PHE LEU PHE THR VAL GLY
SEQRES  28 A  514  GLY LEU THR GLY ILE VAL LEU ALA ASN SER SER LEU ASP
SEQRES  29 A  514  ILE VAL LEU HIS ASP THR TYR TYR VAL VAL ALA HIS PHE
SEQRES  30 A  514  HIS TYR VAL LEU SER MET GLY ALA VAL PHE ALA ILE MET
SEQRES  31 A  514  GLY GLY PHE VAL HIS TRP PHE PRO LEU PHE SER GLY TYR
SEQRES  32 A  514  THR LEU ASN ASP THR TRP ALA LYS ILE HIS PHE ALA ILE
SEQRES  33 A  514  MET PHE VAL GLY VAL ASN MET THR PHE PHE PRO GLN HIS
SEQRES  34 A  514  PHE LEU GLY LEU SER GLY MET PRO ARG ARG TYR SER ASP
SEQRES  35 A  514  TYR PRO ASP ALA TYR THR MET TRP ASN THR ILE SER SER
SEQRES  36 A  514  MET GLY SER PHE ILE SER LEU THR ALA VAL MET LEU MET
SEQRES  37 A  514  VAL PHE ILE ILE TRP GLU ALA PHE ALA SER LYS ARG GLU
SEQRES  38 A  514  VAL LEU THR VAL ASP LEU THR THR THR ASN LEU GLU TRP
SEQRES  39 A  514  LEU ASN GLY CYS PRO PRO PRO TYR HIS THR PHE GLU GLU
SEQRES  40 A  514  PRO THR TYR VAL ASN LEU LYS
SEQRES   1 B  227  FME ALA TYR PRO MET GLN LEU GLY PHE GLN ASP ALA THR
SEQRES   2 B  227  SER PRO ILE MET GLU GLU LEU LEU HIS PHE HIS ASP HIS
SEQRES   3 B  227  THR LEU MET ILE VAL PHE LEU ILE SER SER LEU VAL LEU
SEQRES   4 B  227  TYR ILE ILE SER LEU MET LEU THR THR LYS LEU THR HIS
SEQRES   5 B  227  THR SER THR MET ASP ALA GLN GLU VAL GLU THR ILE TRP
SEQRES   6 B  227  THR ILE LEU PRO ALA ILE ILE LEU ILE LEU ILE ALA LEU
SEQRES   7 B  227  PRO SER LEU ARG ILE LEU TYR MET MET ASP GLU ILE ASN
SEQRES   8 B  227  ASN PRO SER LEU THR VAL LYS THR MET GLY HIS GLN TRP
SEQRES   9 B  227  TYR TRP SER TYR GLU TYR THR ASP TYR GLU ASP LEU SER
SEQRES  10 B  227  PHE ASP SER TYR MET ILE PRO THR SER GLU LEU LYS PRO
SEQRES  11 B  227  GLY GLU LEU ARG LEU LEU GLU VAL ASP ASN ARG VAL VAL
SEQRES  12 B  227  LEU PRO MET GLU MET THR ILE ARG MET LEU VAL SER SER
SEQRES  13 B  227  GLU ASP VAL LEU HIS SER TRP ALA VAL PRO SER LEU GLY
SEQRES  14 B  227  LEU LYS THR ASP ALA ILE PRO GLY ARG LEU ASN GLN THR
SEQRES  15 B  227  THR LEU MET SER SER ARG PRO GLY LEU TYR TYR GLY GLN
SEQRES  16 B  227  CYS SER GLU ILE CYS GLY SER ASN HIS SER PHE MET PRO
SEQRES  17 B  227  ILE VAL LEU GLU LEU VAL PRO LEU LYS TYR PHE GLU LYS
SEQRES  18 B  227  TRP SER ALA SER MET LEU
SEQRES   1 C  261  MET THR HIS GLN THR HIS ALA TYR HIS MET VAL ASN PRO
SEQRES   2 C  261  SER PRO TRP PRO LEU THR GLY ALA LEU SER ALA LEU LEU
SEQRES   3 C  261  MET THR SER GLY LEU THR MET TRP PHE HIS PHE ASN SER
SEQRES   4 C  261  MET THR LEU LEU MET ILE GLY LEU THR THR ASN MET LEU
SEQRES   5 C  261  THR MET TYR GLN TRP TRP ARG ASP VAL ILE ARG GLU SER
SEQRES   6 C  261  THR PHE GLN GLY HIS HIS THR PRO ALA VAL GLN LYS GLY
SEQRES   7 C  261  LEU ARG TYR GLY MET ILE LEU PHE ILE ILE SER GLU VAL
SEQRES   8 C  261  LEU PHE PHE THR GLY PHE PHE TRP ALA PHE TYR HIS SER
SEQRES   9 C  261  SER LEU ALA PRO THR PRO GLU LEU GLY GLY CYS TRP PRO
SEQRES  10 C  261  PRO THR GLY ILE HIS PRO LEU ASN PRO LEU GLU VAL PRO
SEQRES  11 C  261  LEU LEU ASN THR SER VAL LEU LEU ALA SER GLY VAL SER
SEQRES  12 C  261  ILE THR TRP ALA HIS HIS SER LEU MET GLU GLY ASP ARG
SEQRES  13 C  261  LYS HIS MET LEU GLN ALA LEU PHE ILE THR ILE THR LEU
SEQRES  14 C  261  GLY VAL TYR PHE THR LEU LEU GLN ALA SER GLU TYR TYR
SEQRES  15 C  261  GLU ALA PRO PHE THR ILE SER ASP GLY VAL TYR GLY SER
SEQRES  16 C  261  THR PHE PHE VAL ALA THR GLY PHE HIS GLY LEU HIS VAL
SEQRES  17 C  261  ILE ILE GLY SER THR PHE LEU ILE VAL CYS PHE PHE ARG
SEQRES  18 C  261  GLN LEU LYS PHE HIS PHE THR SER ASN HIS HIS PHE GLY
SEQRES  19 C  261  PHE GLU ALA ALA ALA TRP TYR TRP HIS PHE VAL ASP VAL
SEQRES  20 C  261  VAL TRP LEU PHE LEU TYR VAL SER ILE TYR TRP TRP GLY
SEQRES  21 C  261  SER
SEQRES   1 D  147  ALA HIS GLY SER VAL VAL LYS SER GLU ASP TYR ALA LEU
SEQRES   2 D  147  PRO SER TYR VAL ASP ARG ARG ASP TYR PRO LEU PRO ASP
SEQRES   3 D  147  VAL ALA HIS VAL LYS ASN LEU SER ALA SER GLN LYS ALA
SEQRES   4 D  147  LEU LYS GLU LYS GLU LYS ALA SER TRP SER SER LEU SER
SEQRES   5 D  147  ILE ASP GLU LYS VAL GLU LEU TYR ARG LEU LYS PHE LYS
SEQRES   6 D  147  GLU SER PHE ALA GLU MET ASN ARG SER THR ASN GLU TRP
SEQRES   7 D  147  LYS THR VAL VAL GLY ALA ALA MET PHE PHE ILE GLY PHE
SEQRES   8 D  147  THR ALA LEU LEU LEU ILE TRP GLU LYS HIS TYR VAL TYR
SEQRES   9 D  147  GLY PRO ILE PRO HIS THR PHE GLU GLU GLU TRP VAL ALA
SEQRES  10 D  147  LYS GLN THR LYS ARG MET LEU ASP MET LYS VAL ALA PRO
SEQRES  11 D  147  ILE GLN GLY PHE SER ALA LYS TRP ASP TYR ASP LYS ASN
SEQRES  12 D  147  GLU TRP LYS LYS
SEQRES   1 E  109  SER HIS GLY SER HIS GLU THR ASP GLU GLU PHE ASP ALA
SEQRES   2 E  109  ARG TRP VAL THR TYR PHE ASN LYS PRO ASP ILE ASP ALA
SEQRES   3 E  109  TRP GLU LEU ARG LYS GLY MET ASN THR LEU VAL GLY TYR
SEQRES   4 E  109  ASP LEU VAL PRO GLU PRO LYS ILE ILE ASP ALA ALA LEU
SEQRES   5 E  109  ARG ALA CYS ARG ARG LEU ASN ASP PHE ALA SER ALA VAL
SEQRES   6 E  109  ARG ILE LEU GLU VAL VAL LYS ASP LYS ALA GLY PRO HIS
SEQRES   7 E  109  LYS GLU ILE TYR PRO TYR VAL ILE GLN GLU LEU ARG PRO
SEQRES   8 E  109  THR LEU ASN GLU LEU GLY ILE SER THR PRO GLU GLU LEU
SEQRES   9 E  109  GLY LEU ASP LYS VAL
SEQRES   1 F   98  ALA SER GLY GLY GLY VAL PRO THR ASP GLU GLU GLN ALA
SEQRES   2 F   98  THR GLY LEU GLU ARG GLU VAL MET LEU ALA ALA ARG LYS
SEQRES   3 F   98  GLY GLN ASP PRO TYR ASN ILE LEU ALA PRO LYS ALA THR
SEQRES   4 F   98  SER GLY THR LYS GLU ASP PRO ASN LEU VAL PRO SER ILE
SEQRES   5 F   98  THR ASN LYS ARG ILE VAL GLY CYS ILE CYS GLU GLU ASP
SEQRES   6 F   98  ASN SER THR VAL ILE TRP PHE TRP LEU HIS LYS GLY GLU
SEQRES   7 F   98  ALA GLN ARG CYS PRO SER CYS GLY THR HIS TYR LYS LEU
SEQRES   8 F   98  VAL PRO HIS GLN LEU ALA HIS
SEQRES   1 G   85  ALA SER ALA ALA LYS GLY ASP HIS GLY GLY TPO GLY ALA
SEQRES   2 G   85  ARG THR TRP ARG PHE LEU THR PHE GLY LEU ALA LEU PRO
SEQRES   3 G   85  SER VAL ALA LEU CYS THR LEU ASN SER TRP LEU HIS SER
SEQRES   4 G   85  GLY HIS ARG GLU ARG PRO ALA PHE ILE PRO TYR HIS HIS
SEQRES   5 G   85  LEU ARG ILE ARG THR LYS PRO PHE SER TRP GLY ASP GLY
SEQRES   6 G   85  ASN HIS THR PHE PHE HIS ASN PRO ARG VAL ASN PRO LEU
SEQRES   7 G   85  PRO THR GLY TYR GLU LYS PRO
SEQRES   1 H   85  ALA GLU ASP ILE GLN ALA LYS ILE LYS ASN TYR GLN THR
SEQRES   2 H   85  ALA PRO PHE ASP SER ARG PHE PRO ASN GLN ASN GLN THR
SEQRES   3 H   85  ARG ASN CYS TRP GLN ASN TYR LEU ASP PHE HIS ARG CYS
SEQRES   4 H   85  GLU LYS ALA MET THR ALA LYS GLY GLY ASP VAL SER VAL
SEQRES   5 H   85  CYS GLU TRP TYR ARG ARG VAL TYR LYS SER LEU CYS PRO
SEQRES   6 H   85  ILE SER TRP VAL SER THR TRP ASP ASP ARG ARG ALA GLU
SEQRES   7 H   85  GLY THR PHE PRO GLY LYS ILE
SEQRES   1 I   73  SAC THR ALA LEU ALA LYS PRO GLN MET ARG GLY LEU LEU
SEQRES   2 I   73  ALA ARG ARG LEU ARG PHE HIS ILE VAL GLY ALA PHE MET
SEQRES   3 I   73  VAL SER LEU GLY PHE ALA THR PHE TYR LYS PHE ALA VAL
SEQRES   4 I   73  ALA GLU LYS ARG LYS LYS ALA TYR ALA ASP PHE TYR ARG
SEQRES   5 I   73  ASN TYR ASP SER MET LYS ASP PHE GLU GLU MET ARG LYS
SEQRES   6 I   73  ALA GLY ILE PHE GLN SER ALA LYS
SEQRES   1 J   59  PHE GLU ASN ARG VAL ALA GLU LYS GLN LYS LEU PHE GLN
SEQRES   2 J   59  GLU ASP ASN GLY LEU PRO VAL HIS LEU LYS GLY GLY ALA
SEQRES   3 J   59  THR ASP ASN ILE LEU TYR ARG VAL THR MET THR LEU CYS
SEQRES   4 J   59  LEU GLY GLY THR LEU TYR SER LEU TYR CYS LEU GLY TRP
SEQRES   5 J   59  ALA SER PHE PRO HIS LYS LYS
SEQRES   1 K   56  ILE HIS GLN LYS ARG ALA PRO ASP PHE HIS ASP LYS TYR
SEQRES   2 K   56  GLY ASN ALA VAL LEU ALA SER GLY ALA THR PHE CYS VAL
SEQRES   3 K   56  ALA VAL TRP VAL TYR MET ALA THR GLN ILE GLY ILE GLU
SEQRES   4 K   56  TRP ASN PRO SER PRO VAL GLY ARG VAL THR PRO LYS GLU
SEQRES   5 K   56  TRP ARG GLU GLN
SEQRES   1 L   47  SER HIS TYR GLU GLU GLY PRO GLY LYS ASN ILE PRO PHE
SEQRES   2 L   47  SER VAL GLU ASN LYS TRP ARG LEU LEU ALA MET MET THR
SEQRES   3 L   47  LEU PHE PHE GLY SER GLY PHE ALA ALA PRO PHE PHE ILE
SEQRES   4 L   47  VAL ARG HIS GLN LEU LEU LYS LYS
SEQRES   1 M   46  ILE THR ALA LYS PRO ALA LYS THR PRO THR SER PRO LYS
SEQRES   2 M   46  GLU GLN ALA ILE GLY LEU SER VAL THR PHE LEU SER PHE
SEQRES   3 M   46  LEU LEU PRO ALA GLY TRP VAL LEU TYR HIS LEU ASP ASN
SEQRES   4 M   46  TYR LYS LYS SER SER ALA ALA
SEQRES   1 N  514  FME PHE ILE ASN ARG TRP LEU PHE SER THR ASN HIS LYS
SEQRES   2 N  514  ASP ILE GLY THR LEU TYR LEU LEU PHE GLY ALA TRP ALA
SEQRES   3 N  514  GLY MET VAL GLY THR ALA LEU SER LEU LEU ILE ARG ALA
SEQRES   4 N  514  GLU LEU GLY GLN PRO GLY THR LEU LEU GLY ASP ASP GLN
SEQRES   5 N  514  ILE TYR ASN VAL VAL VAL THR ALA HIS ALA PHE VAL MET
SEQRES   6 N  514  ILE PHE PHE MET VAL MET PRO ILE MET ILE GLY GLY PHE
SEQRES   7 N  514  GLY ASN TRP LEU VAL PRO LEU MET ILE GLY ALA PRO ASP
SEQRES   8 N  514  MET ALA PHE PRO ARG MET ASN ASN MET SER PHE TRP LEU
SEQRES   9 N  514  LEU PRO PRO SER PHE LEU LEU LEU LEU ALA SER SER MET
SEQRES  10 N  514  VAL GLU ALA GLY ALA GLY THR GLY TRP THR VAL TYR PRO
SEQRES  11 N  514  PRO LEU ALA GLY ASN LEU ALA HIS ALA GLY ALA SER VAL
SEQRES  12 N  514  ASP LEU THR ILE PHE SER LEU HIS LEU ALA GLY VAL SER
SEQRES  13 N  514  SER ILE LEU GLY ALA ILE ASN PHE ILE THR THR ILE ILE
SEQRES  14 N  514  ASN MET LYS PRO PRO ALA MET SER GLN TYR GLN THR PRO
SEQRES  15 N  514  LEU PHE VAL TRP SER VAL MET ILE THR ALA VAL LEU LEU
SEQRES  16 N  514  LEU LEU SER LEU PRO VAL LEU ALA ALA GLY ILE THR MET
SEQRES  17 N  514  LEU LEU THR ASP ARG ASN LEU ASN THR THR PHE PHE ASP
SEQRES  18 N  514  PRO ALA GLY GLY GLY ASP PRO ILE LEU TYR GLN HIS LEU
SEQRES  19 N  514  PHE TRP PHE PHE GLY HIS PRO GLU VAL TYR ILE LEU ILE
SEQRES  20 N  514  LEU PRO GLY PHE GLY MET ILE SER HIS ILE VAL THR TYR
SEQRES  21 N  514  TYR SER GLY LYS LYS GLU PRO PHE GLY TYR MET GLY MET
SEQRES  22 N  514  VAL TRP ALA MET MET SER ILE GLY PHE LEU GLY PHE ILE
SEQRES  23 N  514  VAL TRP ALA HIS HIS MET PHE THR VAL GLY MET ASP VAL
SEQRES  24 N  514  ASP THR ARG ALA TYR PHE THR SER ALA THR MET ILE ILE
SEQRES  25 N  514  ALA ILE PRO THR GLY VAL LYS VAL PHE SER TRP LEU ALA
SEQRES  26 N  514  THR LEU HIS GLY GLY ASN ILE LYS TRP SER PRO ALA MET
SEQRES  27 N  514  MET TRP ALA LEU GLY PHE ILE PHE LEU PHE THR VAL GLY
SEQRES  28 N  514  GLY LEU THR GLY ILE VAL LEU ALA ASN SER SER LEU ASP
SEQRES  29 N  514  ILE VAL LEU HIS ASP THR TYR TYR VAL VAL ALA HIS PHE
SEQRES  30 N  514  HIS TYR VAL LEU SER MET GLY ALA VAL PHE ALA ILE MET
SEQRES  31 N  514  GLY GLY PHE VAL HIS TRP PHE PRO LEU PHE SER GLY TYR
SEQRES  32 N  514  THR LEU ASN ASP THR TRP ALA LYS ILE HIS PHE ALA ILE
SEQRES  33 N  514  MET PHE VAL GLY VAL ASN MET THR PHE PHE PRO GLN HIS
SEQRES  34 N  514  PHE LEU GLY LEU SER GLY MET PRO ARG ARG TYR SER ASP
SEQRES  35 N  514  TYR PRO ASP ALA TYR THR MET TRP ASN THR ILE SER SER
SEQRES  36 N  514  MET GLY SER PHE ILE SER LEU THR ALA VAL MET LEU MET
SEQRES  37 N  514  VAL PHE ILE ILE TRP GLU ALA PHE ALA SER LYS ARG GLU
SEQRES  38 N  514  VAL LEU THR VAL ASP LEU THR THR THR ASN LEU GLU TRP
SEQRES  39 N  514  LEU ASN GLY CYS PRO PRO PRO TYR HIS THR PHE GLU GLU
SEQRES  40 N  514  PRO THR TYR VAL ASN LEU LYS
SEQRES   1 O  227  FME ALA TYR PRO MET GLN LEU GLY PHE GLN ASP ALA THR
SEQRES   2 O  227  SER PRO ILE MET GLU GLU LEU LEU HIS PHE HIS ASP HIS
SEQRES   3 O  227  THR LEU MET ILE VAL PHE LEU ILE SER SER LEU VAL LEU
SEQRES   4 O  227  TYR ILE ILE SER LEU MET LEU THR THR LYS LEU THR HIS
SEQRES   5 O  227  THR SER THR MET ASP ALA GLN GLU VAL GLU THR ILE TRP
SEQRES   6 O  227  THR ILE LEU PRO ALA ILE ILE LEU ILE LEU ILE ALA LEU
SEQRES   7 O  227  PRO SER LEU ARG ILE LEU TYR MET MET ASP GLU ILE ASN
SEQRES   8 O  227  ASN PRO SER LEU THR VAL LYS THR MET GLY HIS GLN TRP
SEQRES   9 O  227  TYR TRP SER TYR GLU TYR THR ASP TYR GLU ASP LEU SER
SEQRES  10 O  227  PHE ASP SER TYR MET ILE PRO THR SER GLU LEU LYS PRO
SEQRES  11 O  227  GLY GLU LEU ARG LEU LEU GLU VAL ASP ASN ARG VAL VAL
SEQRES  12 O  227  LEU PRO MET GLU MET THR ILE ARG MET LEU VAL SER SER
SEQRES  13 O  227  GLU ASP VAL LEU HIS SER TRP ALA VAL PRO SER LEU GLY
SEQRES  14 O  227  LEU LYS THR ASP ALA ILE PRO GLY ARG LEU ASN GLN THR
SEQRES  15 O  227  THR LEU MET SER SER ARG PRO GLY LEU TYR TYR GLY GLN
SEQRES  16 O  227  CYS SER GLU ILE CYS GLY SER ASN HIS SER PHE MET PRO
SEQRES  17 O  227  ILE VAL LEU GLU LEU VAL PRO LEU LYS TYR PHE GLU LYS
SEQRES  18 O  227  TRP SER ALA SER MET LEU
SEQRES   1 P  261  MET THR HIS GLN THR HIS ALA TYR HIS MET VAL ASN PRO
SEQRES   2 P  261  SER PRO TRP PRO LEU THR GLY ALA LEU SER ALA LEU LEU
SEQRES   3 P  261  MET THR SER GLY LEU THR MET TRP PHE HIS PHE ASN SER
SEQRES   4 P  261  MET THR LEU LEU MET ILE GLY LEU THR THR ASN MET LEU
SEQRES   5 P  261  THR MET TYR GLN TRP TRP ARG ASP VAL ILE ARG GLU SER
SEQRES   6 P  261  THR PHE GLN GLY HIS HIS THR PRO ALA VAL GLN LYS GLY
SEQRES   7 P  261  LEU ARG TYR GLY MET ILE LEU PHE ILE ILE SER GLU VAL
SEQRES   8 P  261  LEU PHE PHE THR GLY PHE PHE TRP ALA PHE TYR HIS SER
SEQRES   9 P  261  SER LEU ALA PRO THR PRO GLU LEU GLY GLY CYS TRP PRO
SEQRES  10 P  261  PRO THR GLY ILE HIS PRO LEU ASN PRO LEU GLU VAL PRO
SEQRES  11 P  261  LEU LEU ASN THR SER VAL LEU LEU ALA SER GLY VAL SER
SEQRES  12 P  261  ILE THR TRP ALA HIS HIS SER LEU MET GLU GLY ASP ARG
SEQRES  13 P  261  LYS HIS MET LEU GLN ALA LEU PHE ILE THR ILE THR LEU
SEQRES  14 P  261  GLY VAL TYR PHE THR LEU LEU GLN ALA SER GLU TYR TYR
SEQRES  15 P  261  GLU ALA PRO PHE THR ILE SER ASP GLY VAL TYR GLY SER
SEQRES  16 P  261  THR PHE PHE VAL ALA THR GLY PHE HIS GLY LEU HIS VAL
SEQRES  17 P  261  ILE ILE GLY SER THR PHE LEU ILE VAL CYS PHE PHE ARG
SEQRES  18 P  261  GLN LEU LYS PHE HIS PHE THR SER ASN HIS HIS PHE GLY
SEQRES  19 P  261  PHE GLU ALA ALA ALA TRP TYR TRP HIS PHE VAL ASP VAL
SEQRES  20 P  261  VAL TRP LEU PHE LEU TYR VAL SER ILE TYR TRP TRP GLY
SEQRES  21 P  261  SER
SEQRES   1 Q  147  ALA HIS GLY SER VAL VAL LYS SER GLU ASP TYR ALA LEU
SEQRES   2 Q  147  PRO SER TYR VAL ASP ARG ARG ASP TYR PRO LEU PRO ASP
SEQRES   3 Q  147  VAL ALA HIS VAL LYS ASN LEU SER ALA SER GLN LYS ALA
SEQRES   4 Q  147  LEU LYS GLU LYS GLU LYS ALA SER TRP SER SER LEU SER
SEQRES   5 Q  147  ILE ASP GLU LYS VAL GLU LEU TYR ARG LEU LYS PHE LYS
SEQRES   6 Q  147  GLU SER PHE ALA GLU MET ASN ARG SER THR ASN GLU TRP
SEQRES   7 Q  147  LYS THR VAL VAL GLY ALA ALA MET PHE PHE ILE GLY PHE
SEQRES   8 Q  147  THR ALA LEU LEU LEU ILE TRP GLU LYS HIS TYR VAL TYR
SEQRES   9 Q  147  GLY PRO ILE PRO HIS THR PHE GLU GLU GLU TRP VAL ALA
SEQRES  10 Q  147  LYS GLN THR LYS ARG MET LEU ASP MET LYS VAL ALA PRO
SEQRES  11 Q  147  ILE GLN GLY PHE SER ALA LYS TRP ASP TYR ASP LYS ASN
SEQRES  12 Q  147  GLU TRP LYS LYS
SEQRES   1 R  109  SER HIS GLY SER HIS GLU THR ASP GLU GLU PHE ASP ALA
SEQRES   2 R  109  ARG TRP VAL THR TYR PHE ASN LYS PRO ASP ILE ASP ALA
SEQRES   3 R  109  TRP GLU LEU ARG LYS GLY MET ASN THR LEU VAL GLY TYR
SEQRES   4 R  109  ASP LEU VAL PRO GLU PRO LYS ILE ILE ASP ALA ALA LEU
SEQRES   5 R  109  ARG ALA CYS ARG ARG LEU ASN ASP PHE ALA SER ALA VAL
SEQRES   6 R  109  ARG ILE LEU GLU VAL VAL LYS ASP LYS ALA GLY PRO HIS
SEQRES   7 R  109  LYS GLU ILE TYR PRO TYR VAL ILE GLN GLU LEU ARG PRO
SEQRES   8 R  109  THR LEU ASN GLU LEU GLY ILE SER THR PRO GLU GLU LEU
SEQRES   9 R  109  GLY LEU ASP LYS VAL
SEQRES   1 S   98  ALA SER GLY GLY GLY VAL PRO THR ASP GLU GLU GLN ALA
SEQRES   2 S   98  THR GLY LEU GLU ARG GLU VAL MET LEU ALA ALA ARG LYS
SEQRES   3 S   98  GLY GLN ASP PRO TYR ASN ILE LEU ALA PRO LYS ALA THR
SEQRES   4 S   98  SER GLY THR LYS GLU ASP PRO ASN LEU VAL PRO SER ILE
SEQRES   5 S   98  THR ASN LYS ARG ILE VAL GLY CYS ILE CYS GLU GLU ASP
SEQRES   6 S   98  ASN SER THR VAL ILE TRP PHE TRP LEU HIS LYS GLY GLU
SEQRES   7 S   98  ALA GLN ARG CYS PRO SER CYS GLY THR HIS TYR LYS LEU
SEQRES   8 S   98  VAL PRO HIS GLN LEU ALA HIS
SEQRES   1 T   85  ALA SER ALA ALA LYS GLY ASP HIS GLY GLY TPO GLY ALA
SEQRES   2 T   85  ARG THR TRP ARG PHE LEU THR PHE GLY LEU ALA LEU PRO
SEQRES   3 T   85  SER VAL ALA LEU CYS THR LEU ASN SER TRP LEU HIS SER
SEQRES   4 T   85  GLY HIS ARG GLU ARG PRO ALA PHE ILE PRO TYR HIS HIS
SEQRES   5 T   85  LEU ARG ILE ARG THR LYS PRO PHE SER TRP GLY ASP GLY
SEQRES   6 T   85  ASN HIS THR PHE PHE HIS ASN PRO ARG VAL ASN PRO LEU
SEQRES   7 T   85  PRO THR GLY TYR GLU LYS PRO
SEQRES   1 U   85  ALA GLU ASP ILE GLN ALA LYS ILE LYS ASN TYR GLN THR
SEQRES   2 U   85  ALA PRO PHE ASP SER ARG PHE PRO ASN GLN ASN GLN THR
SEQRES   3 U   85  ARG ASN CYS TRP GLN ASN TYR LEU ASP PHE HIS ARG CYS
SEQRES   4 U   85  GLU LYS ALA MET THR ALA LYS GLY GLY ASP VAL SER VAL
SEQRES   5 U   85  CYS GLU TRP TYR ARG ARG VAL TYR LYS SER LEU CYS PRO
SEQRES   6 U   85  ILE SER TRP VAL SER THR TRP ASP ASP ARG ARG ALA GLU
SEQRES   7 U   85  GLY THR PHE PRO GLY LYS ILE
SEQRES   1 V   73  SAC THR ALA LEU ALA LYS PRO GLN MET ARG GLY LEU LEU
SEQRES   2 V   73  ALA ARG ARG LEU ARG PHE HIS ILE VAL GLY ALA PHE MET
SEQRES   3 V   73  VAL SER LEU GLY PHE ALA THR PHE TYR LYS PHE ALA VAL
SEQRES   4 V   73  ALA GLU LYS ARG LYS LYS ALA TYR ALA ASP PHE TYR ARG
SEQRES   5 V   73  ASN TYR ASP SER MET LYS ASP PHE GLU GLU MET ARG LYS
SEQRES   6 V   73  ALA GLY ILE PHE GLN SER ALA LYS
SEQRES   1 W   59  PHE GLU ASN ARG VAL ALA GLU LYS GLN LYS LEU PHE GLN
SEQRES   2 W   59  GLU ASP ASN GLY LEU PRO VAL HIS LEU LYS GLY GLY ALA
SEQRES   3 W   59  THR ASP ASN ILE LEU TYR ARG VAL THR MET THR LEU CYS
SEQRES   4 W   59  LEU GLY GLY THR LEU TYR SER LEU TYR CYS LEU GLY TRP
SEQRES   5 W   59  ALA SER PHE PRO HIS LYS LYS
SEQRES   1 X   56  ILE HIS GLN LYS ARG ALA PRO ASP PHE HIS ASP LYS TYR
SEQRES   2 X   56  GLY ASN ALA VAL LEU ALA SER GLY ALA THR PHE CYS VAL
SEQRES   3 X   56  ALA VAL TRP VAL TYR MET ALA THR GLN ILE GLY ILE GLU
SEQRES   4 X   56  TRP ASN PRO SER PRO VAL GLY ARG VAL THR PRO LYS GLU
SEQRES   5 X   56  TRP ARG GLU GLN
SEQRES   1 Y   47  SER HIS TYR GLU GLU GLY PRO GLY LYS ASN ILE PRO PHE
SEQRES   2 Y   47  SER VAL GLU ASN LYS TRP ARG LEU LEU ALA MET MET THR
SEQRES   3 Y   47  LEU PHE PHE GLY SER GLY PHE ALA ALA PRO PHE PHE ILE
SEQRES   4 Y   47  VAL ARG HIS GLN LEU LEU LYS LYS
SEQRES   1 Z   46  ILE THR ALA LYS PRO ALA LYS THR PRO THR SER PRO LYS
SEQRES   2 Z   46  GLU GLN ALA ILE GLY LEU SER VAL THR PHE LEU SER PHE
SEQRES   3 Z   46  LEU LEU PRO ALA GLY TRP VAL LEU TYR HIS LEU ASP ASN
SEQRES   4 Z   46  TYR LYS LYS SER SER ALA ALA
MODRES 1V54 FME A    1  MET  N-FORMYLMETHIONINE
MODRES 1V54 FME B    1  MET  N-FORMYLMETHIONINE
MODRES 1V54 TPO G   11  THR  PHOSPHOTHREONINE
MODRES 1V54 SAC I    1  SER  N-ACETYL-SERINE
MODRES 1V54 FME N    1  MET  N-FORMYLMETHIONINE
MODRES 1V54 FME O    1  MET  N-FORMYLMETHIONINE
MODRES 1V54 TPO T   11  THR  PHOSPHOTHREONINE
MODRES 1V54 SAC V    1  SER  N-ACETYL-SERINE
HET    FME  A   1      10
HET    FME  B   1      10
HET    TPO  G  11      11
HET    SAC  I   1       9
HET    FME  N   1      10
HET    FME  O   1      10
HET    TPO  T  11      11
HET    SAC  V   1       9
HET     CU  A 517       1
HET     MG  A3518       1
HET     NA  A3519       1
HET    HEA  A 515      60
HET    HEA  A 516      60
HET    TGL  A3521      63
HET    PGV  A3266      51
HET    PGV  A3524      51
HET    CUA  B 228       2
HET    CHD  B4085      29
HET    CHD  C3525      29
HET    CHD  C3271      29
HET    CDL  C3270     100
HET    PEK  C3264      53
HET    PEK  C3265      53
HET    PGV  C3267      51
HET    PGV  C3268      51
HET    UNX  C3262       1
HET    TGL  D3523      63
HET    PSC  E3230      52
HET     ZN  F  99       1
HET    CDL  G3269     100
HET    PEK  G4263      53
HET    CHD  J3060      29
HET    TGL  L3522      63
HET    DMU  M3526      33
HET     CU  N 517       1
HET     MG  N4518       1
HET     NA  N4519       1
HET    HEA  N 515      60
HET    HEA  N 516      60
HET    TGL  N4521      63
HET    TGL  N4522      63
HET    PGV  N4266      51
HET    PGV  N4524      51
HET    CHD  O3085      29
HET    PSC  O4230      52
HET    CUA  O 228       2
HET    CHD  P4525      29
HET    CHD  P4271      29
HET    CDL  P4270     100
HET    PEK  P4264      53
HET    PEK  P4265      53
HET    PGV  P4267      51
HET    PGV  P4268      51
HET    UNX  P4262       1
HET    TGL  Q4523      63
HET     ZN  S  99       1
HET    PEK  T3263      53
HET    CDL  T4269     100
HET    CHD  W4060      29
HET    DMU  Z4526      33
HETNAM     FME N-FORMYLMETHIONINE
HETNAM     TPO PHOSPHOTHREONINE
HETNAM     SAC N-ACETYL-SERINE
HETNAM      CU COPPER (II) ION
HETNAM      MG MAGNESIUM ION
HETNAM      NA SODIUM ION
HETNAM     HEA HEME-A
HETNAM     TGL TRISTEAROYLGLYCEROL
HETNAM     PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)
HETNAM   2 PGV  PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-
HETNAM   3 PGV  OCTADEC-11-ENOATE
HETNAM     CUA DINUCLEAR COPPER ION
HETNAM     CHD CHOLIC ACID
HETNAM     CDL CARDIOLIPIN
HETNAM     PEK (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-
HETNAM   2 PEK  [(STEAROYLOXY)METHYL]ETHYL (5E,8E,11E,14E)-ICOSA-5,8,
HETNAM   3 PEK  11,14-TETRAENOATE
HETNAM     UNX UNKNOWN ATOM OR ION
HETNAM     PSC (7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-
HETNAM   2 PSC  [(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSA-
HETNAM   3 PSC  17,20-DIEN-1-AMINIUM 4-OXIDE
HETNAM      ZN ZINC ION
HETNAM     DMU DECYL-BETA-D-MALTOPYRANOSIDE
HETSYN     TPO PHOSPHONOTHREONINE
HETSYN     TGL TRIACYLGLYCEROL
HETSYN     PGV PHOSPHATIDYLGLYCEROL, 2-VACCENOYL-1-PALMITOYL-SN-
HETSYN   2 PGV  GLYCEROL-3-PHOSPHOGLYCEROL
HETSYN     CDL DIPHOSPHATIDYL GLYCEROL; BIS-(1,2-DIACYL-SN-GLYCERO-3-
HETSYN   2 CDL  PHOSPHO)-1',3'-SN-GLYCEROL
HETSYN     PEK PHOSPHATIDYLETHANOLAMINE, 2-ARACHIDONOYL-1-STEAROYL-SN-
HETSYN   2 PEK  GLYCEROL-3-PHOSPHOETHANOLAMINE
HETSYN     PSC PHOSPHATIDYLCHOLINE, 2-LINOLEOYL-1-PALMITOYL-SN-
HETSYN   2 PSC  GYCEROL-3-PHOSPHOCHOLINE
HETSYN     DMU DECYLMALTOSIDE
FORMUL   1  FME    4(C6 H11 N O3 S)
FORMUL   7  TPO    2(C4 H10 N O6 P)
FORMUL   9  SAC    2(C5 H9 N O4)
FORMUL  27   CU    2(CU 2+)
FORMUL  28   MG    2(MG 2+)
FORMUL  29   NA    2(NA 1+)
FORMUL  30  HEA    4(C49 H56 FE N4 O6)
FORMUL  32  TGL    6(C57 H110 O6)
FORMUL  33  PGV    8(C40 H77 O10 P)
FORMUL  35  CUA    2(CU2)
FORMUL  36  CHD    8(C24 H40 O5)
FORMUL  39  CDL    4(C81 H156 O17 P2 2-)
FORMUL  40  PEK    6(C43 H78 N O8 P)
FORMUL  44  UNX    2(X)
FORMUL  46  PSC    2(C42 H81 N O8 P 1+)
FORMUL  47   ZN    2(ZN 2+)
FORMUL  52  DMU    2(C22 H42 O11)
FORMUL  79  HOH   *1970(H2 O)
HELIX    1   1 FME A    1  LEU A    7  1                                   7
HELIX    2   2 ASN A   11  GLY A   42  1                                  32
HELIX    3   3 ASP A   50  PHE A   68  1                                  19
HELIX    4   4 MET A   69  ILE A   75  1                                   7
HELIX    5   5 GLY A   76  ILE A   87  1                                  12
HELIX    6   6 PHE A   94  LEU A  104  1                                  11
HELIX    7   7 LEU A  104  VAL A  118  1                                  15
HELIX    8   8 ALA A  141  MET A  171  1                                  31
HELIX    9   9 SER A  177  THR A  181  5                                   5
HELIX   10  10 PRO A  182  LEU A  215  1                                  34
HELIX   11  11 ASP A  221  GLY A  225  5                                   5
HELIX   12  12 ASP A  227  SER A  262  1                                  36
HELIX   13  13 GLY A  269  GLY A  284  1                                  16
HELIX   14  14 PHE A  285  ILE A  286  5                                   2
HELIX   15  15 VAL A  287  MET A  292  5                                   6
HELIX   16  16 ASP A  298  ILE A  312  1                                  15
HELIX   17  17 ILE A  312  HIS A  328  1                                  17
HELIX   18  18 SER A  335  ASN A  360  1                                  26
HELIX   19  19 ASN A  360  HIS A  368  1                                   9
HELIX   20  20 THR A  370  SER A  382  1                                  13
HELIX   21  21 MET A  383  GLY A  402  1                                  20
HELIX   22  22 ASN A  406  PHE A  426  1                                  21
HELIX   23  23 PHE A  426  SER A  434  1                                   9
HELIX   24  24 PRO A  444  ALA A  446  5                                   3
HELIX   25  25 TYR A  447  LYS A  479  1                                  33
HELIX   26  26 LEU A  487  LEU A  495  5                                   9
HELIX   27  27 SER B   14  THR B   47  1                                  34
HELIX   28  28 GLU B   60  GLU B   89  1                                  30
HELIX   29  29 PRO B  124  LEU B  128  5                                   5
HELIX   30  30 PRO B  166  GLY B  169  5                                   4
HELIX   31  31 ASN B  203  MET B  207  5                                   5
HELIX   32  32 PRO B  215  MET B  226  1                                  12
HELIX   33  33 PRO C   15  ASN C   38  1                                  24
HELIX   34  34 MET C   40  THR C   66  1                                  27
HELIX   35  35 THR C   72  ALA C  107  1                                  36
HELIX   36  36 THR C  109  GLY C  113  5                                   5
HELIX   37  37 GLU C  128  GLU C  153  1                                  26
HELIX   38  38 ASP C  155  ALA C  184  1                                  30
HELIX   39  39 ASP C  190  LYS C  224  1                                  35
HELIX   40  40 HIS C  232  ILE C  256  1                                  25
HELIX   41  41 LYS D    7  TYR D   11  5                                   5
HELIX   42  42 SER D   34  GLU D   44  1                                  11
HELIX   43  43 LYS D   45  ALA D   46  5                                   2
HELIX   44  44 SER D   47  LEU D   51  5                                   5
HELIX   45  45 SER D   52  PHE D   64  1                                  13
HELIX   46  46 SER D   67  ASN D   72  1                                   6
HELIX   47  47 ASN D   76  VAL D  103  1                                  28
HELIX   48  48 PRO D  108  PHE D  111  5                                   4
HELIX   49  49 GLU D  112  MET D  126  1                                  15
HELIX   50  50 PHE D  134  ALA D  136  5                                   3
HELIX   51  51 THR E    7  ASN E   20  1                                  14
HELIX   52  52 ASP E   25  VAL E   37  1                                  13
HELIX   53  53 GLU E   44  LEU E   58  1                                  15
HELIX   54  54 ASP E   60  ALA E   75  1                                  16
HELIX   55  55 GLU E   80  GLY E   97  1                                  18
HELIX   56  56 THR F    8  ALA F   13  1                                   6
HELIX   57  57 THR F   14  LYS F   26  1                                  13
HELIX   58  58 GLY G   12  LEU G   23  1                                  12
HELIX   59  59 LEU G   23  TRP G   36  1                                  14
HELIX   60  60 GLN H   25  GLY H   47  1                                  23
HELIX   61  61 ASP H   49  VAL H   52  5                                   4
HELIX   62  62 CYS H   53  CYS H   64  1                                  12
HELIX   63  63 PRO H   65  GLY H   79  1                                  15
HELIX   64  64 GLY I   11  VAL I   39  1                                  29
HELIX   65  65 VAL I   39  ASN I   53  1                                  15
HELIX   66  66 ASP I   55  ALA I   66  1                                  12
HELIX   67  67 ARG J    4  GLU J   14  1                                  11
HELIX   68  68 GLY J   25  SER J   54  1                                  30
HELIX   69  69 ASP K    8  ILE K   36  1                                  29
HELIX   70  70 ASN L   17  LEU L   45  1                                  29
HELIX   71  71 SER M   11  HIS M   36  1                                  26
HELIX   72  72 HIS M   36  LYS M   42  1                                   7
HELIX   73  73 FME N    1  LEU N    7  1                                   7
HELIX   74  74 ASN N   11  GLY N   42  1                                  32
HELIX   75  75 ASP N   50  PHE N   68  1                                  19
HELIX   76  76 MET N   69  ILE N   75  1                                   7
HELIX   77  77 GLY N   77  ILE N   87  1                                  11
HELIX   78  78 PHE N   94  LEU N  104  1                                  11
HELIX   79  79 LEU N  104  VAL N  118  1                                  15
HELIX   80  80 ALA N  141  MET N  171  1                                  31
HELIX   81  81 SER N  177  THR N  181  5                                   5
HELIX   82  82 PRO N  182  LEU N  215  1                                  34
HELIX   83  83 ASP N  221  GLY N  225  5                                   5
HELIX   84  84 ASP N  227  SER N  262  1                                  36
HELIX   85  85 GLY N  269  GLY N  284  1                                  16
HELIX   86  86 PHE N  285  ILE N  286  5                                   2
HELIX   87  87 VAL N  287  MET N  292  5                                   6
HELIX   88  88 ASP N  298  ILE N  312  1                                  15
HELIX   89  89 ILE N  312  HIS N  328  1                                  17
HELIX   90  90 SER N  335  ALA N  359  1                                  25
HELIX   91  91 ASN N  360  HIS N  368  1                                   9
HELIX   92  92 THR N  370  SER N  382  1                                  13
HELIX   93  93 MET N  383  GLY N  402  1                                  20
HELIX   94  94 ASN N  406  PHE N  426  1                                  21
HELIX   95  95 PHE N  426  SER N  434  1                                   9
HELIX   96  96 PRO N  444  ALA N  446  5                                   3
HELIX   97  97 TYR N  447  LYS N  479  1                                  33
HELIX   98  98 LEU N  487  LEU N  495  5                                   9
HELIX   99  99 SER O   14  THR O   47  1                                  34
HELIX  100 100 GLU O   60  GLU O   89  1                                  30
HELIX  101 101 PRO O  124  LEU O  128  5                                   5
HELIX  102 102 PRO O  166  GLY O  169  5                                   4
HELIX  103 103 ASN O  203  MET O  207  5                                   5
HELIX  104 104 PRO O  215  MET O  226  1                                  12
HELIX  105 105 PRO P   15  ASN P   38  1                                  24
HELIX  106 106 MET P   40  THR P   66  1                                  27
HELIX  107 107 THR P   72  ALA P  107  1                                  36
HELIX  108 108 THR P  109  GLY P  113  5                                   5
HELIX  109 109 GLU P  128  GLU P  153  1                                  26
HELIX  110 110 ASP P  155  ALA P  184  1                                  30
HELIX  111 111 ASP P  190  LYS P  224  1                                  35
HELIX  112 112 HIS P  232  ILE P  256  1                                  25
HELIX  113 113 LYS Q    7  TYR Q   11  5                                   5
HELIX  114 114 SER Q   34  GLU Q   44  1                                  11
HELIX  115 115 LYS Q   45  ALA Q   46  5                                   2
HELIX  116 116 SER Q   47  LEU Q   51  5                                   5
HELIX  117 117 SER Q   52  PHE Q   64  1                                  13
HELIX  118 118 SER Q   67  ASN Q   72  1                                   6
HELIX  119 119 ASN Q   76  VAL Q  103  1                                  28
HELIX  120 120 PRO Q  108  PHE Q  111  5                                   4
HELIX  121 121 GLU Q  112  MET Q  126  1                                  15
HELIX  122 122 PHE Q  134  ALA Q  136  5                                   3
HELIX  123 123 THR R    7  ASN R   20  1                                  14
HELIX  124 124 ASP R   25  VAL R   37  1                                  13
HELIX  125 125 GLU R   44  LEU R   58  1                                  15
HELIX  126 126 ASP R   60  ALA R   75  1                                  16
HELIX  127 127 GLU R   80  GLY R   97  1                                  18
HELIX  128 128 THR S    8  ALA S   13  1                                   6
HELIX  129 129 THR S   14  LYS S   26  1                                  13
HELIX  130 130 GLY T   12  LEU T   23  1                                  12
HELIX  131 131 LEU T   23  TRP T   36  1                                  14
HELIX  132 132 GLN U   25  GLY U   47  1                                  23
HELIX  133 133 ASP U   49  VAL U   52  5                                   4
HELIX  134 134 CYS U   53  CYS U   64  1                                  12
HELIX  135 135 PRO U   65  GLY U   79  1                                  15
HELIX  136 136 GLY V   11  VAL V   39  1                                  29
HELIX  137 137 VAL V   39  ASN V   53  1                                  15
HELIX  138 138 ASP V   55  ALA V   66  1                                  12
HELIX  139 139 ARG W    4  GLU W   14  1                                  11
HELIX  140 140 GLY W   25  SER W   54  1                                  30
HELIX  141 141 ASP X    8  ILE X   36  1                                  29
HELIX  142 142 ASN Y   17  LEU Y   45  1                                  29
HELIX  143 143 SER Z   11  HIS Z   36  1                                  26
HELIX  144 144 HIS Z   36  LYS Z   42  1                                   7
SHEET    1   A 3 TYR A 510  VAL A 511  0
SHEET    2   A 3 LYS F  55  CYS F  60  1  O  GLY F  59   N  TYR A 510
SHEET    3   A 3 ILE F  70  HIS F  75 -1  O  PHE F  72   N  VAL F  58
SHEET    1   B 5 LEU B 116  SER B 120  0
SHEET    2   B 5 TYR B 105  TYR B 110 -1  N  TYR B 110   O  LEU B 116
SHEET    3   B 5 LEU B  95  HIS B 102 -1  N  LYS B  98   O  GLU B 109
SHEET    4   B 5 ILE B 150  SER B 156  1  O  ARG B 151   N  LEU B  95
SHEET    5   B 5 ASN B 180  LEU B 184 -1  O  ASN B 180   N  VAL B 154
SHEET    1   C 3 VAL B 142  PRO B 145  0
SHEET    2   C 3 ILE B 209  VAL B 214  1  O  GLU B 212   N  LEU B 144
SHEET    3   C 3 GLY B 190  GLY B 194 -1  N  TYR B 192   O  LEU B 211
SHEET    1   D 2 HIS B 161  VAL B 165  0
SHEET    2   D 2 LEU B 170  ALA B 174 -1  O  ALA B 174   N  HIS B 161
SHEET    1   E 2 TRP D 138  ASP D 139  0
SHEET    2   E 2 GLU D 144  TRP D 145 -1  O  GLU D 144   N  ASP D 139
SHEET    1   F 3 ASN F  47  PRO F  50  0
SHEET    2   F 3 HIS F  88  VAL F  92  1  O  LYS F  90   N  VAL F  49
SHEET    3   F 3 GLN F  80  ARG F  81 -1  N  GLN F  80   O  TYR F  89
SHEET    1   G 2 VAL N 482  THR N 484  0
SHEET    2   G 2 THR Z   2  ALA Z   3 -1  O  THR Z   2   N  THR N 484
SHEET    1   H 3 TYR N 510  VAL N 511  0
SHEET    2   H 3 LYS S  55  CYS S  60  1  O  ILE S  57   N  TYR N 510
SHEET    3   H 3 ILE S  70  HIS S  75 -1  O  PHE S  72   N  VAL S  58
SHEET    1   I 5 LEU O 116  SER O 120  0
SHEET    2   I 5 TYR O 105  TYR O 110 -1  N  TYR O 108   O  PHE O 118
SHEET    3   I 5 LEU O  95  HIS O 102 -1  N  LYS O  98   O  GLU O 109
SHEET    4   I 5 ILE O 150  SER O 156  1  O  ARG O 151   N  LEU O  95
SHEET    5   I 5 ASN O 180  LEU O 184 -1  O  ASN O 180   N  VAL O 154
SHEET    1   J 3 VAL O 142  PRO O 145  0
SHEET    2   J 3 ILE O 209  VAL O 214  1  O  GLU O 212   N  LEU O 144
SHEET    3   J 3 GLY O 190  GLY O 194 -1  N  TYR O 192   O  LEU O 211
SHEET    1   K 2 HIS O 161  VAL O 165  0
SHEET    2   K 2 LEU O 170  ALA O 174 -1  O  ALA O 174   N  HIS O 161
SHEET    1   L 2 TRP Q 138  ASP Q 139  0
SHEET    2   L 2 GLU Q 144  TRP Q 145 -1  O  GLU Q 144   N  ASP Q 139
SHEET    1   M 3 ASN S  47  PRO S  50  0
SHEET    2   M 3 HIS S  88  VAL S  92  1  O  LYS S  90   N  VAL S  49
SHEET    3   M 3 GLN S  80  ARG S  81 -1  N  GLN S  80   O  TYR S  89
SSBOND   1 CYS H   29    CYS H   64                          1555   1555  2.05
SSBOND   2 CYS H   39    CYS H   53                          1555   1555  2.06
SSBOND   3 CYS U   29    CYS U   64                          1555   1555  2.05
SSBOND   4 CYS U   39    CYS U   53                          1555   1555  2.05
LINK         C   FME A   1                 N   PHE A   2     1555   1555  1.33
LINK         C   FME B   1                 N   ALA B   2     1555   1555  1.33
LINK         C   GLY G  10                 N   TPO G  11     1555   1555  1.33
LINK         C   TPO G  11                 N   GLY G  12     1555   1555  1.35
LINK         C   SAC I   1                 N   THR I   2     1555   1555  1.33
LINK         C   FME N   1                 N   PHE N   2     1555   1555  1.33
LINK         C   FME O   1                 N   ALA O   2     1555   1555  1.33
LINK         C   GLY T  10                 N   TPO T  11     1555   1555  1.33
LINK         C   TPO T  11                 N   GLY T  12     1555   1555  1.35
LINK         C   SAC V   1                 N   THR V   2     1555   1555  1.34
LINK         O   GLU A  40                NA    NA A3519     1555   1555  2.40
LINK         OE1 GLU A  40                NA    NA A3519     1555   1555  2.47
LINK         O   GLY A  45                NA    NA A3519     1555   1555  2.37
LINK         NE2 HIS A  61                FE   HEA A 515     1555   1555  1.97
LINK         ND1 HIS A 240                CU    CU A 517     1555   1555  2.02
LINK         NE2 HIS A 290                CU    CU A 517     1555   1555  2.02
LINK         NE2 HIS A 291                CU    CU A 517     1555   1555  1.96
LINK         NE2 HIS A 368                MG    MG A3518     1555   1555  2.21
LINK         OD1 ASP A 369                MG    MG A3518     1555   1555  2.05
LINK         NE2 HIS A 376                FE   HEA A 516     1555   1555  2.04
LINK         NE2 HIS A 378                FE   HEA A 515     1555   1555  1.96
LINK         O   SER A 441                NA    NA A3519     1555   1555  2.39
LINK         ND1 HIS B 161                CU1  CUA B 228     1555   1555  2.02
LINK         OE1 GLU B 198                MG    MG A3518     1555   1555  2.08
LINK         ND1 HIS B 204                CU2  CUA B 228     1555   1555  2.02
LINK         SG  CYS F  60                ZN    ZN F  99     1555   1555  2.26
LINK         SG  CYS F  62                ZN    ZN F  99     1555   1555  2.24
LINK         SG  CYS F  82                ZN    ZN F  99     1555   1555  2.22
LINK         SG  CYS F  85                ZN    ZN F  99     1555   1555  2.29
LINK         O   GLU N  40                NA    NA N4519     1555   1555  2.38
LINK         OE1 GLU N  40                NA    NA N4519     1555   1555  2.45
LINK         O   GLY N  45                NA    NA N4519     1555   1555  2.35
LINK         NE2 HIS N  61                FE   HEA N 515     1555   1555  1.96
LINK         ND1 HIS N 240                CU    CU N 517     1555   1555  2.00
LINK         NE2 HIS N 290                CU    CU N 517     1555   1555  1.99
LINK         NE2 HIS N 291                CU    CU N 517     1555   1555  1.98
LINK         NE2 HIS N 368                MG    MG N4518     1555   1555  2.18
LINK         OD1 ASP N 369                MG    MG N4518     1555   1555  2.08
LINK         NE2 HIS N 376                FE   HEA N 516     1555   1555  2.15
LINK         NE2 HIS N 378                FE   HEA N 515     1555   1555  2.01
LINK         O   SER N 441                NA    NA N4519     1555   1555  2.37
LINK         ND1 HIS O 161                CU1  CUA O 228     1555   1555  2.03
LINK         OE1 GLU O 198                MG    MG N4518     1555   1555  2.05
LINK         ND1 HIS O 204                CU2  CUA O 228     1555   1555  2.04
LINK         SG  CYS S  60                ZN    ZN S  99     1555   1555  2.27
LINK         SG  CYS S  62                ZN    ZN S  99     1555   1555  2.27
LINK         SG  CYS S  82                ZN    ZN S  99     1555   1555  2.22
LINK         SG  CYS S  85                ZN    ZN S  99     1555   1555  2.29
LINK        MG    MG A3518                 O   HOH B4093     1555   1555  2.31
LINK        MG    MG A3518                 O   HOH B4091     1555   1555  2.33
LINK        MG    MG A3518                 O   HOH B4092     1555   1555  2.31
LINK        NA    NA A3519                 O   HOH A3544     1555   1555  2.02
LINK        MG    MG N4518                 O   HOH O1033     1555   1555  2.33
LINK        MG    MG N4518                 O   HOH O1032     1555   1555  2.34
LINK        MG    MG N4518                 O   HOH O1031     1555   1555  2.33
LINK        NA    NA N4519                 O   HOH N1026     1555   1555  2.03
LINK         NE2 HIS A 240                 CE2 TYR A 244     1555   1555  1.37
LINK         NE2 HIS N 240                 CE2 TYR N 244     1555   1555  1.36
CISPEP   1 PRO A  130    PRO A  131          0         2.43
CISPEP   2 CYS A  498    PRO A  499          0        -0.13
CISPEP   3 TRP C  116    PRO C  117          0        -0.34
CISPEP   4 PRO N  130    PRO N  131          0        -2.23
CISPEP   5 CYS N  498    PRO N  499          0        -0.56
CISPEP   6 TRP P  116    PRO P  117          0        -0.43
SITE     1 AC1  3 HIS A 240  HIS A 290  HIS A 291
SITE     1 AC2  6 HIS A 368  ASP A 369  GLU B 198  HOH B4091
SITE     2 AC2  6 HOH B4092  HOH B4093
SITE     1 AC3  4 GLU A  40  GLY A  45  SER A 441  HOH A3544
SITE     1 AC4 27 GLY A  27  MET A  28  THR A  31  SER A  34
SITE     2 AC4 27 ILE A  37  ARG A  38  TYR A  54  VAL A  58
SITE     3 AC4 27 HIS A  61  ALA A  62  MET A  65  VAL A  70
SITE     4 AC4 27 GLY A 125  TRP A 126  TYR A 371  PHE A 377
SITE     5 AC4 27 HIS A 378  SER A 382  VAL A 386  PHE A 425
SITE     6 AC4 27 GLN A 428  ARG A 438  ARG A 439  MET A 468
SITE     7 AC4 27 HOH A3528  HOH A3548  HOH A3555
SITE     1 AC5 27 TRP A 126  TRP A 236  VAL A 243  TYR A 244
SITE     2 AC5 27 HIS A 290  HIS A 291  THR A 316  GLY A 317
SITE     3 AC5 27 GLY A 352  GLY A 355  ILE A 356  LEU A 358
SITE     4 AC5 27 ALA A 359  ASP A 364  HIS A 368  VAL A 373
SITE     5 AC5 27 HIS A 376  PHE A 377  VAL A 380  LEU A 381
SITE     6 AC5 27 ARG A 438  HOH A3529  HOH A3536  HOH A3546
SITE     7 AC5 27 HOH A3554  PRO B  69  ILE B  72
SITE     1 AC6 16 VAL A 350  ASN A 422  PHE A 426  PHE A 430
SITE     2 AC6 16 LEU A 433  HOH A3717  HOH A3749  LEU B   7
SITE     3 AC6 16 GLY B   8  LEU B  28  VAL B  31  PHE B  32
SITE     4 AC6 16 SER B  35  LEU B  39  ARG I  43  HOH I 363
SITE     1 AC7 16 PHE A  94  PRO A  95  ARG A  96  MET A  97
SITE     2 AC7 16 MET A 100  HOH A3595  HOH A3616  HIS C   9
SITE     3 AC7 16 ASN C  50  MET C  54  TRP C  57  TRP C  58
SITE     4 AC7 16 GLU C  64  HIS C  71  LEU C  79  GLY C  82
SITE     1 AC8 16 ASN A 406  THR A 408  TRP A 409  HOH A3745
SITE     2 AC8 16 HOH A3746  HOH A3747  PHE D  87  PHE K   9
SITE     3 AC8 16 HIS K  10  HOH K  77  GLN M  15  ALA M  16
SITE     4 AC8 16 LEU M  19  SER M  20  HOH M 749  HOH M2659
SITE     1 AC9  6 HIS B 161  CYS B 196  GLU B 198  CYS B 200
SITE     2 AC9  6 HIS B 204  MET B 207
SITE     1 BC1 12 MET A 271  GLN B  59  GLU B  62  THR B  63
SITE     2 BC1 12 HOH B4147  HOH B4156  PEK P4265  ARG T  14
SITE     3 BC1 12 ARG T  17  PHE T  18  GLY T  22  HOH T1289
SITE     1 BC2  8 HIS A 233  ASP A 300  THR A 301  TYR A 304
SITE     2 BC2  8 HOH A3684  TRP C  99  HIS C 103  HOH C3634
SITE     1 BC3  6 ARG C 156  GLN C 161  PHE C 164  LEU C 223
SITE     2 BC3  6 HOH C3640  PHE J   1
SITE     1 BC4 15 MET C  51  MET C  54  TYR C  55  TRP C  58
SITE     2 BC4 15 ARG C  59  ARG C  63  PHE C  67  THR C 213
SITE     3 BC4 15 ILE C 216  LYS C 224  HIS C 226  PGV C3267
SITE     4 BC4 15 HOH C3613  HOH C3618  LYS J   8
SITE     1 BC5 16 HIS A 151  TYR C 181  TYR C 182  ALA C 184
SITE     2 BC5 16 PHE C 186  THR C 187  ILE C 188  PHE C 198
SITE     3 BC5 16 GLY C 202  TRP G  62  THR G  68  PHE G  69
SITE     4 BC5 16 PHE G  70  HIS G  71  ASN G  76  HOH G 241
SITE     1 BC6 13 LYS C 157  HIS C 158  LEU C 169  TYR C 172
SITE     2 BC6 13 ALA F   1  ARG G  17  PHE G  21  CDL G3269
SITE     3 BC6 13 TRP N 275  SER N 279  GLN O  59  THR O  66
SITE     4 BC6 13 CHD O3085
SITE     1 BC7 21 MET C  54  TRP C  58  VAL C  61  SER C  65
SITE     2 BC7 21 THR C  66  HIS C 207  ILE C 210  THR C 213
SITE     3 BC7 21 PHE C 214  ARG C 221  HIS C 226  PHE C 227
SITE     4 BC7 21 THR C 228  HIS C 231  HIS C 232  PHE C 233
SITE     5 BC7 21 GLY C 234  CDL C3270  HOH C3532  HOH C3555
SITE     6 BC7 21 HOH C3570
SITE     1 BC8  7 ASP A 298  HOH A3680  TRP C  99  TYR C 102
SITE     2 BC8  7 HIS C 103  HOH C3617  HOH H2096
SITE     1 BC9  3 HIS C 148  HIS C 232  GLU C 236
SITE     1 CC1 18 TRP A 334  MET A 339  LEU A 342  GLY A 343
SITE     2 CC1 18 PHE A 414  ILE B  42  THR B  47  HOH B4144
SITE     3 CC1 18 HOH B4247  HOH B4263  ARG D  73  SER D  74
SITE     4 CC1 18 GLU D  77  TRP D  78  VAL D  81  ILE D  89
SITE     5 CC1 18 HOH D3588  HOH D3613
SITE     1 CC2 15 PHE A 321  HOH A3721  ILE B  41  HIS B  52
SITE     2 CC2 15 MET B  56  ASP B  57  VAL B  61  TRP B  65
SITE     3 CC2 15 HIS E   5  ASP E   8  PHE E  11  LEU E  41
SITE     4 CC2 15 HOH E3243  ARG I  10  ALA I  14
SITE     1 CC3  4 CYS F  60  CYS F  62  CYS F  82  CYS F  85
SITE     1 CC4 23 LEU C 127  LEU C 131  SER C 135  TYR C 253
SITE     2 CC4 23 VAL C 254  PEK C3265  LEU G  23  SER G  27
SITE     3 CC4 23 LEU G  30  CYS G  31  ASN G  34  LEU G  37
SITE     4 CC4 23 HIS G  38  PHE N 282  ILE N 286  ASP N 300
SITE     5 CC4 23 TYR N 304  SER N 307  ILE N 311  ALA O  77
SITE     6 CC4 23 LEU O  78  LEU O  81  TYR O  85
SITE     1 CC5 16 SER G   2  ALA G   3  LYS G   5  GLY G   6
SITE     2 CC5 16 HIS G   8  TPO G  11  LYS P  77  ARG P  80
SITE     3 CC5 16 TYR P  81  ILE P  84  THR P  95  PHE P  98
SITE     4 CC5 16 TRP P 240  PHE P 244  VAL P 247  VAL P 248
SITE     1 CC6  5 TYR J  32  ARG J  33  MET J  36  THR J  37
SITE     2 CC6  5 LEU J  40
SITE     1 CC7 16 PHE A   2  THR A  17  LEU A  21  PHE A  22
SITE     2 CC7 16 TRP A  81  LEU A 113  PHE A 400  ILE A 472
SITE     3 CC7 16 ASN L  10  ILE L  11  PRO L  12  PHE L  13
SITE     4 CC7 16 SER L  14  ARG L  20  MET L  24  HOH L2432
SITE     1 CC8  8 TRP D  98  LEU M  27  LEU M  28  GLY M  31
SITE     2 CC8  8 TRP M  32  TYR M  35  HIS M  36  HOH M2052
SITE     1 CC9  3 HIS N 240  HIS N 290  HIS N 291
SITE     1 DC1  6 HIS N 368  ASP N 369  GLU O 198  HOH O1031
SITE     2 DC1  6 HOH O1032  HOH O1033
SITE     1 DC2  4 GLU N  40  GLY N  45  SER N 441  HOH N1026
SITE     1 DC3 28 GLY N  27  MET N  28  THR N  31  SER N  34
SITE     2 DC3 28 ILE N  37  ARG N  38  TYR N  54  VAL N  58
SITE     3 DC3 28 HIS N  61  ALA N  62  MET N  65  VAL N  70
SITE     4 DC3 28 GLY N 125  TRP N 126  TYR N 371  PHE N 377
SITE     5 DC3 28 HIS N 378  SER N 382  VAL N 386  PHE N 393
SITE     6 DC3 28 PHE N 425  GLN N 428  ARG N 438  ARG N 439
SITE     7 DC3 28 MET N 468  HOH N1005  HOH N1036  HOH N1045
SITE     1 DC4 30 TRP N 126  TRP N 236  VAL N 243  TYR N 244
SITE     2 DC4 30 HIS N 290  HIS N 291  THR N 309  ALA N 313
SITE     3 DC4 30 THR N 316  GLY N 317  GLY N 352  GLY N 355
SITE     4 DC4 30 ILE N 356  LEU N 358  ALA N 359  ASP N 364
SITE     5 DC4 30 HIS N 368  VAL N 373  HIS N 376  PHE N 377
SITE     6 DC4 30 VAL N 380  LEU N 381  ARG N 438  HOH N1007
SITE     7 DC4 30 HOH N1016  HOH N1034  HOH N1044  ILE O  34
SITE     8 DC4 30 PRO O  69  LEU O  73
SITE     1 DC5 18 VAL N 350  ASN N 422  PHE N 426  HIS N 429
SITE     2 DC5 18 PHE N 430  LEU N 433  HOH N1521  HOH N2290
SITE     3 DC5 18 HOH N2537  GLY O   8  LEU O  28  VAL O  31
SITE     4 DC5 18 PHE O  32  SER O  35  LEU O  39  HOH O1488
SITE     5 DC5 18 HOH Q1363  ARG V  43
SITE     1 DC6 18 THR N  17  LEU N  20  LEU N  21  PHE N  22
SITE     2 DC6 18 TRP N  81  LEU N 113  PHE N 400  ILE N 472
SITE     3 DC6 18 ASN Y  10  ILE Y  11  PRO Y  12  PHE Y  13
SITE     4 DC6 18 SER Y  14  ARG Y  20  MET Y  24  PHE Y  28
SITE     5 DC6 18 SER Y  31  HOH Y2236
SITE     1 DC7 16 PHE N  94  PRO N  95  ARG N  96  MET N  97
SITE     2 DC7 16 HOH N1125  HOH N1213  HIS P   9  ASN P  50
SITE     3 DC7 16 MET P  54  TRP P  57  TRP P  58  GLU P  64
SITE     4 DC7 16 HIS P  71  LEU P  79  GLY P  82  SER P  89
SITE     1 DC8  9 ASN N 406  THR N 408  TRP N 409  PHE Q  87
SITE     2 DC8  9 GLN Z  15  ALA Z  16  LEU Z  19  SER Z  20
SITE     3 DC8  9 HOH Z2517
SITE     1 DC9 13 PEK C3265  ARG G  14  ARG G  17  PHE G  21
SITE     2 DC9 13 GLY G  22  HOH G 289  MET N 271  GLN O  59
SITE     3 DC9 13 GLU O  62  THR O  63  HOH O1362  HOH O2101
SITE     4 DC9 13 HOH O2313
SITE     1 EC1 14 PHE N 321  HOH N1561  ILE O  41  HIS O  52
SITE     2 EC1 14 MET O  56  ASP O  57  VAL O  61  TRP O  65
SITE     3 EC1 14 LEU O  68  HIS R   5  GLU R   6  ASP R   8
SITE     4 EC1 14 PHE R  11  ARG V  10
SITE     1 EC2  6 HIS O 161  CYS O 196  GLU O 198  CYS O 200
SITE     2 EC2  6 HIS O 204  MET O 207
SITE     1 EC3  6 HIS N 233  ASP N 300  THR N 301  TYR N 304
SITE     2 EC3  6 TRP P  99  HIS P 103
SITE     1 EC4  5 ARG P 156  PHE P 164  LEU P 223  HOH P2546
SITE     2 EC4  5 PHE W   1
SITE     1 EC5 14 MET P  51  MET P  54  TYR P  55  TRP P  58
SITE     2 EC5 14 ARG P  59  ARG P  63  PHE P  67  THR P 213
SITE     3 EC5 14 ILE P 216  LYS P 224  HIS P 226  HOH P2180
SITE     4 EC5 14 HOH P2406  PGV P4267
SITE     1 EC6 16 HIS N 151  TYR P 181  TYR P 182  ALA P 184
SITE     2 EC6 16 PHE P 186  THR P 187  ILE P 188  PHE P 198
SITE     3 EC6 16 GLY P 202  HOH P2487  TRP T  62  THR T  68
SITE     4 EC6 16 PHE T  69  PHE T  70  HIS T  71  ASN T  76
SITE     1 EC7 16 TRP A 275  SER A 279  GLN B  59  THR B  66
SITE     2 EC7 16 CHD B4085  HOH B4241  LYS P 157  HIS P 158
SITE     3 EC7 16 LEU P 169  TYR P 172  ALA S   1  ARG T  17
SITE     4 EC7 16 PHE T  21  GLY T  22  HOH T2507  CDL T4269
SITE     1 EC8 19 TRP P  58  VAL P  61  SER P  65  THR P  66
SITE     2 EC8 19 HIS P 207  ILE P 210  THR P 213  PHE P 214
SITE     3 EC8 19 ARG P 221  HIS P 226  PHE P 227  THR P 228
SITE     4 EC8 19 HIS P 231  HIS P 232  PHE P 233  GLY P 234
SITE     5 EC8 19 HOH P1117  HOH P1201  CDL P4270
SITE     1 EC9  8 ASP N 298  TRP P  99  TYR P 102  HIS P 103
SITE     2 EC9  8 HOH P2124  HOH P2168  HOH P2446  HOH U1487
SITE     1 FC1  3 HIS P 148  HIS P 232  GLU P 236
SITE     1 FC2 16 TRP N 334  MET N 339  GLY N 343  PHE N 414
SITE     2 FC2 16 HOH N2197  ILE O  42  THR O  47  LYS O  49
SITE     3 FC2 16 HOH O2513  ARG Q  73  SER Q  74  GLU Q  77
SITE     4 FC2 16 TRP Q  78  VAL Q  81  ILE Q  89  HOH Q1562
SITE     1 FC3  4 CYS S  60  CYS S  62  CYS S  82  CYS S  85
SITE     1 FC4 16 LYS C  77  ARG C  80  TYR C  81  ILE C  84
SITE     2 FC4 16 THR C  95  PHE C  98  TRP C 240  PHE C 244
SITE     3 FC4 16 VAL C 247  SER T   2  ALA T   3  LYS T   5
SITE     4 FC4 16 GLY T   6  HIS T   8  HOH T2281  HOH T2308
SITE     1 FC5 28 PHE A 282  ASP A 300  TYR A 304  SER A 307
SITE     2 FC5 28 ILE A 311  ILE B  74  ALA B  77  LEU B  78
SITE     3 FC5 28 LEU B  81  TYR B  85  HOH C3634  LEU P 127
SITE     4 FC5 28 LEU P 131  SER P 135  LEU P 250  TYR P 253
SITE     5 FC5 28 VAL P 254  PEK P4265  LEU T  23  SER T  27
SITE     6 FC5 28 LEU T  30  CYS T  31  LEU T  33  ASN T  34
SITE     7 FC5 28 LEU T  37  HIS T  38  HOH T2312  HOH T2558
SITE     1 FC6  4 LEU N   7  TYR W  32  ARG W  33  MET W  36
SITE     1 FC7  9 PHE N 459  TRP Q  98  LEU Z  27  LEU Z  28
SITE     2 FC7  9 GLY Z  31  TRP Z  32  TYR Z  35  HIS Z  36
SITE     3 FC7  9 HOH Z2220
CRYST1  182.590  205.140  178.250  90.00  90.00  90.00 P 21 21 21    8
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      0.005477  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004875  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005610        0.00000
      
PROCHECK
Go to PROCHECK summary
 References