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PDBsum entry 2eim

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Top Page protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
2eim
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
PGV ×8
CHD ×8
CUA ×2
TGL ×6
PSC ×2
DMU ×4
PEK ×6
CDL ×4
Metals
_ZN ×6
_CU ×2
_MG ×2
_NA ×2
Waters ×1227
HEADER    OXIDOREDUCTASE                          13-MAR-07   2EIM
TITLE     ZINC ION BINDING STRUCTURE OF BOVINE HEART CYTOCHROME C OXIDASE IN THE
TITLE    2 FULLY REDUCED STATE
CAVEAT     2EIM    THERE ARE SEVERAL CHIRALITY ERRORS IN CHD.
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 1;
COMPND   3 CHAIN: A, N;
COMPND   4 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE I;
COMPND   5 EC: 1.9.3.1;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 2;
COMPND   8 CHAIN: B, O;
COMPND   9 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE II;
COMPND  10 EC: 1.9.3.1;
COMPND  11 MOL_ID: 3;
COMPND  12 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 3;
COMPND  13 CHAIN: C, P;
COMPND  14 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE III;
COMPND  15 EC: 1.9.3.1;
COMPND  16 MOL_ID: 4;
COMPND  17 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 4 ISOFORM 1;
COMPND  18 CHAIN: D, Q;
COMPND  19 SYNONYM: CYTOCHROME C OXIDASE SUBUNIT IV ISOFORM 1, COX IV-1,
COMPND  20 CYTOCHROME C OXIDASE POLYPEPTIDE IV;
COMPND  21 EC: 1.9.3.1;
COMPND  22 MOL_ID: 5;
COMPND  23 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VA;
COMPND  24 CHAIN: E, R;
COMPND  25 EC: 1.9.3.1;
COMPND  26 MOL_ID: 6;
COMPND  27 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VB;
COMPND  28 CHAIN: F, S;
COMPND  29 SYNONYM: VI;
COMPND  30 EC: 1.9.3.1;
COMPND  31 MOL_ID: 7;
COMPND  32 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIA-HEART;
COMPND  33 CHAIN: G, T;
COMPND  34 SYNONYM: COXVIAH, POLYPEPTIDE VIB;
COMPND  35 EC: 1.9.3.1;
COMPND  36 MOL_ID: 8;
COMPND  37 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT VIB ISOFORM 1;
COMPND  38 CHAIN: H, U;
COMPND  39 SYNONYM: COX VIB-1, CYTOCHROME C OXIDASE POLYPEPTIDE VII, CYTOCHROME
COMPND  40 C OXIDASE SUBUNIT AED;
COMPND  41 EC: 1.9.3.1;
COMPND  42 MOL_ID: 9;
COMPND  43 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIC;
COMPND  44 CHAIN: I, V;
COMPND  45 SYNONYM: STA;
COMPND  46 EC: 1.9.3.1;
COMPND  47 MOL_ID: 10;
COMPND  48 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA-HEART;
COMPND  49 CHAIN: J, W;
COMPND  50 SYNONYM: CYTOCHROME C OXIDASE SUBUNIT VIIA-H, COX VIIA-M, VIIIC;
COMPND  51 EC: 1.9.3.1;
COMPND  52 MOL_ID: 11;
COMPND  53 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIIB;
COMPND  54 CHAIN: K, X;
COMPND  55 SYNONYM: IHQ;
COMPND  56 EC: 1.9.3.1;
COMPND  57 MOL_ID: 12;
COMPND  58 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIIC;
COMPND  59 CHAIN: L, Y;
COMPND  60 SYNONYM: VIIIA;
COMPND  61 EC: 1.9.3.1;
COMPND  62 MOL_ID: 13;
COMPND  63 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE VIII-HEART;
COMPND  64 CHAIN: M, Z;
COMPND  65 SYNONYM: CYTOCHROME C OXIDASE SUBUNIT 8-1, VIIIB, IX;
COMPND  66 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    K.MURAMOTO,K.HIRATA,K.SHINZAWA-ITOH,S.YOKO-O,E.YAMASHITA,H.AOYAMA,
AUTHOR   2 T.TSUKIHARA,S.YOSHIKAWA
REVDAT   3   13-JUL-11 2EIM    1       VERSN
REVDAT   2   24-FEB-09 2EIM    1       VERSN
REVDAT   1   29-MAY-07 2EIM    0
JRNL        AUTH   K.MURAMOTO,K.HIRATA,K.SHINZAWA-ITOH,S.YOKO-O,E.YAMASHITA,
JRNL        AUTH 2 H.AOYAMA,T.TSUKIHARA,S.YOSHIKAWA
JRNL        TITL   A HISTIDINE RESIDUE ACTING AS A CONTROLLING SITE FOR
JRNL        TITL 2 DIOXYGEN REDUCTION AND PROTON PUMPING BY CYTOCHROME C
JRNL        TITL 3 OXIDASE
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 104  7881 2007
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   17470809
JRNL        DOI    10.1073/PNAS.0610031104
REMARK   2
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : X-PLOR 3.851
REMARK   3   AUTHORS     : BRUNGER
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
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             : 189097
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) : 0.204
REMARK   3   FREE R VALUE                     : 0.256
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          : 2228
REMARK   3   SOLVENT ATOMS            : 1227
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: NULL
REMARK   4
REMARK   4 2EIM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-MAR-07.
REMARK 100 THE RCSB ID CODE IS RCSB026709.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-00
REMARK 200  TEMPERATURE           (KELVIN) : 100
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) : 0.9
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   : 189149
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 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: 1V55
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 70.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.13
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       91.95450
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       89.16850
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      103.36050
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       89.16850
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       91.95450
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      103.36050
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: 174500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 110320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1545.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, M, C, Z, P, F, N, S, B,
REMARK 350                    AND CHAINS: D, O, E, G, L, H, I, J, K,
REMARK 350                    AND CHAINS: T, Q, R, U, V, W, X, Y
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE
REMARK 500   NE2  HIS N   240     CD2  TYR N   244              2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    LEU B 128   CA  -  CB  -  CG  ANGL. DEV. =  13.9 DEGREES
REMARK 500    HIS F  94   N   -  CA  -  C   ANGL. DEV. =  17.4 DEGREES
REMARK 500    HIS S  94   N   -  CA  -  C   ANGL. DEV. =  18.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    THR A  10       17.53   -149.77
REMARK 500    ASP A  91     -172.51   -176.58
REMARK 500    GLU A 119     -129.15     52.25
REMARK 500    SER A 142      -58.59    -29.36
REMARK 500    HIS A 290        0.79    -65.76
REMARK 500    HIS A 328      107.27    -59.23
REMARK 500    TYR A 371        1.53    -67.89
REMARK 500    LEU A 487       26.60     48.56
REMARK 500    HIS B  52       95.03   -162.24
REMARK 500    GLN B  59       64.12    -61.75
REMARK 500    GLU B  60      -53.46   -170.68
REMARK 500    TRP B  65       27.37    -79.13
REMARK 500    ASN B  92       90.28     48.79
REMARK 500    SER B 117      147.79   -170.06
REMARK 500    PRO B 130      121.39    -37.62
REMARK 500    LEU B 135      -11.45     69.64
REMARK 500    ASP B 158     -111.86   -152.24
REMARK 500    VAL B 159     -162.28    -78.99
REMARK 500    LYS B 171      110.66   -172.14
REMARK 500    MET B 185      103.00   -169.40
REMARK 500    ASN C  38       76.97     32.98
REMARK 500    SER C  65      -65.65    -93.60
REMARK 500    PRO C 118      155.74    -49.66
REMARK 500    GLU C 128     -113.49   -105.42
REMARK 500    HIS C 232       61.21   -155.11
REMARK 500    TRP C 258      -72.36    -96.20
REMARK 500    GLN D 132      -47.04   -143.99
REMARK 500    LEU E  41      155.96    177.96
REMARK 500    LYS E  74       -8.86    -54.32
REMARK 500    THR F  39     -156.11    -87.21
REMARK 500    LYS F  55      141.80   -172.12
REMARK 500    ILE F  61       74.16   -105.31
REMARK 500    CYS F  62      -56.06    -29.07
REMARK 500    ASP F  65       -6.04     77.98
REMARK 500    ALA F  79      151.08    -49.52
REMARK 500    VAL F  92       76.93   -118.17
REMARK 500    PRO F  93      169.18    -48.45
REMARK 500    HIS F  94      173.42     47.95
REMARK 500    GLN F  95     -105.18     88.91
REMARK 500    LEU F  96      -75.42     66.92
REMARK 500    ALA G   3      -89.54     87.42
REMARK 500    ALA G   4        1.02    161.59
REMARK 500    LYS G   5     -105.43    -98.42
REMARK 500    ASP G   7     -102.50      4.85
REMARK 500    HIS G   8      -14.36     53.18
REMARK 500    LEU G  23      -62.76   -136.02
REMARK 500    LEU G  37      -54.19   -159.24
REMARK 500    SER G  39     -121.15    -65.79
REMARK 500    GLU G  43      108.79    -49.90
REMARK 500    PRO G  49       49.49    -65.08
REMARK 500
REMARK 500 THIS ENTRY HAS     117 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         0.15    SIDE CHAIN
REMARK 500    TYR A 443         0.08    SIDE CHAIN
REMARK 500    TYR B 218         0.07    SIDE CHAIN
REMARK 500    TYR N  19         0.08    SIDE CHAIN
REMARK 500    HIS N 240         0.16    SIDE CHAIN
REMARK 500    TYR N 244         0.06    SIDE CHAIN
REMARK 500    TYR N 304         0.07    SIDE CHAIN
REMARK 500    TYR N 379         0.07    SIDE CHAIN
REMARK 500    TYR O 192         0.06    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    PRO A 130        45.8      L          L   OUTSIDE RANGE
REMARK 500    TRP B  65        23.8      L          L   OUTSIDE RANGE
REMARK 500    HIS F  94        22.1      L          L   OUTSIDE RANGE
REMARK 500    GLN F  95        19.6      L          L   OUTSIDE RANGE
REMARK 500    ASP G   7        24.3      L          L   OUTSIDE RANGE
REMARK 500    PRO N 130        45.4      L          L   OUTSIDE RANGE
REMARK 500    TRP O  65        23.8      L          L   OUTSIDE RANGE
REMARK 500    PRO S  93        23.9      L          L   OUTSIDE RANGE
REMARK 500    HIS S  94        16.3      L          L   OUTSIDE RANGE
REMARK 500    ASP T   7        23.2      L          L   OUTSIDE RANGE
REMARK 500    HIS T   8        24.6      L          L   OUTSIDE RANGE
REMARK 500    ASP W  15        24.8      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 C4275        DISTANCE =  5.16 ANGSTROMS
REMARK 525    HOH G4244        DISTANCE =  6.39 ANGSTROMS
REMARK 525    HOH J4266        DISTANCE =  5.95 ANGSTROMS
REMARK 525    HOH N4192        DISTANCE =  5.11 ANGSTROMS
REMARK 525    HOH T4004        DISTANCE =  5.14 ANGSTROMS
REMARK 525    HOH T4383        DISTANCE =  6.89 ANGSTROMS
REMARK 525    HOH V4292        DISTANCE =  5.55 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 A 519  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A  40   O
REMARK 620 2 GLU A  40   OE1  90.4
REMARK 620 3 GLY A  45   O   119.6  94.8
REMARK 620 4 SER A 441   O   119.7  83.0 120.8
REMARK 620 5 HOH A2026   O    90.5 175.4  88.6  92.6
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  101.0
REMARK 620 3 HEA A 515   NB   83.6  93.1
REMARK 620 4 HEA A 515   NC   82.1 176.8  87.0
REMARK 620 5 HEA A 515   ND   93.3  90.3 175.7  89.8
REMARK 620 6 HIS A 378   NE2 167.3  87.5  86.6  89.3  96.1
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 107.1
REMARK 620 3 HIS A 291   NE2 149.1  90.6
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A 518  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 368   NE2
REMARK 620 2 ASP A 369   OD1  93.3
REMARK 620 3 GLU B 198   OE1 152.3 111.4
REMARK 620 4 HOH B2033   O    76.0  96.0  88.6
REMARK 620 5 HOH B2031   O    81.4 174.4  74.2  84.5
REMARK 620 6 HOH B2032   O    95.3 101.0  92.3 161.4  77.9
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   98.2
REMARK 620 3 HEA A 516   NB  110.2  93.4
REMARK 620 4 HEA A 516   NC   97.0 162.6  89.3
REMARK 620 5 HEA A 516   ND   83.5  89.1 165.5  84.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A 603  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 503   NE2
REMARK 620 2 HIS L   2   NE2  76.4
REMARK 620 3 HOH A2078   O    96.9 100.0
REMARK 620 4 HOH A2077   O   133.8 148.0  70.3
REMARK 620 N                    1     2     3
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  139.5
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 GLU B 198   O
REMARK 620 2 CUA B 228  CU1  105.7
REMARK 620 3 HIS B 204   ND1  80.8 172.7
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN C 262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 148   NE2
REMARK 620 2 HIS C 232   NE2 108.1
REMARK 620 3 GLU C 236   OE1  89.6  88.6
REMARK 620 4 HOH C2027   O   109.8 101.8 153.3
REMARK 620 N                    1     2     3
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  123.1
REMARK 620 3 CYS F  82   SG  118.7 105.6
REMARK 620 4 CYS F  85   SG  106.0  93.4 105.8
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA N1519  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU N  40   O
REMARK 620 2 GLU N  40   OE1  98.4
REMARK 620 3 GLY N  45   O   117.3  96.4
REMARK 620 4 SER N 441   O   120.8  89.5 119.8
REMARK 620 5 HOH N3026   O    86.8 174.4  79.3  89.5
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   92.2
REMARK 620 3 HEA N 515   NB   76.4  91.2
REMARK 620 4 HEA N 515   NC   87.6 177.2  86.0
REMARK 620 5 HEA N 515   ND  100.3  90.6 176.3  92.2
REMARK 620 6 HIS N 378   NE2 160.9  85.6  84.6  93.8  98.7
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 105.0
REMARK 620 3 HIS N 291   NE2 149.0  87.8
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG N1518  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 368   NE2
REMARK 620 2 ASP N 369   OD1  90.3
REMARK 620 3 GLU O 198   OE1 157.6 105.8
REMARK 620 4 HOH O3033   O    74.8 102.4  86.3
REMARK 620 5 HOH O3032   O    99.8 101.7  92.2 155.3
REMARK 620 6 HOH O3031   O    83.9 173.7  80.5  78.4  77.0
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  103.5  91.7
REMARK 620 4 HEA N 516   NC   98.1 166.9  89.5
REMARK 620 5 HEA N 516   ND   89.3  90.4 166.9  85.7
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN N1603  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 503   NE2
REMARK 620 2 HIS Y   2   NE2  78.3
REMARK 620 3 HOH Y3077   O   132.2 148.5
REMARK 620 4 HOH Y3078   O   101.3 101.4  68.8
REMARK 620 N                    1     2     3
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  138.2
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 GLU O 198   O
REMARK 620 2 CUA O 228  CU1  114.2
REMARK 620 3 HIS O 204   ND1  82.2 161.8
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN P1262  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS P 148   NE2
REMARK 620 2 HIS P 232   NE2 109.3
REMARK 620 3 GLU P 236   OE1  99.5  89.5
REMARK 620 4 HOH P3027   O   102.1 109.6 144.1
REMARK 620 N                    1     2     3
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  106.0
REMARK 620 3 CYS S  82   SG  110.2 110.4
REMARK 620 4 CYS S  85   SG  104.6 105.9 119.0
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 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 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV A 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD A 525
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 TGL B 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSC B 230
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD B 1086
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU C 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK C 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK C 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV C 266
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV C 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV C 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL C 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD C 271
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL D 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 99
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL G 269
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK G 1263
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD J 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL L 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU M 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU N 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 1518
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA N 1519
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 1603
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA N 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA N 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD N 1604
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL N 1522
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL N 1523
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV N 1524
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA O 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL O 1521
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSC O 1230
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU P 1272
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN P 1262
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD P 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK P 1264
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK P 1265
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV P 1266
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV P 1267
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV P 1268
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL P 1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN S 99
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK T 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL T 1269
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD W 1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD W 1060
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU Z 1526
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DYR   RELATED DB: PDB
REMARK 900 RELATED ID: 2DYS   RELATED DB: PDB
REMARK 900 RELATED ID: 1V54   RELATED DB: PDB
REMARK 900 RELATED ID: 1V55   RELATED DB: PDB
REMARK 900 RELATED ID: 2OCC   RELATED DB: PDB
REMARK 900 RELATED ID: 1OCR   RELATED DB: PDB
REMARK 900 RELATED ID: 1OCO   RELATED DB: PDB
REMARK 900 RELATED ID: 1OCZ   RELATED DB: PDB
REMARK 900 RELATED ID: 1OCC   RELATED DB: PDB
REMARK 900 RELATED ID: 2EIJ   RELATED DB: PDB
REMARK 900 RELATED ID: 2EIK   RELATED DB: PDB
REMARK 900 RELATED ID: 2EIL   RELATED DB: PDB
REMARK 900 RELATED ID: 2EIN   RELATED DB: PDB
DBREF  2EIM A    1   514  UNP    P00396   COX1_BOVIN       1    514
DBREF  2EIM B    1   227  UNP    P68530   COX2_BOVIN       1    227
DBREF  2EIM C    1   261  UNP    P00415   COX3_BOVIN       1    261
DBREF  2EIM D    1   147  UNP    P00423   COX41_BOVIN     23    169
DBREF  2EIM E    1   109  UNP    P00426   COX5A_BOVIN     44    152
DBREF  2EIM F    1    98  UNP    P00428   COX5B_BOVIN     32    129
DBREF  2EIM G    1    85  UNP    P07471   CX6A2_BOVIN     13     97
DBREF  2EIM H    1    85  UNP    P00429   CX6B1_BOVIN      2     86
DBREF  2EIM I    1    73  UNP    P04038   COX6C_BOVIN      1     73
DBREF  2EIM J    1    59  UNP    P07470   CX7A1_BOVIN     22     80
DBREF  2EIM K    1    56  UNP    P13183   COX7B_BOVIN     25     80
DBREF  2EIM L    1    47  UNP    P00430   COX7C_BOVIN     17     63
DBREF  2EIM M    1    46  UNP    P10175   COX81_BOVIN     25     70
DBREF  2EIM N    1   514  UNP    P00396   COX1_BOVIN       1    514
DBREF  2EIM O    1   227  UNP    P68530   COX2_BOVIN       1    227
DBREF  2EIM P    1   261  UNP    P00415   COX3_BOVIN       1    261
DBREF  2EIM Q    1   147  UNP    P00423   COX41_BOVIN     23    169
DBREF  2EIM R    1   109  UNP    P00426   COX5A_BOVIN     44    152
DBREF  2EIM S    1    98  UNP    P00428   COX5B_BOVIN     32    129
DBREF  2EIM T    1    85  UNP    P07471   CX6A2_BOVIN     13     97
DBREF  2EIM U    1    85  UNP    P00429   CX6B1_BOVIN      2     86
DBREF  2EIM V    1    73  UNP    P04038   COX6C_BOVIN      1     73
DBREF  2EIM W    1    59  UNP    P07470   CX7A1_BOVIN     22     80
DBREF  2EIM X    1    56  UNP    P13183   COX7B_BOVIN     25     80
DBREF  2EIM Y    1    47  UNP    P00430   COX7C_BOVIN     17     63
DBREF  2EIM 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 2EIM FME A    1  MET  N-FORMYLMETHIONINE
MODRES 2EIM FME B    1  MET  N-FORMYLMETHIONINE
MODRES 2EIM TPO G   11  THR  PHOSPHOTHREONINE
MODRES 2EIM SAC I    1  SER  N-ACETYL-SERINE
MODRES 2EIM FME N    1  MET  N-FORMYLMETHIONINE
MODRES 2EIM FME O    1  MET  N-FORMYLMETHIONINE
MODRES 2EIM TPO T   11  THR  PHOSPHOTHREONINE
MODRES 2EIM 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  A 518       1
HET     NA  A 519       1
HET     ZN  A 603       1
HET    HEA  A 515      60
HET    HEA  A 516      60
HET    PGV  A 524      51
HET    CHD  A 525      29
HET    CUA  B 228       2
HET    TGL  B 521      63
HET    PSC  B 230      52
HET    CHD  B1086      29
HET    DMU  C 272      33
HET     ZN  C 262       1
HET    PEK  C 264      53
HET    PEK  C 265      53
HET    PGV  C 266      51
HET    PGV  C 267      51
HET    PGV  C 268      51
HET    CDL  C 270     100
HET    CHD  C 271      29
HET    TGL  D 523      63
HET     ZN  F  99       1
HET    CDL  G 269     100
HET    PEK  G1263      53
HET    CHD  J  60      29
HET    TGL  L 522      63
HET    DMU  M 526      33
HET     CU  N 517       1
HET     MG  N1518       1
HET     NA  N1519       1
HET     ZN  N1603       1
HET    HEA  N 515      60
HET    HEA  N 516      60
HET    CHD  N1604      29
HET    TGL  N1522      63
HET    TGL  N1523      63
HET    PGV  N1524      51
HET    CUA  O 228       2
HET    TGL  O1521      63
HET    PSC  O1230      52
HET    DMU  P1272      33
HET     ZN  P1262       1
HET    CHD  P1525      29
HET    PEK  P1264      53
HET    PEK  P1265      53
HET    PGV  P1266      51
HET    PGV  P1267      51
HET    PGV  P1268      51
HET    CDL  P1270     100
HET     ZN  S  99       1
HET    PEK  T 263      53
HET    CDL  T1269     100
HET    CHD  W1271      29
HET    CHD  W1060      29
HET    DMU  Z1526      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      ZN ZINC ION
HETNAM     HEA HEME-A
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     CHD CHOLIC ACID
HETNAM     CUA DINUCLEAR COPPER ION
HETNAM     TGL TRISTEAROYLGLYCEROL
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     DMU DECYL-BETA-D-MALTOPYRANOSIDE
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     CDL CARDIOLIPIN
HETSYN     TPO PHOSPHONOTHREONINE
HETSYN     PGV PHOSPHATIDYLGLYCEROL, 2-VACCENOYL-1-PALMITOYL-SN-
HETSYN   2 PGV  GLYCEROL-3-PHOSPHOGLYCEROL
HETSYN     TGL TRIACYLGLYCEROL
HETSYN     PSC PHOSPHATIDYLCHOLINE, 2-LINOLEOYL-1-PALMITOYL-SN-
HETSYN   2 PSC  GYCEROL-3-PHOSPHOCHOLINE
HETSYN     DMU DECYLMALTOSIDE
HETSYN     PEK PHOSPHATIDYLETHANOLAMINE, 2-ARACHIDONOYL-1-STEAROYL-SN-
HETSYN   2 PEK  GLYCEROL-3-PHOSPHOETHANOLAMINE
HETSYN     CDL DIPHOSPHATIDYL GLYCEROL; BIS-(1,2-DIACYL-SN-GLYCERO-3-
HETSYN   2 CDL  PHOSPHO)-1',3'-SN-GLYCEROL
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   ZN    6(ZN 2+)
FORMUL  31  HEA    4(C49 H56 FE N4 O6)
FORMUL  33  PGV    8(C40 H77 O10 P)
FORMUL  34  CHD    8(C24 H40 O5)
FORMUL  35  CUA    2(CU2)
FORMUL  36  TGL    6(C57 H110 O6)
FORMUL  37  PSC    2(C42 H81 N O8 P 1+)
FORMUL  39  DMU    4(C22 H42 O11)
FORMUL  41  PEK    6(C43 H78 N O8 P)
FORMUL  46  CDL    4(C81 H156 O17 P2 2-)
FORMUL  83  HOH   *1227(H2 O)
HELIX    1   1 FME A    1  LEU A    7  1                                   7
HELIX    2   2 ASN A   11  LEU A   41  1                                  31
HELIX    3   3 ASP A   50  PHE A   68  1                                  19
HELIX    4   4 MET A   69  GLY A   76  1                                   8
HELIX    5   5 GLY A   76  ILE A   87  1                                  12
HELIX    6   6 ARG A   96  LEU A  104  1                                   9
HELIX    7   7 LEU A  104  VAL A  118  1                                  15
HELIX    8   8 GLY A  140  MET A  171  1                                  32
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  LEU A  246  1                                  20
HELIX   13  13 ILE A  247  SER A  262  1                                  16
HELIX   14  14 GLY A  269  GLY A  284  1                                  16
HELIX   15  15 PHE A  285  ILE A  286  5                                   2
HELIX   16  16 VAL A  287  GLY A  296  5                                  10
HELIX   17  17 ASP A  298  ILE A  312  1                                  15
HELIX   18  18 ILE A  312  HIS A  328  1                                  17
HELIX   19  19 SER A  335  ALA A  359  1                                  25
HELIX   20  20 ASN A  360  HIS A  368  1                                   9
HELIX   21  21 THR A  370  LEU A  381  1                                  12
HELIX   22  22 LEU A  381  GLY A  402  1                                  22
HELIX   23  23 ASN A  406  PHE A  426  1                                  21
HELIX   24  24 PHE A  426  SER A  434  1                                   9
HELIX   25  25 PRO A  444  ALA A  446  5                                   3
HELIX   26  26 TYR A  447  LYS A  479  1                                  33
HELIX   27  27 ASN A  491  LEU A  495  5                                   5
HELIX   28  28 SER B   14  LEU B   46  1                                  33
HELIX   29  29 GLU B   60  GLU B   89  1                                  30
HELIX   30  30 ASN B  203  MET B  207  5                                   5
HELIX   31  31 PRO B  215  LEU B  227  1                                  13
HELIX   32  32 PRO C   15  ASN C   38  1                                  24
HELIX   33  33 MET C   40  THR C   66  1                                  27
HELIX   34  34 THR C   72  ALA C  107  1                                  36
HELIX   35  35 THR C  109  GLY C  113  5                                   5
HELIX   36  36 GLU C  128  GLU C  153  1                                  26
HELIX   37  37 ASP C  155  ALA C  184  1                                  30
HELIX   38  38 ASP C  190  LYS C  224  1                                  35
HELIX   39  39 HIS C  232  ILE C  256  1                                  25
HELIX   40  40 LYS D    7  TYR D   11  5                                   5
HELIX   41  41 SER D   34  GLU D   44  1                                  11
HELIX   42  42 LYS D   45  ALA D   46  5                                   2
HELIX   43  43 SER D   47  LEU D   51  5                                   5
HELIX   44  44 SER D   52  PHE D   64  1                                  13
HELIX   45  45 SER D   67  ASN D   72  1                                   6
HELIX   46  46 ASN D   76  VAL D  103  1                                  28
HELIX   47  47 PRO D  108  PHE D  111  5                                   4
HELIX   48  48 GLU D  112  MET D  126  1                                  15
HELIX   49  49 PHE D  134  ALA D  136  5                                   3
HELIX   50  50 THR E    7  LYS E   21  1                                  15
HELIX   51  51 ASP E   25  VAL E   37  1                                  13
HELIX   52  52 GLU E   44  LEU E   58  1                                  15
HELIX   53  53 ASP E   60  ALA E   75  1                                  16
HELIX   54  54 GLU E   80  GLY E   97  1                                  18
HELIX   55  55 THR E  100  GLY E  105  1                                   6
HELIX   56  56 THR F    8  ALA F   13  1                                   6
HELIX   57  57 THR F   14  ALA F   24  1                                  11
HELIX   58  58 GLY G   12  LEU G   23  1                                  12
HELIX   59  59 LEU G   23  SER G   39  1                                  17
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  LYS I   36  1                                  26
HELIX   65  65 VAL I   39  ASN I   53  1                                  15
HELIX   66  66 ASP I   55  LYS I   65  1                                  11
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  GLN K   35  1                                  28
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  LEU N   41  1                                  31
HELIX   75  75 ASP N   50  PHE N   68  1                                  19
HELIX   76  76 MET N   69  GLY N   76  1                                   8
HELIX   77  77 GLY N   76  ILE N   87  1                                  12
HELIX   78  78 ARG N   96  LEU N  104  1                                   9
HELIX   79  79 LEU N  104  VAL N  118  1                                  15
HELIX   80  80 GLY N  140  MET N  171  1                                  32
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  LEU N  246  1                                  20
HELIX   85  85 ILE N  247  SER N  262  1                                  16
HELIX   86  86 GLY N  269  GLY N  284  1                                  16
HELIX   87  87 PHE N  285  ILE N  286  5                                   2
HELIX   88  88 VAL N  287  GLY N  296  5                                  10
HELIX   89  89 ASP N  298  ILE N  312  1                                  15
HELIX   90  90 ILE N  312  HIS N  328  1                                  17
HELIX   91  91 SER N  335  ALA N  359  1                                  25
HELIX   92  92 ASN N  360  HIS N  368  1                                   9
HELIX   93  93 THR N  370  LEU N  381  1                                  12
HELIX   94  94 LEU N  381  GLY N  402  1                                  22
HELIX   95  95 ASN N  406  PHE N  426  1                                  21
HELIX   96  96 PHE N  426  SER N  434  1                                   9
HELIX   97  97 PRO N  444  ALA N  446  5                                   3
HELIX   98  98 TYR N  447  LYS N  479  1                                  33
HELIX   99  99 ASN N  491  LEU N  495  5                                   5
HELIX  100 100 SER O   14  LEU O   46  1                                  33
HELIX  101 101 GLU O   60  GLU O   89  1                                  30
HELIX  102 102 ASN O  203  MET O  207  5                                   5
HELIX  103 103 PRO O  215  LEU O  227  1                                  13
HELIX  104 104 PRO P   15  ASN P   38  1                                  24
HELIX  105 105 MET P   40  THR P   66  1                                  27
HELIX  106 106 THR P   72  ALA P  107  1                                  36
HELIX  107 107 THR P  109  GLY P  113  5                                   5
HELIX  108 108 GLU P  128  GLU P  153  1                                  26
HELIX  109 109 ASP P  155  ALA P  184  1                                  30
HELIX  110 110 ASP P  190  LYS P  224  1                                  35
HELIX  111 111 HIS P  232  ILE P  256  1                                  25
HELIX  112 112 LYS Q    7  TYR Q   11  5                                   5
HELIX  113 113 SER Q   34  GLU Q   44  1                                  11
HELIX  114 114 LYS Q   45  ALA Q   46  5                                   2
HELIX  115 115 SER Q   47  LEU Q   51  5                                   5
HELIX  116 116 SER Q   52  PHE Q   64  1                                  13
HELIX  117 117 SER Q   67  ASN Q   72  1                                   6
HELIX  118 118 ASN Q   76  VAL Q  103  1                                  28
HELIX  119 119 PRO Q  108  PHE Q  111  5                                   4
HELIX  120 120 GLU Q  112  MET Q  126  1                                  15
HELIX  121 121 PHE Q  134  ALA Q  136  5                                   3
HELIX  122 122 THR R    7  LYS R   21  1                                  15
HELIX  123 123 ASP R   25  VAL R   37  1                                  13
HELIX  124 124 GLU R   44  LEU R   58  1                                  15
HELIX  125 125 ASP R   60  LYS R   74  1                                  15
HELIX  126 126 GLU R   80  GLY R   97  1                                  18
HELIX  127 127 THR R  100  GLY R  105  1                                   6
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  SER T   39  1                                  17
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  GLU U   78  1                                  14
HELIX  136 136 GLY V   11  LYS V   36  1                                  26
HELIX  137 137 VAL V   39  ASN V   53  1                                  15
HELIX  138 138 ASP V   55  LYS V   65  1                                  11
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 2 VAL A 482  THR A 484  0
SHEET    2   A 2 THR M   2  ALA M   3 -1  O  THR M   2   N  LEU A 483
SHEET    1   B 3 TYR A 510  VAL A 511  0
SHEET    2   B 3 LYS F  55  CYS F  60  1  O  GLY F  59   N  TYR A 510
SHEET    3   B 3 ILE F  70  HIS F  75 -1  O  LEU F  74   N  ARG F  56
SHEET    1   C 5 LEU B 116  SER B 120  0
SHEET    2   C 5 TYR B 105  TYR B 110 -1  N  TRP B 106   O  SER B 120
SHEET    3   C 5 LEU B  95  HIS B 102 -1  N  MET B 100   O  SER B 107
SHEET    4   C 5 ILE B 150  SER B 156  1  O  ARG B 151   N  VAL B  97
SHEET    5   C 5 ASN B 180  LEU B 184 -1  O  THR B 182   N  MET B 152
SHEET    1   D 3 VAL B 142  PRO B 145  0
SHEET    2   D 3 ILE B 209  VAL B 214  1  O  GLU B 212   N  LEU B 144
SHEET    3   D 3 GLY B 190  GLY B 194 -1  N  TYR B 192   O  LEU B 211
SHEET    1   E 2 HIS B 161  VAL B 165  0
SHEET    2   E 2 LEU B 170  ALA B 174 -1  O  ALA B 174   N  HIS B 161
SHEET    1   F 2 TRP D 138  ASP D 139  0
SHEET    2   F 2 GLU D 144  TRP D 145 -1  O  GLU D 144   N  ASP D 139
SHEET    1   G 3 ASN F  47  PRO F  50  0
SHEET    2   G 3 HIS F  88  VAL F  92  1  O  LYS F  90   N  ASN F  47
SHEET    3   G 3 GLN F  80  ARG F  81 -1  N  GLN F  80   O  TYR F  89
SHEET    1   H 2 VAL N 482  THR N 484  0
SHEET    2   H 2 THR Z   2  ALA Z   3 -1  O  THR Z   2   N  LEU N 483
SHEET    1   I 3 TYR N 510  VAL N 511  0
SHEET    2   I 3 LYS S  55  CYS S  60  1  O  GLY S  59   N  TYR N 510
SHEET    3   I 3 ILE S  70  HIS S  75 -1  O  LEU S  74   N  ARG S  56
SHEET    1   J 5 LEU O 116  SER O 120  0
SHEET    2   J 5 TYR O 105  TYR O 110 -1  N  TRP O 106   O  SER O 120
SHEET    3   J 5 LEU O  95  HIS O 102 -1  N  HIS O 102   O  TYR O 105
SHEET    4   J 5 ILE O 150  SER O 156  1  O  ARG O 151   N  VAL O  97
SHEET    5   J 5 ASN O 180  LEU O 184 -1  O  THR O 182   N  MET O 152
SHEET    1   K 3 VAL O 142  PRO O 145  0
SHEET    2   K 3 ILE O 209  VAL O 214  1  O  GLU O 212   N  LEU O 144
SHEET    3   K 3 GLY O 190  GLY O 194 -1  N  TYR O 192   O  LEU O 211
SHEET    1   L 2 HIS O 161  VAL O 165  0
SHEET    2   L 2 LEU O 170  ALA O 174 -1  O  ALA O 174   N  HIS O 161
SHEET    1   M 2 TRP Q 138  ASP Q 139  0
SHEET    2   M 2 GLU Q 144  TRP Q 145 -1  O  GLU Q 144   N  ASP Q 139
SHEET    1   N 3 ASN S  47  PRO S  50  0
SHEET    2   N 3 HIS S  88  VAL S  92  1  O  LYS S  90   N  ASN S  47
SHEET    3   N 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  2.04
SSBOND   3 CYS U   29    CYS U   64                          1555   1555  2.04
SSBOND   4 CYS U   39    CYS U   53                          1555   1555  2.04
LINK         NE2 HIS A 240                 CE2 TYR A 244     1555   1555  1.38
LINK         NE2 HIS N 240                 CE2 TYR N 244     1555   1555  1.37
LINK         C   FME A   1                 N   PHE A   2     1555   1555  1.33
LINK         C   FME B   1                 N   ALA B   2     1555   1555  1.32
LINK         C   GLY G  10                 N   TPO G  11     1555   1555  1.34
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 A 519     1555   1555  2.31
LINK         OE1 GLU A  40                NA    NA A 519     1555   1555  2.21
LINK         O   GLY A  45                NA    NA A 519     1555   1555  2.39
LINK         NE2 HIS A  61                FE   HEA A 515     1555   1555  2.07
LINK         ND1 HIS A 240                CU    CU A 517     1555   1555  2.02
LINK         NE2 HIS A 290                CU    CU A 517     1555   1555  1.99
LINK         NE2 HIS A 291                CU    CU A 517     1555   1555  1.99
LINK         NE2 HIS A 368                MG    MG A 518     1555   1555  2.22
LINK         OD1 ASP A 369                MG    MG A 518     1555   1555  2.02
LINK         NE2 HIS A 376                FE   HEA A 516     1555   1555  2.00
LINK         NE2 HIS A 378                FE   HEA A 515     1555   1555  1.83
LINK         O   SER A 441                NA    NA A 519     1555   1555  2.29
LINK         NE2 HIS A 503                ZN    ZN A 603     1555   1555  2.06
LINK         ND1 HIS B 161                CU1  CUA B 228     1555   1555  2.02
LINK         O   GLU B 198                CU2  CUA B 228     1555   1555  2.38
LINK         OE1 GLU B 198                MG    MG A 518     1555   1555  2.08
LINK         ND1 HIS B 204                CU2  CUA B 228     1555   1555  1.97
LINK         NE2 HIS C 148                ZN    ZN C 262     1555   1555  1.92
LINK         NE2 HIS C 232                ZN    ZN C 262     1555   1555  1.95
LINK         OE1 GLU C 236                ZN    ZN C 262     1555   1555  2.19
LINK         SG  CYS F  60                ZN    ZN F  99     1555   1555  2.20
LINK         SG  CYS F  62                ZN    ZN F  99     1555   1555  2.25
LINK         SG  CYS F  82                ZN    ZN F  99     1555   1555  2.20
LINK         SG  CYS F  85                ZN    ZN F  99     1555   1555  2.19
LINK         NE2 HIS L   2                ZN    ZN A 603     1555   1555  2.03
LINK         O   GLU N  40                NA    NA N1519     1555   1555  2.28
LINK         OE1 GLU N  40                NA    NA N1519     1555   1555  2.24
LINK         O   GLY N  45                NA    NA N1519     1555   1555  2.40
LINK         NE2 HIS N  61                FE   HEA N 515     1555   1555  2.03
LINK         ND1 HIS N 240                CU    CU N 517     1555   1555  1.99
LINK         NE2 HIS N 290                CU    CU N 517     1555   1555  2.02
LINK         NE2 HIS N 291                CU    CU N 517     1555   1555  1.94
LINK         NE2 HIS N 368                MG    MG N1518     1555   1555  2.23
LINK         OD1 ASP N 369                MG    MG N1518     1555   1555  2.07
LINK         NE2 HIS N 376                FE   HEA N 516     1555   1555  2.02
LINK         NE2 HIS N 378                FE   HEA N 515     1555   1555  2.05
LINK         O   SER N 441                NA    NA N1519     1555   1555  2.30
LINK         NE2 HIS N 503                ZN    ZN N1603     1555   1555  2.14
LINK         ND1 HIS O 161                CU1  CUA O 228     1555   1555  2.00
LINK         O   GLU O 198                CU2  CUA O 228     1555   1555  2.39
LINK         OE1 GLU O 198                MG    MG N1518     1555   1555  2.05
LINK         ND1 HIS O 204                CU2  CUA O 228     1555   1555  2.07
LINK         NE2 HIS P 148                ZN    ZN P1262     1555   1555  1.93
LINK         NE2 HIS P 232                ZN    ZN P1262     1555   1555  2.07
LINK         OE1 GLU P 236                ZN    ZN P1262     1555   1555  2.10
LINK         SG  CYS S  60                ZN    ZN S  99     1555   1555  2.21
LINK         SG  CYS S  62                ZN    ZN S  99     1555   1555  2.22
LINK         SG  CYS S  82                ZN    ZN S  99     1555   1555  2.23
LINK         SG  CYS S  85                ZN    ZN S  99     1555   1555  2.19
LINK         NE2 HIS Y   2                ZN    ZN N1603     1555   1555  2.13
LINK        MG    MG A 518                 O   HOH B2033     1555   1555  2.36
LINK        MG    MG A 518                 O   HOH B2031     1555   1555  2.35
LINK        MG    MG A 518                 O   HOH B2032     1555   1555  2.34
LINK        NA    NA A 519                 O   HOH A2026     1555   1555  2.54
LINK        ZN    ZN C 262                 O   HOH C2027     1555   1555  2.16
LINK        ZN    ZN A 603                 O   HOH A2078     1555   1555  2.28
LINK        ZN    ZN A 603                 O   HOH A2077     1555   1555  2.33
LINK        MG    MG N1518                 O   HOH O3033     1555   1555  2.37
LINK        MG    MG N1518                 O   HOH O3032     1555   1555  2.31
LINK        MG    MG N1518                 O   HOH O3031     1555   1555  2.34
LINK        NA    NA N1519                 O   HOH N3026     1555   1555  2.56
LINK        ZN    ZN P1262                 O   HOH P3027     1555   1555  2.18
LINK        ZN    ZN N1603                 O   HOH Y3077     1555   1555  2.36
LINK        ZN    ZN N1603                 O   HOH Y3078     1555   1555  2.31
CISPEP   1 PRO A  130    PRO A  131          0         0.49
CISPEP   2 CYS A  498    PRO A  499          0         1.36
CISPEP   3 GLN B  103    TRP B  104          0         0.02
CISPEP   4 TRP C  116    PRO C  117          0         0.09
CISPEP   5 PRO N  130    PRO N  131          0        -1.42
CISPEP   6 CYS N  498    PRO N  499          0        -0.53
CISPEP   7 GLN O  103    TRP O  104          0         0.33
CISPEP   8 TRP P  116    PRO P  117          0        -0.19
SITE     1 AC1  3 HIS A 240  HIS A 290  HIS A 291
SITE     1 AC2  7 HIS A 368  ASP A 369  SER B 197  GLU B 198
SITE     2 AC2  7 HOH B2031  HOH B2032  HOH B2033
SITE     1 AC3  4 GLU A  40  GLY A  45  SER A 441  HOH A2026
SITE     1 AC4  4 HIS A 503  HOH A2077  HOH A2078  HIS L   2
SITE     1 AC5 26 MET A  28  SER A  34  ILE A  37  ARG A  38
SITE     2 AC5 26 TYR A  54  VAL A  58  HIS A  61  ALA A  62
SITE     3 AC5 26 MET A  65  ILE A  73  GLY A 125  TRP A 126
SITE     4 AC5 26 TYR A 371  PHE A 377  HIS A 378  LEU A 381
SITE     5 AC5 26 SER A 382  PHE A 425  GLN A 428  ARG A 438
SITE     6 AC5 26 ARG A 439  VAL A 465  MET A 468  HOH A2005
SITE     7 AC5 26 HOH A2036  HOH A2072
SITE     1 AC6 31 TRP A 126  TRP A 236  VAL A 243  TYR A 244
SITE     2 AC6 31 HIS A 290  HIS A 291  THR A 309  ILE A 312
SITE     3 AC6 31 ALA A 313  THR A 316  GLY A 317  THR A 349
SITE     4 AC6 31 GLY A 352  GLY A 355  LEU A 358  ALA A 359
SITE     5 AC6 31 ASP A 364  HIS A 368  VAL A 373  HIS A 376
SITE     6 AC6 31 PHE A 377  VAL A 380  LEU A 381  ARG A 438
SITE     7 AC6 31 HOH A2007  HOH A2016  HOH A2034  HOH A2044
SITE     8 AC6 31 ILE B  34  PRO B  69  ILE B  72
SITE     1 AC7 11 ASN A 406  THR A 408  TRP A 409  HOH A4201
SITE     2 AC7 11 ALA D  84  PHE D  87  GLN M  15  ALA M  16
SITE     3 AC7 11 LEU M  19  SER M  20  HOH M2160
SITE     1 AC8  7 HIS A 233  ASP A 300  THR A 301  TYR A 304
SITE     2 AC8  7 TRP C  99  HIS C 103  PGV C 268
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 ASN A 422  PHE A 430  LEU A 433  HOH A4145
SITE     2 BC1 12 LEU B   7  LEU B  28  VAL B  31  SER B  35
SITE     3 BC1 12 LEU B  39  HOH B4171  ARG I  43  HOH I2383
SITE     1 BC2 17 PHE A 321  ILE B  41  MET B  45  HIS B  52
SITE     2 BC2 17 MET B  56  ASP B  57  VAL B  61  TRP B  65
SITE     3 BC2 17 HIS E   5  ASP E   8  PHE E  11  LEU E  41
SITE     4 BC2 17 HOH E2129  HOH E2401  ARG I  10  ALA I  14
SITE     5 BC2 17 HOH I4178
SITE     1 BC3 10 MET A 271  GLU B  62  THR B  63  HOH B2112
SITE     2 BC3 10 HOH B2382  PEK P1265  ARG T  14  PHE T  18
SITE     3 BC3 10 GLY T  22  HOH T3309
SITE     1 BC4  4 TRP C  34  MET C  40  TRP G  62  GLY G  63
SITE     1 BC5  4 HIS C 148  HIS C 232  GLU C 236  HOH C2027
SITE     1 BC6 17 HIS A 151  TRP C  34  TYR C 181  TYR C 182
SITE     2 BC6 17 ALA C 184  PHE C 186  THR C 187  ILE C 188
SITE     3 BC6 17 PHE C 198  GLY C 202  TRP G  62  THR G  68
SITE     4 BC6 17 PHE G  69  PHE G  70  HIS G  71  ASN G  76
SITE     5 BC6 17 HOH G2261
SITE     1 BC7 17 LYS C 157  HIS C 158  THR C 168  TYR C 172
SITE     2 BC7 17 HOH C4087  ALA F   1  LYS G   5  ARG G  17
SITE     3 BC7 17 PHE G  21  GLY G  22  CDL G 269  TRP N 275
SITE     4 BC7 17 SER N 279  ILE N 314  CHD N1604  GLN O  59
SITE     5 BC7 17 THR O  66
SITE     1 BC8 16 PHE A  94  PRO A  95  ARG A  96  MET A  97
SITE     2 BC8 16 HOH A2233  HIS C   9  THR C  28  ASN C  50
SITE     3 BC8 16 MET C  54  TRP C  57  TRP C  58  GLU C  64
SITE     4 BC8 16 HIS C  71  LEU C  79  GLU C  90  HOH C2145
SITE     1 BC9 23 MET C  54  TRP C  58  VAL C  61  SER C  65
SITE     2 BC9 23 THR C  66  HIS C  71  GLU C  90  HIS C 207
SITE     3 BC9 23 ILE C 210  THR C 213  PHE C 214  ARG C 221
SITE     4 BC9 23 HIS C 226  PHE C 227  THR C 228  HIS C 231
SITE     5 BC9 23 HIS C 232  PHE C 233  GLY C 234  CDL C 270
SITE     6 BC9 23 HOH C2221  HOH C2357  HOH F2137
SITE     1 CC1  7 CHD A 525  TRP C  99  TYR C 102  HIS C 103
SITE     2 CC1  7 ASN H  22  ASN H  24  CDL T1269
SITE     1 CC2 19 MET C  51  LEU C  52  MET C  54  TYR C  55
SITE     2 CC2 19 TRP C  58  ARG C  59  ARG C  63  PHE C  67
SITE     3 CC2 19 THR C 213  ILE C 216  VAL C 217  PHE C 220
SITE     4 CC2 19 LYS C 224  HIS C 226  PGV C 267  HOH C4089
SITE     5 CC2 19 LYS J   8  THR J  27  HOH J4266
SITE     1 CC3  6 ARG C 156  LEU C 160  PHE C 164  LEU C 223
SITE     2 CC3  6 HOH C4275  PHE J   1
SITE     1 CC4 15 TRP A 334  LEU A 342  GLY A 343  LYS A 411
SITE     2 CC4 15 PHE A 414  PHE A 418  ILE B  42  HOH B2360
SITE     3 CC4 15 ARG D  73  SER D  74  GLU D  77  TRP D  78
SITE     4 CC4 15 ILE D  89  HOH D4040  HOH D4382
SITE     1 CC5  4 CYS F  60  CYS F  62  CYS F  82  CYS F  85
SITE     1 CC6 25 LEU C 127  LEU C 131  LEU C 250  TYR C 253
SITE     2 CC6 25 PEK C 265  LEU G  23  SER G  27  LEU G  30
SITE     3 CC6 25 CYS G  31  ASN G  34  LEU G  37  HIS G  38
SITE     4 CC6 25 ARG G  42  HOH G4354  PHE N 282  ILE N 286
SITE     5 CC6 25 ASP N 300  TYR N 304  SER N 307  ILE N 311
SITE     6 CC6 25 ALA O  77  LEU O  78  LEU O  81  TYR O  85
SITE     7 CC6 25 PGV P1268
SITE     1 CC7 13 SER G   2  ALA G   3  LYS G   5  GLY G   6
SITE     2 CC7 13 HIS G   8  LYS P  77  ARG P  80  TYR P  81
SITE     3 CC7 13 ILE P  84  PHE P  98  TRP P 240  PHE P 244
SITE     4 CC7 13 VAL P 247
SITE     1 CC8  5 TYR J  32  ARG J  33  MET J  36  THR J  37
SITE     2 CC8  5 LEU J  40
SITE     1 CC9 18 THR A  17  LEU A  20  LEU A  21  PHE A  22
SITE     2 CC9 18 TRP A  25  TRP A  81  LEU A 113  PHE A 400
SITE     3 CC9 18 ILE A 472  ILE L  11  PRO L  12  PHE L  13
SITE     4 CC9 18 SER L  14  ARG L  20  MET L  24  MET L  25
SITE     5 CC9 18 PHE L  28  PHE L  29
SITE     1 DC1  7 TRP D  98  LEU M  27  LEU M  28  GLY M  31
SITE     2 DC1  7 TRP M  32  TYR M  35  HIS M  36
SITE     1 DC2  3 HIS N 240  HIS N 290  HIS N 291
SITE     1 DC3  6 HIS N 368  ASP N 369  GLU O 198  HOH O3031
SITE     2 DC3  6 HOH O3032  HOH O3033
SITE     1 DC4  4 GLU N  40  GLY N  45  SER N 441  HOH N3026
SITE     1 DC5  4 HIS N 503  HIS Y   2  HOH Y3077  HOH Y3078
SITE     1 DC6 26 SER N  34  ILE N  37  ARG N  38  TYR N  54
SITE     2 DC6 26 VAL N  58  HIS N  61  ALA N  62  MET N  65
SITE     3 DC6 26 ILE N  73  GLY N 125  TRP N 126  TYR N 371
SITE     4 DC6 26 PHE N 377  HIS N 378  LEU N 381  SER N 382
SITE     5 DC6 26 VAL N 386  PHE N 425  GLN N 428  ARG N 438
SITE     6 DC6 26 ARG N 439  VAL N 465  MET N 468  HOH N3005
SITE     7 DC6 26 HOH N3036  HOH N3072
SITE     1 DC7 31 TRP N 126  TRP N 236  VAL N 243  TYR N 244
SITE     2 DC7 31 ILE N 247  HIS N 290  HIS N 291  ILE N 312
SITE     3 DC7 31 ALA N 313  THR N 316  GLY N 317  THR N 349
SITE     4 DC7 31 GLY N 352  GLY N 355  ILE N 356  LEU N 358
SITE     5 DC7 31 ALA N 359  ASP N 364  HIS N 368  VAL N 373
SITE     6 DC7 31 HIS N 376  PHE N 377  LEU N 381  ARG N 438
SITE     7 DC7 31 HOH N3007  HOH N3016  HOH N3034  HOH N3044
SITE     8 DC7 31 ILE O  34  PRO O  69  LEU O  73
SITE     1 DC8 10 PEK C 265  ARG G  14  ARG G  17  GLY G  22
SITE     2 DC8 10 MET N 271  HOH N2309  HOH N3112  HOH N3382
SITE     3 DC8 10 GLU O  62  THR O  63
SITE     1 DC9 15 THR N  17  LEU N  18  LEU N  20  TRP N  25
SITE     2 DC9 15 LEU N 113  PHE N 400  ILE N 472  ILE Y  11
SITE     3 DC9 15 PRO Y  12  PHE Y  13  SER Y  14  MET Y  24
SITE     4 DC9 15 PHE Y  28  PHE Y  29  HOH Y4161
SITE     1 EC1 20 TRP N 334  MET N 339  LEU N 342  GLY N 343
SITE     2 EC1 20 LYS N 411  PHE N 418  HOH N4206  HOH N4235
SITE     3 EC1 20 LEU O  39  ILE O  42  LEU O  46  LYS O  49
SITE     4 EC1 20 HOH O3360  ARG Q  73  SER Q  74  THR Q  75
SITE     5 EC1 20 GLU Q  77  TRP Q  78  ILE Q  89  ARG V  16
SITE     1 EC2 11 ASN N 406  THR N 408  TRP N 409  HOH N4191
SITE     2 EC2 11 ALA Q  84  PHE Q  87  GLN Z  15  ALA Z  16
SITE     3 EC2 11 LEU Z  19  SER Z  20  HOH Z3160
SITE     1 EC3  6 HIS O 161  CYS O 196  GLU O 198  CYS O 200
SITE     2 EC3  6 HIS O 204  MET O 207
SITE     1 EC4 14 ASN N 422  PHE N 426  PHE N 430  LEU N 433
SITE     2 EC4 14 LEU O   7  LEU O  28  VAL O  31  PHE O  32
SITE     3 EC4 14 SER O  35  LEU O  39  HOH O4117  HOH O4170
SITE     4 EC4 14 ARG V  43  HOH V3383
SITE     1 EC5 16 PHE N 321  HIS N 328  ILE O  41  HIS O  52
SITE     2 EC5 16 MET O  56  ASP O  57  VAL O  61  TRP O  65
SITE     3 EC5 16 LEU O  68  HIS R   5  ASP R   8  PHE R  11
SITE     4 EC5 16 ASP R  40  LEU R  41  ARG V  10  ALA V  14
SITE     1 EC6  5 TRP P  34  MET P  40  PEK P1264  TRP T  62
SITE     2 EC6  5 GLY T  63
SITE     1 EC7  4 HIS P 148  HIS P 232  GLU P 236  HOH P3027
SITE     1 EC8  7 HIS N 233  ASP N 300  THR N 301  TYR N 304
SITE     2 EC8  7 TRP P  99  HIS P 103  PGV P1268
SITE     1 EC9 18 HIS N 151  TRP P  34  TYR P 181  TYR P 182
SITE     2 EC9 18 ALA P 184  PHE P 186  THR P 187  ILE P 188
SITE     3 EC9 18 PHE P 198  GLY P 202  DMU P1272  TRP T  62
SITE     4 EC9 18 THR T  68  PHE T  69  PHE T  70  HIS T  71
SITE     5 EC9 18 ASN T  76  HOH T3261
SITE     1 FC1 15 TRP A 275  SER A 279  ILE A 314  GLN B  59
SITE     2 FC1 15 CHD B1086  HOH B4027  LYS P 157  HIS P 158
SITE     3 FC1 15 THR P 168  TYR P 172  ALA S   1  ARG T  17
SITE     4 FC1 15 PHE T  21  GLY T  22  CDL T1269
SITE     1 FC2 18 PHE N  94  PRO N  95  ARG N  96  MET N  97
SITE     2 FC2 18 MET N 100  PHE N 148  HOH N3233  HIS P   9
SITE     3 FC2 18 THR P  28  ASN P  50  TRP P  57  TRP P  58
SITE     4 FC2 18 VAL P  61  GLU P  64  HIS P  71  LEU P  79
SITE     5 FC2 18 GLU P  90  HOH P3145
SITE     1 FC3 22 MET P  54  TRP P  58  VAL P  61  SER P  65
SITE     2 FC3 22 THR P  66  GLU P  90  HIS P 207  ILE P 210
SITE     3 FC3 22 THR P 213  PHE P 214  ARG P 221  HIS P 226
SITE     4 FC3 22 PHE P 227  THR P 228  HIS P 231  HIS P 232
SITE     5 FC3 22 PHE P 233  GLY P 234  CDL P1270  HOH P3221
SITE     6 FC3 22 HOH P3357  HOH S3137
SITE     1 FC4  5 CDL G 269  TRP P  99  TYR P 102  HIS P 103
SITE     2 FC4  5 CHD P1525
SITE     1 FC5 13 MET P  51  TYR P  55  TRP P  58  ARG P  59
SITE     2 FC5 13 ILE P  62  ARG P  63  PHE P  67  THR P 213
SITE     3 FC5 13 LYS P 224  HIS P 226  PGV P1267  LYS W   8
SITE     4 FC5 13 THR W  27
SITE     1 FC6  4 CYS S  60  CYS S  62  CYS S  82  CYS S  85
SITE     1 FC7 15 LYS C  77  ARG C  80  TYR C  81  ILE C  84
SITE     2 FC7 15 THR C  95  TRP C 240  PHE C 244  VAL C 247
SITE     3 FC7 15 PHE C 251  SER T   2  ALA T   3  LYS T   5
SITE     4 FC7 15 GLY T   6  HIS T   8  HOH T4411
SITE     1 FC8 28 PHE A 282  ILE A 286  ASP A 300  TYR A 304
SITE     2 FC8 28 SER A 307  ILE B  74  ALA B  77  LEU B  78
SITE     3 FC8 28 LEU B  81  TYR B  85  HOH B4283  PGV C 268
SITE     4 FC8 28 LEU P 127  LEU P 131  THR P 134  LEU P 250
SITE     5 FC8 28 TYR P 253  PEK P1265  LEU T  23  SER T  27
SITE     6 FC8 28 LEU T  30  CYS T  31  ASN T  34  LEU T  37
SITE     7 FC8 28 HIS T  38  ARG T  42  HOH T4060  HOH T4261
SITE     1 FC9  7 ARG P 156  LYS P 157  LEU P 160  PHE P 164
SITE     2 FC9  7 LEU P 223  PHE W   1  HOH W4222
SITE     1 GC1  4 TYR W  32  ARG W  33  MET W  36  THR W  37
SITE     1 GC2  7 TRP Q  98  LEU Z  27  LEU Z  28  GLY Z  31
SITE     2 GC2  7 TRP Z  32  TYR Z  35  HIS Z  36
CRYST1  183.909  206.721  178.337  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      0.005437  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004837  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005607        0.00000
      
PROCHECK
Go to PROCHECK summary
 References