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PDBsum entry 3ag3

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Top Page protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
3ag3
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 ×2
HEA-_NO ×2
TGL ×6
PGV ×8
CUA ×2
PSC ×2
CHD ×8
UNX ×2
PEK ×6
CDL ×4
DMU
Metals
_ZN
_CU ×2
_MG ×2
_NA ×2
Waters ×1743
HEADER    OXIDOREDUCTASE                          19-MAR-10   3AG3
TITLE     BOVINE HEART CYTOCHROME C OXIDASE IN THE NITRIC OXIDE-BOUND FULLY
TITLE    2 REDUCED STATE AT 100 K
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 SUBUNIT 5A;
COMPND  24 CHAIN: E, R;
COMPND  25 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VA;
COMPND  26 EC: 1.9.3.1;
COMPND  27 MOL_ID: 6;
COMPND  28 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 5B;
COMPND  29 CHAIN: F, S;
COMPND  30 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VB, CYTOCHROME C OXIDASE
COMPND  31 POLYPEPTIDE VIA;
COMPND  32 EC: 1.9.3.1;
COMPND  33 MOL_ID: 7;
COMPND  34 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 6A2;
COMPND  35 CHAIN: G, T;
COMPND  36 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIA-HEART, COXVIAH,
COMPND  37 CYTOCHROME C OXIDASE POLYPEPTIDE VIB;
COMPND  38 EC: 1.9.3.1;
COMPND  39 MOL_ID: 8;
COMPND  40 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 6B1;
COMPND  41 CHAIN: H, U;
COMPND  42 SYNONYM: CYTOCHROME C OXIDASE SUBUNIT VIB ISOFORM 1, COX VIB-1,
COMPND  43 CYTOCHROME C OXIDASE POLYPEPTIDE VII, CYTOCHROME C OXIDASE SUBUNIT
COMPND  44 AED;
COMPND  45 EC: 1.9.3.1;
COMPND  46 MOL_ID: 9;
COMPND  47 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 6C;
COMPND  48 CHAIN: I, V;
COMPND  49 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIC, CYTOCHROME C OXIDASE
COMPND  50 SUBUNIT STA;
COMPND  51 EC: 1.9.3.1;
COMPND  52 MOL_ID: 10;
COMPND  53 MOLECULE: CYTOCHROME C OXIDASE POLYPEPTIDE 7A1;
COMPND  54 CHAIN: J, W;
COMPND  55 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIA-HEART, CYTOCHROME C
COMPND  56 OXIDASE SUBUNIT VIIA-H, COX VIIA-M, VIIIC;
COMPND  57 EC: 1.9.3.1;
COMPND  58 MOL_ID: 11;
COMPND  59 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 7B;
COMPND  60 CHAIN: K, X;
COMPND  61 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIB, IHQ;
COMPND  62 EC: 1.9.3.1;
COMPND  63 MOL_ID: 12;
COMPND  64 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 7C;
COMPND  65 CHAIN: L, Y;
COMPND  66 SYNONYM: CYTOCHROME C OXIDASE POLYPEPTIDE VIIC, CYTOCHROME C OXIDASE
COMPND  67 POLYPEPTIDE VIIIA;
COMPND  68 EC: 1.9.3.1;
COMPND  69 MOL_ID: 13;
COMPND  70 MOLECULE: CYTOCHROME C OXIDASE SUBUNIT 8B;
COMPND  71 CHAIN: M, Z;
COMPND  72 SYNONYM: CYTOCHROME C OXIDASE SUBUNIT 8H, CYTOCHROME C OXIDASE
COMPND  73 POLYPEPTIDE VIII-HEART, CYTOCHROME C OXIDASE SUBUNIT 8-1, VIIIB, IX;
COMPND  74 EC: 1.9.3.1
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   3 ORGANISM_COMMON: BOVINE;
SOURCE   4 ORGANISM_TAXID: 9913;
SOURCE   5 MOL_ID: 2;
SOURCE   6 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE   7 ORGANISM_COMMON: BOVINE;
SOURCE   8 ORGANISM_TAXID: 9913;
SOURCE   9 MOL_ID: 3;
SOURCE  10 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  11 ORGANISM_COMMON: BOVINE;
SOURCE  12 ORGANISM_TAXID: 9913;
SOURCE  13 MOL_ID: 4;
SOURCE  14 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  15 ORGANISM_COMMON: BOVINE;
SOURCE  16 ORGANISM_TAXID: 9913;
SOURCE  17 MOL_ID: 5;
SOURCE  18 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  19 ORGANISM_COMMON: BOVINE;
SOURCE  20 ORGANISM_TAXID: 9913;
SOURCE  21 MOL_ID: 6;
SOURCE  22 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  23 ORGANISM_COMMON: BOVINE;
SOURCE  24 ORGANISM_TAXID: 9913;
SOURCE  25 MOL_ID: 7;
SOURCE  26 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  27 ORGANISM_COMMON: BOVINE;
SOURCE  28 ORGANISM_TAXID: 9913;
SOURCE  29 MOL_ID: 8;
SOURCE  30 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  31 ORGANISM_COMMON: BOVINE;
SOURCE  32 ORGANISM_TAXID: 9913;
SOURCE  33 MOL_ID: 9;
SOURCE  34 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  35 ORGANISM_COMMON: BOVINE;
SOURCE  36 ORGANISM_TAXID: 9913;
SOURCE  37 MOL_ID: 10;
SOURCE  38 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  39 ORGANISM_COMMON: BOVINE;
SOURCE  40 ORGANISM_TAXID: 9913;
SOURCE  41 MOL_ID: 11;
SOURCE  42 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  43 ORGANISM_COMMON: BOVINE;
SOURCE  44 ORGANISM_TAXID: 9913;
SOURCE  45 MOL_ID: 12;
SOURCE  46 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  47 ORGANISM_COMMON: BOVINE;
SOURCE  48 ORGANISM_TAXID: 9913;
SOURCE  49 MOL_ID: 13;
SOURCE  50 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE  51 ORGANISM_COMMON: BOVINE;
SOURCE  52 ORGANISM_TAXID: 9913
KEYWDS    OXIDOREDUCTASE, COPPER, ELECTRON TRANSPORT, FORMYLATION, HEME, IRON,
KEYWDS   2 MEMBRANE, MITOCHONDRION, MITOCHONDRION INNER MEMBRANE, RESPIRATORY
KEYWDS   3 CHAIN, TRANSMEMBRANE, TRANSPORT, ACETYLATION, TRANSIT PEPTIDE, ZINC,
KEYWDS   4 ISOPEPTIDE BOND, UBL CONJUGATION
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.MURAMOTO,K.OHTA,K.SHINZAWA-ITOH,K.KANDA,M.TANIGUCHI,H.NABEKURA,
AUTHOR   2 E.YAMASHITA,T.TSUKIHARA,S.YOSHIKAWA
REVDAT   2   19-MAY-10 3AG3    1       JRNL
REVDAT   1   28-APR-10 3AG3    0
JRNL        AUTH   K.MURAMOTO,K.OHTA,K.SHINZAWA-ITOH,K.KANDA,M.TANIGUCHI,
JRNL        AUTH 2 H.NABEKURA,E.YAMASHITA,T.TSUKIHARA,S.YOSHIKAWA
JRNL        TITL   BOVINE CYTOCHROME C OXIDASE STRUCTURES ENABLE O2 REDUCTION
JRNL        TITL 2 WITH MINIMIZATION OF REACTIVE OXYGENS AND PROVIDE A
JRNL        TITL 3 PROTON-PUMPING GATE
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 107  7740 2010
JRNL        REFN                   ISSN 0027-8424
JRNL        PMID   20385840
JRNL        DOI    10.1073/PNAS.0910410107
REMARK   2
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.3
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 586677
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 + TEST SET) : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.175
REMARK   3   FREE R VALUE                     : 0.203
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : 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   REFLECTION IN BIN     (WORKING SET) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL
REMARK   3   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          : 2230
REMARK   3   SOLVENT ATOMS            : 1743
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 OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : NULL
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : NULL
REMARK   3   ION PROBE RADIUS   : NULL
REMARK   3   SHRINKAGE RADIUS   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3AG3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-APR-10.
REMARK 100 THE RCSB ID CODE IS RCSB029209.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 1
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 : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 617758
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800
REMARK 200  RESOLUTION RANGE LOW       (A) : 83.600
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: 2EIJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 70.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.12
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       91.14450
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.95800
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      104.17900
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.95800
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       91.14450
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      104.17900
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIDECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350                    AND CHAINS: J, K, L, M
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIDECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: N, O, P, Q, R, S, T, U, V,
REMARK 350                    AND CHAINS: W, X, Y, Z
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465   M RES C SSSEQI
REMARK 465     MET C     1
REMARK 465     THR C     2
REMARK 465     ALA D     1
REMARK 465     HIS D     2
REMARK 465     GLY D     3
REMARK 465     SER E     1
REMARK 465     HIS E     2
REMARK 465     GLY E     3
REMARK 465     SER E     4
REMARK 465     PRO G    85
REMARK 465     ALA H     1
REMARK 465     GLU H     2
REMARK 465     ASP H     3
REMARK 465     ILE H     4
REMARK 465     GLN H     5
REMARK 465     ALA H     6
REMARK 465     LYS J    59
REMARK 465     ILE K     1
REMARK 465     HIS K     2
REMARK 465     GLN K     3
REMARK 465     LYS K     4
REMARK 465     ARG K     5
REMARK 465     GLU K    55
REMARK 465     GLN K    56
REMARK 465     SER L     1
REMARK 465     SER M    44
REMARK 465     ALA M    45
REMARK 465     ALA M    46
REMARK 465     MET P     1
REMARK 465     THR P     2
REMARK 465     ALA Q     1
REMARK 465     HIS Q     2
REMARK 465     GLY Q     3
REMARK 465     SER R     1
REMARK 465     HIS R     2
REMARK 465     GLY R     3
REMARK 465     SER R     4
REMARK 465     PRO T    85
REMARK 465     ALA U     1
REMARK 465     GLU U     2
REMARK 465     ASP U     3
REMARK 465     ILE U     4
REMARK 465     GLN U     5
REMARK 465     ALA U     6
REMARK 465     LYS W    59
REMARK 465     ILE X     1
REMARK 465     HIS X     2
REMARK 465     GLN X     3
REMARK 465     LYS X     4
REMARK 465     ARG X     5
REMARK 465     GLU X    55
REMARK 465     GLN X    56
REMARK 465     SER Y     1
REMARK 465     SER Z    44
REMARK 465     ALA Z    45
REMARK 465     ALA Z    46
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: 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   O    HOH A  2027     O    HOH A  2494              1.49
REMARK 500   O    ILE S    52     CE1  HIS S    94              1.49
REMARK 500   O    ASN M    39     OG   SER M    43              1.86
REMARK 500   O    HOH A  2701     O    HOH A  2702              1.99
REMARK 500   O    HOH N  3701     O    HOH N  3702              2.02
REMARK 500   C38  PEK P  1265     C27  CDL T  1269              2.06
REMARK 500   O    ILE S    52     ND1  HIS S    94              2.07
REMARK 500  UNK   UNX P   262     O    HOH P  3259              2.09
REMARK 500   OD1  ASP A    51     OG   SER A   441              2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   OG1  THR I     2     OE1  GLU R    80     3647     1.64
REMARK 500   O    SER O   126     CB   HIS S    94     2684     2.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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   RES CSSEQI ATM2   DEVIATION
REMARK 500    TYR A  19   CZ    TYR A  19   CE2     0.080
REMARK 500    ARG A  38   CZ    ARG A  38   NH2     0.083
REMARK 500    ALA A  89   CA    ALA A  89   CB      0.136
REMARK 500    SER A 101   CB    SER A 101   OG      0.086
REMARK 500    ALA A 122   CA    ALA A 122   CB      0.141
REMARK 500    TRP A 126   CZ3   TRP A 126   CH2     0.124
REMARK 500    TYR A 129   CZ    TYR A 129   CE2    -0.089
REMARK 500    TYR A 129   CE2   TYR A 129   CD2     0.111
REMARK 500    GLY A 154   N     GLY A 154   CA      0.097
REMARK 500    MET A 189   CG    MET A 189   SD     -0.233
REMARK 500    TYR A 231   CG    TYR A 231   CD1     0.083
REMARK 500    PHE A 238   CD1   PHE A 238   CE1     0.127
REMARK 500    TYR A 244   CD1   TYR A 244   CE1     0.108
REMARK 500    PHE A 293   CB    PHE A 293   CG      0.111
REMARK 500    MET A 297   CG    MET A 297   SD      0.206
REMARK 500    ASP A 298   CB    ASP A 298   CG      0.130
REMARK 500    ASP A 298   CG    ASP A 298   OD2     0.148
REMARK 500    ARG A 302   CZ    ARG A 302   NH1     0.108
REMARK 500    PHE A 346   CD1   PHE A 346   CE1     0.157
REMARK 500    PHE A 346   CE2   PHE A 346   CD2     0.142
REMARK 500    TYR A 379   CD1   TYR A 379   CE1     0.091
REMARK 500    VAL A 394   CB    VAL A 394   CG2    -0.157
REMARK 500    GLU A 507   CG    GLU A 507   CD      0.096
REMARK 500    ASN A 512   CB    ASN A 512   CG     -0.201
REMARK 500    GLU B  18   CD    GLU B  18   OE1     0.079
REMARK 500    GLU B  18   CD    GLU B  18   OE2     0.067
REMARK 500    TYR B  40   CD1   TYR B  40   CE1     0.112
REMARK 500    GLN B  59   CG    GLN B  59   CD      0.195
REMARK 500    GLU B  60   CG    GLU B  60   CD      0.101
REMARK 500    TRP B  65   CB    TRP B  65   CG     -0.157
REMARK 500    TYR B  85   CD1   TYR B  85   CE1     0.095
REMARK 500    MET B  87   CG    MET B  87   SD      0.213
REMARK 500    ASN B  92   CB    ASN B  92   CG      0.150
REMARK 500    ASP B 115   CB    ASP B 115   CG      0.145
REMARK 500    GLU B 132   CD    GLU B 132   OE2     0.106
REMARK 500    GLU B 147   CG    GLU B 147   CD      0.096
REMARK 500    GLU B 157   CB    GLU B 157   CG      0.150
REMARK 500    SER B 167   CB    SER B 167   OG     -0.158
REMARK 500    TYR B 192   CG    TYR B 192   CD1     0.083
REMARK 500    TYR B 192   CZ    TYR B 192   CE2     0.115
REMARK 500    TYR B 218   CD1   TYR B 218   CE1     0.110
REMARK 500    TYR B 218   CE2   TYR B 218   CD2     0.091
REMARK 500    SER C  29   CA    SER C  29   CB      0.140
REMARK 500    SER C  29   CB    SER C  29   OG     -0.099
REMARK 500    TYR C  81   CD1   TYR C  81   CE1     0.107
REMARK 500    TYR C 181   CD1   TYR C 181   CE1     0.127
REMARK 500    TYR C 181   CE2   TYR C 181   CD2     0.114
REMARK 500    TYR C 253   CG    TYR C 253   CD1     0.083
REMARK 500    PHE D  87   CD1   PHE D  87   CE1     0.137
REMARK 500    LYS D 100   CE    LYS D 100   NZ      0.212
REMARK 500
REMARK 500 THIS ENTRY HAS     136 BOND DEVIATIONS.
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    ARG A   5   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    TYR A 129   CB  -  CG  -  CD1 ANGL. DEV. =  -3.9 DEGREES
REMARK 500    LEU A 136   CA  -  CB  -  CG  ANGL. DEV. =  16.9 DEGREES
REMARK 500    LEU A 136   CB  -  CG  -  CD2 ANGL. DEV. = -20.4 DEGREES
REMARK 500    LEU A 152   CB  -  CG  -  CD1 ANGL. DEV. = -10.7 DEGREES
REMARK 500    ILE A 169   CG1 -  CB  -  CG2 ANGL. DEV. = -14.1 DEGREES
REMARK 500    MET A 189   CA  -  CB  -  CG  ANGL. DEV. = -12.2 DEGREES
REMARK 500    MET A 189   CG  -  SD  -  CE  ANGL. DEV. = -16.0 DEGREES
REMARK 500    MET A 297   CG  -  SD  -  CE  ANGL. DEV. = -15.2 DEGREES
REMARK 500    ASP A 298   CB  -  CG  -  OD2 ANGL. DEV. =   8.0 DEGREES
REMARK 500    ARG A 302   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    MET A 310   CG  -  SD  -  CE  ANGL. DEV. =  -9.8 DEGREES
REMARK 500    VAL A 380   CB  -  CA  -  C   ANGL. DEV. = -13.3 DEGREES
REMARK 500    MET A 417   CG  -  SD  -  CE  ANGL. DEV. = -11.8 DEGREES
REMARK 500    ARG A 438   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES
REMARK 500    ARG A 439   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    ASP A 442   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    TYR A 510   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES
REMARK 500    ASN A 512   CB  -  CA  -  C   ANGL. DEV. = -13.4 DEGREES
REMARK 500    SER B  36   CB  -  CA  -  C   ANGL. DEV. =  11.7 DEGREES
REMARK 500    LEU B  37   CB  -  CG  -  CD1 ANGL. DEV. = -17.7 DEGREES
REMARK 500    GLU B  60   N   -  CA  -  C   ANGL. DEV. = -19.3 DEGREES
REMARK 500    TRP B  65   CB  -  CA  -  C   ANGL. DEV. =  16.9 DEGREES
REMARK 500    THR B  66   OG1 -  CB  -  CG2 ANGL. DEV. =  15.1 DEGREES
REMARK 500    ARG B  82   CG  -  CD  -  NE  ANGL. DEV. = -18.1 DEGREES
REMARK 500    ARG B  82   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    MET B  87   CA  -  CB  -  CG  ANGL. DEV. =  13.4 DEGREES
REMARK 500    SER C  29   CA  -  CB  -  OG  ANGL. DEV. = -17.6 DEGREES
REMARK 500    PHE C  94   CB  -  CG  -  CD2 ANGL. DEV. =  -5.5 DEGREES
REMARK 500    TYR C 102   CB  -  CG  -  CD2 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    LEU C 176   CB  -  CG  -  CD1 ANGL. DEV. = -11.1 DEGREES
REMARK 500    ARG C 221   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    PHE C 233   CB  -  CG  -  CD2 ANGL. DEV. =  -4.5 DEGREES
REMARK 500    SER D   4   N   -  CA  -  CB  ANGL. DEV. =  10.5 DEGREES
REMARK 500    ARG D  19   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.7 DEGREES
REMARK 500    ARG D  19   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES
REMARK 500    ARG D  20   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES
REMARK 500    ARG D  20   CD  -  NE  -  CZ  ANGL. DEV. =   8.6 DEGREES
REMARK 500    ARG D  20   NE  -  CZ  -  NH1 ANGL. DEV. =   8.9 DEGREES
REMARK 500    ARG D  20   NE  -  CZ  -  NH2 ANGL. DEV. = -10.6 DEGREES
REMARK 500    ASP D  21   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES
REMARK 500    SER D  36   N   -  CA  -  CB  ANGL. DEV. =   9.7 DEGREES
REMARK 500    LEU D  94   CB  -  CG  -  CD2 ANGL. DEV. =  10.9 DEGREES
REMARK 500    ASP E  40   CB  -  CG  -  OD2 ANGL. DEV. =   9.4 DEGREES
REMARK 500    ASP E  60   CB  -  CG  -  OD2 ANGL. DEV. =   6.9 DEGREES
REMARK 500    ARG E  90   CG  -  CD  -  NE  ANGL. DEV. = -12.6 DEGREES
REMARK 500    ARG E  90   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES
REMARK 500    ARG E  90   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES
REMARK 500    LEU F  48   CB  -  CG  -  CD1 ANGL. DEV. =  11.3 DEGREES
REMARK 500    ARG G  17   CB  -  CG  -  CD  ANGL. DEV. = -19.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS     108 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    ASP A  50       98.93   -163.58
REMARK 500    MET A  69      -63.60   -107.62
REMARK 500    ASP A  91     -162.12   -175.50
REMARK 500    GLU A 119     -129.23     50.00
REMARK 500    THR A 218       43.00   -141.30
REMARK 500    GLU B  60      -50.78   -178.55
REMARK 500    ASN B  92       86.01     47.45
REMARK 500    TYR B 113      -55.93   -131.14
REMARK 500    ASP B 158      -99.43   -148.49
REMARK 500    SER C  65      -66.27    -97.15
REMARK 500    GLU C 128     -114.44   -101.49
REMARK 500    HIS C 232       51.79   -165.31
REMARK 500    TRP C 258      -67.45   -106.91
REMARK 500    GLN D 132      -41.39   -140.26
REMARK 500    PHE D 134      -79.08   -146.27
REMARK 500    ASP F  65       -8.87     77.79
REMARK 500    HIS F  94      160.67    128.76
REMARK 500    GLN F  95      -98.60    105.19
REMARK 500    LEU F  96     -128.06     76.93
REMARK 500    ALA G   3      -69.23     74.89
REMARK 500    ALA G   4       13.23    142.00
REMARK 500    LYS G   5     -136.15   -110.64
REMARK 500    ASP G   7      -86.78    -12.31
REMARK 500    HIS G   8      -11.96     41.82
REMARK 500    TRP G  36       50.76    -90.77
REMARK 500    LEU G  37      -43.44   -165.35
REMARK 500    HIS G  38       30.56    -89.22
REMARK 500    SER G  39     -148.61    -83.71
REMARK 500    ILE H   8       13.52     81.54
REMARK 500    LYS H   9     -145.90    -84.04
REMARK 500    ASN H  10       31.30     80.90
REMARK 500    ALA H  45      -87.76    -53.66
REMARK 500    LYS H  46       17.68    -54.35
REMARK 500    SER H  51      -32.61    -34.16
REMARK 500    VAL I  39      -60.13   -127.54
REMARK 500    ASN L  10       37.98    -99.53
REMARK 500    THR N  10       32.08   -140.63
REMARK 500    MET N  69      -65.72   -106.57
REMARK 500    ASP N  91     -168.23   -172.25
REMARK 500    GLU N 119     -133.29     57.63
REMARK 500    THR N 218       41.20   -140.08
REMARK 500    LEU N 483      -69.25    -94.97
REMARK 500    ASN N 491       76.37   -154.19
REMARK 500    GLU O  60      -57.90    167.90
REMARK 500    ASN O  92       75.97     47.60
REMARK 500    TYR O 113      -65.96   -136.35
REMARK 500    ASP O 158      -92.58   -145.73
REMARK 500    SER P  65      -65.27   -103.84
REMARK 500    GLU P 128     -116.46   -101.95
REMARK 500    HIS P 232       53.41   -164.31
REMARK 500
REMARK 500 THIS ENTRY HAS      83 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 PRO F   93     HIS F   94                  132.02
REMARK 500 PRO S   93     HIS S   94                  131.78
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 304         0.07    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    FME B   1        23.2      L          L   OUTSIDE RANGE
REMARK 500    TRP B  65        21.8      L          L   OUTSIDE RANGE
REMARK 500    ASN B  92        13.4      L          L   OUTSIDE RANGE
REMARK 500    SER D   4        23.6      L          L   OUTSIDE RANGE
REMARK 500    HIS F  94        18.2      L          L   OUTSIDE RANGE
REMARK 500    GLN F  95        23.4      L          L   OUTSIDE RANGE
REMARK 500    ALA G   3        23.8      L          L   OUTSIDE RANGE
REMARK 500    ASP G   7        21.0      L          L   OUTSIDE RANGE
REMARK 500    HIS G   8        19.9      L          L   OUTSIDE RANGE
REMARK 500    ILE H   8        23.9      L          L   OUTSIDE RANGE
REMARK 500    TRP O  65        20.7      L          L   OUTSIDE RANGE
REMARK 500    ASN O  92        11.4      L          L   OUTSIDE RANGE
REMARK 500    HIS S  94        23.7      L          L   OUTSIDE RANGE
REMARK 500    ALA T   3        21.5      L          L   OUTSIDE RANGE
REMARK 500    HIS T   8        21.4      L          L   OUTSIDE RANGE
REMARK 500    THR V   2        18.9      L          L   OUTSIDE RANGE
REMARK 500    HIS W  57        22.5      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 L4359        DISTANCE =  5.03 ANGSTROMS
REMARK 525    HOH Y4638        DISTANCE =  5.07 ANGSTROMS
REMARK 525    HOH J4729        DISTANCE =  6.13 ANGSTROMS
REMARK 525    HOH K4945        DISTANCE =  5.21 ANGSTROMS
REMARK 525    HOH I4813        DISTANCE =  6.53 ANGSTROMS
REMARK 525    HOH I4876        DISTANCE =  7.78 ANGSTROMS
REMARK 525    HOH U4588        DISTANCE =  5.35 ANGSTROMS
REMARK 525    HOH G4678        DISTANCE =  7.09 ANGSTROMS
REMARK 525    HOH G4838        DISTANCE =  7.76 ANGSTROMS
REMARK 525    HOH T4897        DISTANCE =  6.97 ANGSTROMS
REMARK 525    HOH P4422        DISTANCE =  8.37 ANGSTROMS
REMARK 525    HOH A4246        DISTANCE =  5.46 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                             HEA N 516  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1  NO N 520   N
REMARK 620 2 HEA N 516   NA   83.6
REMARK 620 3 HEA N 516   NB   95.2  88.9
REMARK 620 4 HEA N 516   NC   93.7 177.3  91.7
REMARK 620 5 HEA N 516   ND   86.5  91.7 178.3  87.9
REMARK 620 6 HIS N 376   NE2 171.8  88.3  86.2  94.3  92.2
REMARK 620 7  NO N 520   O    16.4  76.9 109.7 100.4  71.9 157.8
REMARK 620 N                    1     2     3     4     5     6
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  NO A 520   N
REMARK 620 2 HEA A 516   NA   85.4
REMARK 620 3 HEA A 516   NB   95.3  87.6
REMARK 620 4 HEA A 516   NC   93.4 177.7  90.5
REMARK 620 5 HEA A 516   ND   86.1  94.0 177.9  87.8
REMARK 620 6 HIS A 376   NE2 172.4  88.2  88.5  93.1  90.2
REMARK 620 7  NO A 520   O    18.9  78.2 112.1 101.2  69.5 154.5
REMARK 620 N                    1     2     3     4     5     6
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 291   NE2
REMARK 620 2 HIS A 240   ND1 152.5
REMARK 620 3 HIS A 290   NE2  96.1 107.6
REMARK 620 4  NO A 520   O    90.2  96.5 105.7
REMARK 620 N                    1     2     3
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 378   NE2
REMARK 620 2 HEA A 515   NA   86.5
REMARK 620 3 HEA A 515   NB   88.1  89.0
REMARK 620 4 HEA A 515   NC   88.5 174.9  90.0
REMARK 620 5 HEA A 515   ND   93.5  92.4 178.0  88.7
REMARK 620 6 HIS A  61   NE2 176.6  92.7  88.6  92.2  89.9
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 291   NE2 153.5
REMARK 620 3 HIS N 290   NE2 105.1  97.6
REMARK 620 4  NO N 520   O    94.5  92.6 105.2
REMARK 620 N                    1     2     3
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   92.7
REMARK 620 3 HEA N 515   NB   86.5  90.1
REMARK 620 4 HEA N 515   NC   89.5 177.7  89.5
REMARK 620 5 HEA N 515   ND   91.6  91.0 177.8  89.4
REMARK 620 6 HIS N 378   NE2 175.4  85.9  89.1  91.8  92.8
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CUA O 228  CU2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 204   ND1
REMARK 620 2 CUA O 228  CU1  162.9
REMARK 620 3 CYS O 200   SG  115.9  59.6
REMARK 620 4 CYS O 196   SG  125.2  58.0 117.4
REMARK 620 5 GLU O 198   O    84.1 112.8 102.5  96.2
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CUA B 228  CU2
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 204   ND1
REMARK 620 2 CUA B 228  CU1  164.4
REMARK 620 3 CYS B 200   SG  117.6  60.1
REMARK 620 4 CYS B 196   SG  124.8  56.8 116.5
REMARK 620 5 GLU B 198   O    83.2 112.4 103.2  94.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CUA B 228  CU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 161   ND1
REMARK 620 2 CUA B 228  CU2  132.8
REMARK 620 3 CYS B 196   SG  117.1  57.7
REMARK 620 4 MET B 207   SD   98.7 127.0 115.3
REMARK 620 5 CYS B 200   SG  103.1  55.3 112.7 108.5
REMARK 620 N                    1     2     3     4
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 ASP A 369   OD1
REMARK 620 2 GLU B 198   OE1  85.3
REMARK 620 3 HOH B2268   O    93.7  91.8
REMARK 620 4 HOH B2267   O    95.0  84.2 170.1
REMARK 620 5 HOH B2266   O   177.0  92.4  84.5  86.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CUA O 228  CU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS O 161   ND1
REMARK 620 2 CUA O 228  CU2  132.1
REMARK 620 3 CYS O 196   SG  117.4  56.4
REMARK 620 4 CYS O 200   SG  104.3  54.3 110.5
REMARK 620 5 MET O 207   SD   99.2 127.5 114.5 110.0
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG N 518  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP N 369   OD1
REMARK 620 2 HOH O3267   O    93.3
REMARK 620 3 HOH O3266   O   175.4  88.5
REMARK 620 4 GLU O 198   OE1  85.3  82.9  90.7
REMARK 620 5 HOH O3268   O    91.9 172.5  85.9  92.1
REMARK 620 N                    1     2     3     4
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 HOH A2258   O
REMARK 620 2 GLU A  40   OE1 175.5
REMARK 620 3 GLY A  45   O    86.7  95.4
REMARK 620 4 SER A 441   O    96.2  86.1 120.8
REMARK 620 5 GLU A  40   O    89.5  86.0 124.6 114.5
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              NA N 519  NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH N3258   O
REMARK 620 2 GLU N  40   OE1 177.1
REMARK 620 3 GLY N  45   O    83.0  96.0
REMARK 620 4 SER N 441   O    95.9  87.0 120.1
REMARK 620 5 GLU N  40   O    87.6  90.8 124.6 115.1
REMARK 620 N                    1     2     3     4
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  82   SG  106.0
REMARK 620 3 CYS F  85   SG  106.3 109.1
REMARK 620 4 CYS F  62   SG  116.2 108.5 110.4
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  85   SG  107.9
REMARK 620 3 CYS S  62   SG  117.0 110.7
REMARK 620 4 CYS S  82   SG  104.6 109.6 106.8
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 HEA A 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA A 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO A 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL A 521
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV A 522
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 PSC B 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD B 1085
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD C 525
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK C 264
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV C 267
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV C 268
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL C 270
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD C 271
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL D 523
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 99
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK G 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL G 269
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU G 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK G 1263
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD J 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL L 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV M 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU M 526
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA N 515
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEA N 516
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO N 520
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU N 517
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 518
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA N 519
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL N 1522
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV N 1524
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV N 1266
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA O 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD O 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL O 1521
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD P 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK P 1264
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK P 1265
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV P 1267
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV P 1268
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL P 1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD P 1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU P 1272
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL Q 1523
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSC R 1229
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN S 99
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK T 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL T 1269
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD W 1059
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
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: 1OCC   RELATED DB: PDB
REMARK 900 RELATED ID: 1OCZ   RELATED DB: PDB
REMARK 900 RELATED ID: 1OCO   RELATED DB: PDB
REMARK 900 RELATED ID: 1OCR   RELATED DB: PDB
REMARK 900 RELATED ID: 2OCC   RELATED DB: PDB
REMARK 900 RELATED ID: 1V54   RELATED DB: PDB
REMARK 900 RELATED ID: 1V55   RELATED DB: PDB
REMARK 900 RELATED ID: 2DYR   RELATED DB: PDB
REMARK 900 RELATED ID: 2DYS   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: 2EIM   RELATED DB: PDB
REMARK 900 RELATED ID: 2EIN   RELATED DB: PDB
REMARK 900 RELATED ID: 2ZXW   RELATED DB: PDB
REMARK 900 RELATED ID: 3ABK   RELATED DB: PDB
REMARK 900 RELATED ID: 3ABL   RELATED DB: PDB
REMARK 900 RELATED ID: 3ABM   RELATED DB: PDB
REMARK 900 RELATED ID: 3AG1   RELATED DB: PDB
REMARK 900 RELATED ID: 3AG2   RELATED DB: PDB
REMARK 900 RELATED ID: 3AG4   RELATED DB: PDB
DBREF  3AG3 A    1   514  UNP    P00396   COX1_BOVIN       1    514
DBREF  3AG3 B    1   227  UNP    P68530   COX2_BOVIN       1    227
DBREF  3AG3 C    1   261  UNP    P00415   COX3_BOVIN       1    261
DBREF  3AG3 D    1   147  UNP    P00423   COX41_BOVIN     23    169
DBREF  3AG3 E    1   109  UNP    P00426   COX5A_BOVIN     44    152
DBREF  3AG3 F    1    98  UNP    P00428   COX5B_BOVIN     32    129
DBREF  3AG3 G    1    85  UNP    P07471   CX6A2_BOVIN     13     97
DBREF  3AG3 H    1    85  UNP    P00429   CX6B1_BOVIN      2     86
DBREF  3AG3 I    1    73  UNP    P04038   COX6C_BOVIN      2     74
DBREF  3AG3 J    1    59  UNP    P07470   CX7A1_BOVIN     22     80
DBREF  3AG3 K    1    56  UNP    P13183   COX7B_BOVIN     25     80
DBREF  3AG3 L    1    47  UNP    P00430   COX7C_BOVIN     17     63
DBREF  3AG3 M    1    46  UNP    P10175   COX8B_BOVIN     25     70
DBREF  3AG3 N    1   514  UNP    P00396   COX1_BOVIN       1    514
DBREF  3AG3 O    1   227  UNP    P68530   COX2_BOVIN       1    227
DBREF  3AG3 P    1   261  UNP    P00415   COX3_BOVIN       1    261
DBREF  3AG3 Q    1   147  UNP    P00423   COX41_BOVIN     23    169
DBREF  3AG3 R    1   109  UNP    P00426   COX5A_BOVIN     44    152
DBREF  3AG3 S    1    98  UNP    P00428   COX5B_BOVIN     32    129
DBREF  3AG3 T    1    85  UNP    P07471   CX6A2_BOVIN     13     97
DBREF  3AG3 U    1    85  UNP    P00429   CX6B1_BOVIN      2     86
DBREF  3AG3 V    1    73  UNP    P04038   COX6C_BOVIN      2     74
DBREF  3AG3 W    1    59  UNP    P07470   CX7A1_BOVIN     22     80
DBREF  3AG3 X    1    56  UNP    P13183   COX7B_BOVIN     25     80
DBREF  3AG3 Y    1    47  UNP    P00430   COX7C_BOVIN     17     63
DBREF  3AG3 Z    1    46  UNP    P10175   COX8B_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 3AG3 FME A    1  MET  N-FORMYLMETHIONINE
MODRES 3AG3 FME B    1  MET  N-FORMYLMETHIONINE
MODRES 3AG3 TPO G   11  THR  PHOSPHOTHREONINE
MODRES 3AG3 SAC I    1  SER  N-ACETYL-SERINE
MODRES 3AG3 FME N    1  MET  N-FORMYLMETHIONINE
MODRES 3AG3 FME O    1  MET  N-FORMYLMETHIONINE
MODRES 3AG3 TPO T   11  THR  PHOSPHOTHREONINE
MODRES 3AG3 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    HEA  A 515      60
HET    HEA  A 516      60
HET     NO  A 520       2
HET     CU  A 517       1
HET     MG  A 518       1
HET     NA  A 519       1
HET    TGL  A 521      63
HET    PGV  A 522      51
HET    CUA  B 228       2
HET    PSC  B 229      52
HET    CHD  B1085      29
HET    UNX  C 262       1
HET    CHD  C 525      29
HET    PEK  C 264      53
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    PEK  G 265      53
HET    CDL  G 269     100
HET    DMU  G 272      33
HET    PEK  G1263      53
HET    CHD  J  60      29
HET    TGL  L 522      63
HET    PGV  M 524      51
HET    DMU  M 526      33
HET    HEA  N 515      60
HET    HEA  N 516      60
HET     NO  N 520       2
HET     CU  N 517       1
HET     MG  N 518       1
HET     NA  N 519       1
HET    TGL  N1522      63
HET    PGV  N1524      51
HET    PGV  N1266      51
HET    CUA  O 228       2
HET    CHD  O 229      29
HET    TGL  O1521      63
HET    UNX  P 262       1
HET    CHD  P1525      29
HET    PEK  P1264      53
HET    PEK  P1265      53
HET    PGV  P1267      51
HET    PGV  P1268      51
HET    CDL  P1270     100
HET    CHD  P1271      29
HET    DMU  P1272      33
HET    TGL  Q1523      63
HET    PSC  R1229      52
HET     ZN  S  99       1
HET    PEK  T 263      53
HET    CDL  T1269     100
HET    CHD  W1059      29
HET    DMU  Z1526      33
HETNAM     FME N-FORMYLMETHIONINE
HETNAM     TPO PHOSPHOTHREONINE
HETNAM     SAC N-ACETYL-SERINE
HETNAM     HEA HEME-A
HETNAM      NO NITRIC OXIDE
HETNAM      CU COPPER (II) ION
HETNAM      MG MAGNESIUM ION
HETNAM      NA SODIUM ION
HETNAM     TGL TRISTEAROYLGLYCEROL
HETNAM     PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)
HETNAM   2 PGV  PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-
HETNAM   3 PGV  OCTADEC-11-ENOATE
HETNAM     CUA DINUCLEAR COPPER ION
HETNAM     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     CHD CHOLIC ACID
HETNAM     UNX UNKNOWN ATOM OR ION
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
HETNAM      ZN ZINC ION
HETNAM     DMU DECYL-BETA-D-MALTOPYRANOSIDE
HETSYN     TPO PHOSPHONOTHREONINE
HETSYN      NO NITROGEN MONOXIDE
HETSYN     TGL TRIACYLGLYCEROL
HETSYN     PGV PHOSPHATIDYLGLYCEROL, 2-VACCENOYL-1-PALMITOYL-SN-
HETSYN   2 PGV  GLYCEROL-3-PHOSPHOGLYCEROL
HETSYN     PSC PHOSPHATIDYLCHOLINE, 2-LINOLEOYL-1-PALMITOYL-SN-
HETSYN   2 PSC  GYCEROL-3-PHOSPHOCHOLINE
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
HETSYN     DMU DECYLMALTOSIDE
FORMUL   1  FME    4(C6 H11 N O3 S)
FORMUL   7  TPO    2(C4 H10 N O6 P)
FORMUL   9  SAC    2(C5 H9 N O4)
FORMUL  27  HEA    4(C49 H56 FE N4 O6)
FORMUL  29   NO    2(N O)
FORMUL  30   CU    2(CU 2+)
FORMUL  31   MG    2(MG 2+)
FORMUL  32   NA    2(NA 1+)
FORMUL  33  TGL    6(C57 H110 O6)
FORMUL  34  PGV    8(C40 H77 O10 P)
FORMUL  35  CUA    2(CU2)
FORMUL  36  PSC    2(C42 H81 N O8 P 1+)
FORMUL  37  CHD    8(C24 H40 O5)
FORMUL  38  UNX    2(X)
FORMUL  40  PEK    6(C43 H78 N O8 P)
FORMUL  43  CDL    4(C81 H156 O17 P2 2-)
FORMUL  46   ZN    2(ZN 2+)
FORMUL  49  DMU    4(C22 H42 O11)
FORMUL  83  HOH   *1743(H2 O)
HELIX    1   1 FME A    1  LEU A    7  1                                   7
HELIX    2   2 ASN A   11  GLY A   42  1                                  32
HELIX    3   3 ASP A   50  PHE A   68  1                                  19
HELIX    4   4 MET A   69  ILE A   75  1                                   7
HELIX    5   5 GLY A   77  ILE A   87  1                                  11
HELIX    6   6 PHE A   94  LEU A  104  1                                  11
HELIX    7   7 LEU A  104  VAL A  118  1                                  15
HELIX    8   8 ALA A  141  MET A  171  1                                  31
HELIX    9   9 SER A  177  THR A  181  5                                   5
HELIX   10  10 PRO A  182  LEU A  215  1                                  34
HELIX   11  11 ASP A  221  GLY A  225  5                                   5
HELIX   12  12 ASP A  227  SER A  262  1                                  36
HELIX   13  13 GLY A  269  GLY A  284  1                                  16
HELIX   14  14 PHE A  285  ILE A  286  5                                   2
HELIX   15  15 VAL A  287  MET A  292  5                                   6
HELIX   16  16 ASP A  298  ILE A  312  1                                  15
HELIX   17  17 ILE A  312  HIS A  328  1                                  17
HELIX   18  18 SER A  335  ASN A  360  1                                  26
HELIX   19  19 ASN A  360  HIS A  368  1                                   9
HELIX   20  20 THR A  370  LEU A  381  1                                  12
HELIX   21  21 LEU A  381  GLY A  402  1                                  22
HELIX   22  22 ASN A  406  PHE A  426  1                                  21
HELIX   23  23 PRO A  427  SER A  434  1                                   8
HELIX   24  24 PRO A  444  ALA A  446  5                                   3
HELIX   25  25 TYR A  447  LYS A  479  1                                  33
HELIX   26  26 LEU A  487  LEU A  495  5                                   9
HELIX   27  27 SER B   14  LEU B   46  1                                  33
HELIX   28  28 GLU B   60  GLU B   89  1                                  30
HELIX   29  29 PRO B  124  LEU B  128  5                                   5
HELIX   30  30 PRO B  166  GLY B  169  5                                   4
HELIX   31  31 ASN B  203  MET B  207  5                                   5
HELIX   32  32 PRO B  215  MET B  226  1                                  12
HELIX   33  33 PRO C   15  PHE C   37  1                                  23
HELIX   34  34 MET C   40  THR C   66  1                                  27
HELIX   35  35 THR C   72  ALA C  107  1                                  36
HELIX   36  36 THR C  109  GLY C  113  5                                   5
HELIX   37  37 GLU C  128  GLU C  153  1                                  26
HELIX   38  38 ASP C  155  ALA C  184  1                                  30
HELIX   39  39 ASP C  190  LYS C  224  1                                  35
HELIX   40  40 HIS C  232  ILE C  256  1                                  25
HELIX   41  41 LYS D    7  TYR D   11  5                                   5
HELIX   42  42 SER D   34  GLU D   44  1                                  11
HELIX   43  43 LYS D   45  ALA D   46  5                                   2
HELIX   44  44 SER D   47  LEU D   51  5                                   5
HELIX   45  45 SER D   52  PHE D   64  1                                  13
HELIX   46  46 SER D   67  ASN D   72  1                                   6
HELIX   47  47 ASN D   76  VAL D  103  1                                  28
HELIX   48  48 PRO D  108  PHE D  111  5                                   4
HELIX   49  49 GLU D  112  MET D  126  1                                  15
HELIX   50  50 PHE D  134  ALA D  136  5                                   3
HELIX   51  51 THR E    7  LYS E   21  1                                  15
HELIX   52  52 ASP E   25  VAL E   37  1                                  13
HELIX   53  53 GLU E   44  LEU E   58  1                                  15
HELIX   54  54 ASP E   60  GLY E   76  1                                  17
HELIX   55  55 GLU E   80  GLY E   97  1                                  18
HELIX   56  56 THR F    8  ALA F   13  1                                   6
HELIX   57  57 THR F   14  LYS F   26  1                                  13
HELIX   58  58 GLY G   12  LEU G   23  1                                  12
HELIX   59  59 LEU G   23  TRP G   36  1                                  14
HELIX   60  60 GLN H   25  LYS H   46  1                                  22
HELIX   61  61 ASP H   49  VAL H   52  5                                   4
HELIX   62  62 CYS H   53  CYS H   64  1                                  12
HELIX   63  63 PRO H   65  GLY H   79  1                                  15
HELIX   64  64 GLY I   11  VAL I   39  1                                  29
HELIX   65  65 VAL I   39  ASN I   53  1                                  15
HELIX   66  66 ASP I   55  ALA I   66  1                                  12
HELIX   67  67 ARG J    4  GLU J   14  1                                  11
HELIX   68  68 PRO J   19  LYS J   23  5                                   5
HELIX   69  69 GLY J   25  SER J   54  1                                  30
HELIX   70  70 ASP K    8  GLN K   35  1                                  28
HELIX   71  71 ASN L   17  LYS L   46  1                                  30
HELIX   72  72 SER M   11  HIS M   36  1                                  26
HELIX   73  73 HIS M   36  LYS M   42  1                                   7
HELIX   74  74 FME N    1  LEU N    7  1                                   7
HELIX   75  75 ASN N   11  LEU N   41  1                                  31
HELIX   76  76 ASP N   50  PHE N   68  1                                  19
HELIX   77  77 MET N   69  ILE N   75  1                                   7
HELIX   78  78 GLY N   76  ILE N   87  1                                  12
HELIX   79  79 PHE N   94  LEU N  104  1                                  11
HELIX   80  80 LEU N  104  VAL N  118  1                                  15
HELIX   81  81 ALA N  141  MET N  171  1                                  31
HELIX   82  82 SER N  177  THR N  181  5                                   5
HELIX   83  83 PRO N  182  LEU N  215  1                                  34
HELIX   84  84 ASP N  221  GLY N  225  5                                   5
HELIX   85  85 ASP N  227  SER N  262  1                                  36
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  MET N  292  5                                   6
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  ASN N  360  1                                  26
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  SER N  434  1                                  29
HELIX   96  96 PRO N  444  ALA N  446  5                                   3
HELIX   97  97 TYR N  447  LYS N  479  1                                  33
HELIX   98  98 LEU N  487  LEU N  495  5                                   9
HELIX   99  99 SER O   14  LEU O   46  1                                  33
HELIX  100 100 GLU O   60  GLU O   89  1                                  30
HELIX  101 101 PRO O  124  LEU O  128  5                                   5
HELIX  102 102 PRO O  166  GLY O  169  5                                   4
HELIX  103 103 ASN O  203  MET O  207  5                                   5
HELIX  104 104 PRO O  215  MET O  226  1                                  12
HELIX  105 105 PRO P   15  PHE P   37  1                                  23
HELIX  106 106 MET P   40  THR P   66  1                                  27
HELIX  107 107 THR P   72  ALA P  107  1                                  36
HELIX  108 108 THR P  109  GLY P  113  5                                   5
HELIX  109 109 GLU P  128  GLU P  153  1                                  26
HELIX  110 110 ASP P  155  ALA P  184  1                                  30
HELIX  111 111 ASP P  190  LYS P  224  1                                  35
HELIX  112 112 HIS P  232  ILE P  256  1                                  25
HELIX  113 113 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  ALA R   75  1                                  16
HELIX  126 126 GLU R   80  GLY R   97  1                                  18
HELIX  127 127 THR S    8  ALA S   13  1                                   6
HELIX  128 128 THR S   14  LYS S   26  1                                  13
HELIX  129 129 GLY T   12  LEU T   23  1                                  12
HELIX  130 130 LEU T   23  TRP T   36  1                                  14
HELIX  131 131 GLN U   25  LYS U   46  1                                  22
HELIX  132 132 ASP U   49  VAL U   52  5                                   4
HELIX  133 133 CYS U   53  CYS U   64  1                                  12
HELIX  134 134 PRO U   65  GLY U   79  1                                  15
HELIX  135 135 GLY V   11  VAL V   39  1                                  29
HELIX  136 136 VAL V   39  ASN V   53  1                                  15
HELIX  137 137 ASP V   55  ALA V   66  1                                  12
HELIX  138 138 ARG W    4  GLU W   14  1                                  11
HELIX  139 139 GLY W   25  SER W   54  1                                  30
HELIX  140 140 ASP X    8  GLN X   35  1                                  28
HELIX  141 141 ASN Y   17  LYS Y   47  1                                  31
HELIX  142 142 SER Z   11  HIS Z   36  1                                  26
HELIX  143 143 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  PHE F  72   N  VAL F  58
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  LYS B  98   O  GLU B 109
SHEET    4   C 5 ILE B 150  SER B 156  1  O  ARG B 151   N  LEU B  95
SHEET    5   C 5 ASN B 180  LEU B 184 -1  O  ASN B 180   N  VAL B 154
SHEET    1   D 3 VAL B 142  PRO B 145  0
SHEET    2   D 3 ILE B 209  VAL B 214  1  O  VAL B 210   N  VAL B 142
SHEET    3   D 3 GLY B 190  GLY B 194 -1  N  GLY B 194   O  ILE B 209
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  SER F  51  0
SHEET    2   G 3 HIS F  88  PRO F  93  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  PHE S  72   N  VAL S  58
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  LYS O  98   O  GLU O 109
SHEET    4   J 5 ILE O 150  SER O 156  1  O  ARG O 151   N  LEU O  95
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  VAL O 142
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  SER S  51  0
SHEET    2   N 3 HIS S  88  PRO S  93  1  O  LYS S  90   N  VAL S  49
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  2.10
SSBOND   2 CYS H   39    CYS H   53                          1555   1555  2.06
SSBOND   3 CYS U   29    CYS U   64                          1555   1555  2.11
SSBOND   4 CYS U   39    CYS U   53                          1555   1555  2.08
LINK         NE2 HIS A 240                 CE2 TYR A 244     1555   1555  1.35
LINK         NE2 HIS N 240                 CE2 TYR N 244     1555   1555  1.38
LINK         C   FME A   1                 N   PHE A   2     1555   1555  1.33
LINK         C   FME B   1                 N   ALA B   2     1555   1555  1.33
LINK         C   GLY G  10                 N   TPO G  11     1555   1555  1.34
LINK         C   TPO G  11                 N   GLY G  12     1555   1555  1.39
LINK         C   SAC I   1                 N   THR I   2     1555   1555  1.31
LINK         C   FME N   1                 N   PHE N   2     1555   1555  1.33
LINK         C   FME O   1                 N   ALA O   2     1555   1555  1.31
LINK         C   GLY T  10                 N   TPO T  11     1555   1555  1.33
LINK         C   TPO T  11                 N   GLY T  12     1555   1555  1.39
LINK         C   SAC V   1                 N   THR V   2     1555   1555  1.34
LINK        FE   HEA N 516                 N    NO N 520     1555   1555  1.72
LINK        FE   HEA A 516                 N    NO A 520     1555   1555  1.76
LINK         NE2 HIS A 291                CU    CU A 517     1555   1555  1.95
LINK         NE2 HIS A 378                FE   HEA A 515     1555   1555  1.96
LINK         ND1 HIS N 240                CU    CU N 517     1555   1555  1.96
LINK         NE2 HIS N  61                FE   HEA N 515     1555   1555  1.98
LINK         NE2 HIS N 378                FE   HEA N 515     1555   1555  1.99
LINK         NE2 HIS N 291                CU    CU N 517     1555   1555  2.00
LINK         ND1 HIS A 240                CU    CU A 517     1555   1555  2.00
LINK         ND1 HIS O 204                CU2  CUA O 228     1555   1555  2.01
LINK         NE2 HIS A  61                FE   HEA A 515     1555   1555  2.01
LINK         NE2 HIS A 290                CU    CU A 517     1555   1555  2.02
LINK         NE2 HIS N 290                CU    CU N 517     1555   1555  2.03
LINK         ND1 HIS B 204                CU2  CUA B 228     1555   1555  2.05
LINK         ND1 HIS B 161                CU1  CUA B 228     1555   1555  2.06
LINK         OD1 ASP A 369                MG    MG A 518     1555   1555  2.06
LINK         ND1 HIS O 161                CU1  CUA O 228     1555   1555  2.11
LINK         OD1 ASP N 369                MG    MG N 518     1555   1555  2.13
LINK         OE1 GLU B 198                MG    MG A 518     1555   1555  2.17
LINK        MG    MG N 518                 O   HOH O3267     1555   1555  2.21
LINK        MG    MG N 518                 O   HOH O3266     1555   1555  2.21
LINK        NA    NA A 519                 O   HOH A2258     1555   1555  2.22
LINK         OE1 GLU O 198                MG    MG N 518     1555   1555  2.22
LINK        MG    MG A 518                 O   HOH B2268     1555   1555  2.22
LINK         SG  CYS O 200                CU2  CUA O 228     1555   1555  2.23
LINK        MG    MG A 518                 O   HOH B2267     1555   1555  2.23
LINK        NA    NA N 519                 O   HOH N3258     1555   1555  2.25
LINK         OE1 GLU N  40                NA    NA N 519     1555   1555  2.27
LINK         SG  CYS B 200                CU2  CUA B 228     1555   1555  2.27
LINK        MG    MG A 518                 O   HOH B2266     1555   1555  2.27
LINK         OE1 GLU A  40                NA    NA A 519     1555   1555  2.28
LINK        MG    MG N 518                 O   HOH O3268     1555   1555  2.29
LINK         O   GLY N  45                NA    NA N 519     1555   1555  2.29
LINK         NE2 HIS N 376                FE   HEA N 516     1555   1555  2.29
LINK         SG  CYS B 196                CU1  CUA B 228     1555   1555  2.29
LINK         NE2 HIS A 376                FE   HEA A 516     1555   1555  2.29
LINK         SG  CYS O 196                CU2  CUA O 228     1555   1555  2.30
LINK         SG  CYS F  60                ZN    ZN F  99     1555   1555  2.30
LINK         O   GLY A  45                NA    NA A 519     1555   1555  2.31
LINK         SG  CYS S  60                ZN    ZN S  99     1555   1555  2.31
LINK         SG  CYS B 196                CU2  CUA B 228     1555   1555  2.32
LINK         O   SER A 441                NA    NA A 519     1555   1555  2.32
LINK         O   SER N 441                NA    NA N 519     1555   1555  2.32
LINK         SG  CYS O 196                CU1  CUA O 228     1555   1555  2.34
LINK         O   GLU N  40                NA    NA N 519     1555   1555  2.34
LINK         SG  CYS F  82                ZN    ZN F  99     1555   1555  2.34
LINK         SG  CYS S  85                ZN    ZN S  99     1555   1555  2.35
LINK         SG  CYS S  62                ZN    ZN S  99     1555   1555  2.35
LINK         SG  CYS F  85                ZN    ZN F  99     1555   1555  2.36
LINK         O   GLU A  40                NA    NA A 519     1555   1555  2.36
LINK         SG  CYS O 200                CU1  CUA O 228     1555   1555  2.37
LINK         SD  MET B 207                CU1  CUA B 228     1555   1555  2.37
LINK         SG  CYS F  62                ZN    ZN F  99     1555   1555  2.38
LINK         SD  MET O 207                CU1  CUA O 228     1555   1555  2.39
LINK         SG  CYS B 200                CU1  CUA B 228     1555   1555  2.39
LINK         SG  CYS S  82                ZN    ZN S  99     1555   1555  2.39
LINK         O   GLU O 198                CU2  CUA O 228     1555   1555  2.44
LINK         O    NO N 520                CU    CU N 517     1555   1555  2.45
LINK         O    NO A 520                CU    CU A 517     1555   1555  2.50
LINK         O   GLU B 198                CU2  CUA B 228     1555   1555  2.54
LINK        FE   HEA A 516                 O    NO A 520     1555   1555  2.66
LINK        FE   HEA N 516                 O    NO N 520     1555   1555  2.69
CISPEP   1 PRO A  130    PRO A  131          0         0.17
CISPEP   2 CYS A  498    PRO A  499          0        -2.25
CISPEP   3 GLN B  103    TRP B  104          0       -12.21
CISPEP   4 TRP C  116    PRO C  117          0        -6.61
CISPEP   5 PRO N  130    PRO N  131          0         2.58
CISPEP   6 CYS N  498    PRO N  499          0        -6.10
CISPEP   7 GLN O  103    TRP O  104          0        -2.92
CISPEP   8 TRP P  116    PRO P  117          0       -10.94
SITE     1 AC1 29 THR A  31  SER A  34  ILE A  37  ARG A  38
SITE     2 AC1 29 TYR A  54  VAL A  58  HIS A  61  ALA A  62
SITE     3 AC1 29 MET A  65  VAL A  70  ILE A  73  GLY A 125
SITE     4 AC1 29 TRP A 126  TYR A 371  PHE A 377  HIS A 378
SITE     5 AC1 29 LEU A 381  SER A 382  VAL A 386  PHE A 393
SITE     6 AC1 29 MET A 417  PHE A 425  GLN A 428  ARG A 438
SITE     7 AC1 29 ARG A 439  VAL A 465  HOH A2045  HOH A2283
SITE     8 AC1 29 HOH A2700
SITE     1 AC2 30 TRP A 126  TRP A 236  VAL A 243  TYR A 244
SITE     2 AC2 30 ILE A 247  HIS A 290  HIS A 291  THR A 309
SITE     3 AC2 30 ILE A 312  THR A 316  GLY A 317  GLY A 352
SITE     4 AC2 30 GLY A 355  ILE A 356  LEU A 358  ALA A 359
SITE     5 AC2 30 ASP A 364  HIS A 368  VAL A 373  HIS A 376
SITE     6 AC2 30 PHE A 377  VAL A 380  LEU A 381  ARG A 438
SITE     7 AC2 30  NO A 520  HOH A2081  HOH A2183  HOH A2272
SITE     8 AC2 30 HOH A2341  ILE B  34
SITE     1 AC3  5 HIS A 240  HIS A 290  HIS A 291  HEA A 516
SITE     2 AC3  5  CU A 517
SITE     1 AC4  4 HIS A 240  HIS A 290  HIS A 291   NO A 520
SITE     1 AC5  6 HIS A 368  ASP A 369  GLU B 198  HOH B2266
SITE     2 AC5  6 HOH B2267  HOH B2268
SITE     1 AC6  4 GLU A  40  GLY A  45  SER A 441  HOH A2258
SITE     1 AC7 11 ASN A 422  PHE A 426  HIS A 429  PHE A 430
SITE     2 AC7 11 LEU A 433  LEU B   7  LEU B  28  PHE B  32
SITE     3 AC7 11 SER B  35  LEU B  39  HOH D2606
SITE     1 AC8 15 PHE A  94  PRO A  95  ARG A  96  MET A  97
SITE     2 AC8 15 HOH A2289  HIS C   9  ASN C  50  TRP C  57
SITE     3 AC8 15 TRP C  58  GLU C  64  HIS C  71  GLY C  82
SITE     4 AC8 15 SER C  89  PEK C 264  HOH C2085
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 20 PHE A 321  LEU A 324  ALA A 325  HIS A 328
SITE     2 BC1 20 HOH A4197  ILE B  41  MET B  45  HIS B  52
SITE     3 BC1 20 MET B  56  ASP B  57  GLU B  60  LEU B  68
SITE     4 BC1 20 HOH B2042  ASP E   8  PHE E  11  ASP E  40
SITE     5 BC1 20 LEU E  41  HOH E4220  ARG I  10  ALA I  14
SITE     1 BC2 11 MET A 271  GLN B  59  GLU B  62  THR B  63
SITE     2 BC2 11 THR B  66  HOH B2605  HOH B3446  PEK P1265
SITE     3 BC2 11 ARG T  14  ARG T  17  GLY T  22
SITE     1 BC3 11 HIS A 233  ASP A 300  THR A 301  TYR A 304
SITE     2 BC3 11 TRP C  99  HIS C 103  HOH C2155  HOH C4154
SITE     3 BC3 11 HOH C4321  HOH C4757  CDL T1269
SITE     1 BC4 16 HIS A 151  PGV A 522  HOH A4501  TYR C 181
SITE     2 BC4 16 TYR C 182  ALA C 184  PHE C 186  THR C 187
SITE     3 BC4 16 ILE C 188  PHE C 198  GLY C 202  THR G  68
SITE     4 BC4 16 PHE G  69  PHE G  70  HIS G  71  ASN G  76
SITE     1 BC5 18 MET C  54  VAL C  61  SER C  65  THR C  66
SITE     2 BC5 18 HIS C 207  ILE C 210  PHE C 214  ARG C 221
SITE     3 BC5 18 HIS C 226  PHE C 227  HIS C 231  HIS C 232
SITE     4 BC5 18 PHE C 233  GLY C 234  CDL C 270  HOH C2253
SITE     5 BC5 18 HOH C2559  HOH F2065
SITE     1 BC6  8 THR C  95  TRP C  99  TYR C 102  HIS C 103
SITE     2 BC6  8 HOH C4186  HOH C4756  HOH C4799  HOH C4819
SITE     1 BC7 14 MET C  51  TYR C  55  ARG C  59  ARG C  63
SITE     2 BC7 14 PHE C  67  THR C 213  PHE C 220  LYS C 224
SITE     3 BC7 14 HIS C 226  PGV C 267  HOH C2144  HOH C4373
SITE     4 BC7 14 HOH C4862  LYS J   8
SITE     1 BC8  4 ARG C 156  PHE C 164  LEU C 223  PHE J   1
SITE     1 BC9 12 TRP A 334  GLY A 343  PHE A 414  THR B  47
SITE     2 BC9 12 LYS B  49  HOH B2562  ARG D  73  THR D  75
SITE     3 BC9 12 GLU D  77  TRP D  78  VAL D  81  ARG I  16
SITE     1 CC1  4 CYS F  60  CYS F  62  CYS F  82  CYS F  85
SITE     1 CC2 13 LYS C 157  HIS C 158  GLN C 161  THR C 168
SITE     2 CC2 13 TYR C 172  ALA F   1  ARG G  17  GLY G  22
SITE     3 CC2 13 CDL G 269  SER N 279  GLN O  59  CHD O 229
SITE     4 CC2 13 HOH O4943
SITE     1 CC3 22 LEU C 127  LEU C 131  SER G  27  LEU G  30
SITE     2 CC3 22 CYS G  31  ASN G  34  LEU G  37  HIS G  38
SITE     3 CC3 22 ARG G  42  PEK G 265  HOH G4678  HOH G4810
SITE     4 CC3 22 HOH G4838  PHE N 282  ASP N 300  TYR N 304
SITE     5 CC3 22 SER N 307  ILE N 311  ALA O  77  LEU O  78
SITE     6 CC3 22 TYR O  85  CHD P1525
SITE     1 CC4  6 TRP C  34  MET C  40  SER G  61  GLY G  63
SITE     2 CC4  6 PHE G  69  HOH G4531
SITE     1 CC5 12 SER G   2  ALA G   3  LYS G   5  GLY G   6
SITE     2 CC5 12 HIS G   8  HOH G4952  LYS P  77  ARG P  80
SITE     3 CC5 12 TYR P  81  ILE P  84  VAL P 247  VAL P 248
SITE     1 CC6  5 TYR J  32  ARG J  33  MET J  36  THR J  37
SITE     2 CC6  5 LEU J  40
SITE     1 CC7 13 THR A  17  LEU A  20  LEU A  21  TRP A  25
SITE     2 CC7 13 LEU A 113  PHE A 400  ILE L  11  PRO L  12
SITE     3 CC7 13 SER L  14  ARG L  20  MET L  24  PHE L  29
SITE     4 CC7 13 SER L  31
SITE     1 CC8 17 ASN A 406  THR A 408  TRP A 409  PHE D  87
SITE     2 CC8 17 PHE K   9  HIS K  10  PRO M  12  GLN M  15
SITE     3 CC8 17 LEU M  19  SER M  20  HOH M2126  HOH M4279
SITE     4 CC8 17 HOH M4472  HOH M4523  HOH M4609  HOH M4849
SITE     5 CC8 17 HOH M4885
SITE     1 CC9  6 TRP D  98  LEU M  28  GLY M  31  TRP M  32
SITE     2 CC9  6 TYR M  35  HIS M  36
SITE     1 DC1 26 THR N  31  SER N  34  ILE N  37  ARG N  38
SITE     2 DC1 26 TYR N  54  VAL N  58  HIS N  61  ALA N  62
SITE     3 DC1 26 MET N  65  VAL N  70  ILE N  73  GLY N 125
SITE     4 DC1 26 TRP N 126  TYR N 371  PHE N 377  HIS N 378
SITE     5 DC1 26 SER N 382  PHE N 393  PHE N 425  GLN N 428
SITE     6 DC1 26 ARG N 438  ARG N 439  VAL N 465  HOH N3045
SITE     7 DC1 26 HOH N3283  HOH N3700
SITE     1 DC2 28 TRP N 126  TRP N 236  VAL N 243  TYR N 244
SITE     2 DC2 28 HIS N 290  HIS N 291  THR N 309  ILE N 312
SITE     3 DC2 28 THR N 316  GLY N 317  GLY N 352  GLY N 355
SITE     4 DC2 28 ILE N 356  LEU N 358  ALA N 359  ASP N 364
SITE     5 DC2 28 HIS N 368  VAL N 373  HIS N 376  PHE N 377
SITE     6 DC2 28 VAL N 380  LEU N 381  ARG N 438   NO N 520
SITE     7 DC2 28 HOH N3081  HOH N3183  HOH N3272  HOH N3341
SITE     1 DC3  5 HIS N 240  HIS N 290  HIS N 291  HEA N 516
SITE     2 DC3  5  CU N 517
SITE     1 DC4  4 HIS N 240  HIS N 290  HIS N 291   NO N 520
SITE     1 DC5  6 HIS N 368  ASP N 369  GLU O 198  HOH O3266
SITE     2 DC5  6 HOH O3267  HOH O3268
SITE     1 DC6  4 GLU N  40  GLY N  45  SER N 441  HOH N3258
SITE     1 DC7 14 THR N  17  LEU N  18  LEU N  20  TRP N  25
SITE     2 DC7 14 LEU N 113  PHE N 400  HOH N4836  PRO Y  12
SITE     3 DC7 14 PHE Y  13  SER Y  14  ARG Y  20  PHE Y  28
SITE     4 DC7 14 PHE Y  29  HOH Y4638
SITE     1 DC8 11 ASN N 406  THR N 408  TRP N 409  HOH N3126
SITE     2 DC8 11 HOH N4393  ALA Q  84  PHE Q  87  PHE X   9
SITE     3 DC8 11 HIS X  10  PRO Z  12  HOH Z4423
SITE     1 DC9 17 PHE N  94  PRO N  95  ARG N  96  MET N  97
SITE     2 DC9 17 HOH N3085  HOH N3289  HIS P   9  ALA P  24
SITE     3 DC9 17 ASN P  50  TRP P  57  TRP P  58  GLU P  64
SITE     4 DC9 17 HIS P  71  LEU P  79  GLY P  82  SER P  89
SITE     5 DC9 17 PEK P1264
SITE     1 EC1  6 HIS O 161  CYS O 196  GLU O 198  CYS O 200
SITE     2 EC1  6 HIS O 204  MET O 207
SITE     1 EC2 13 ARG G  14  ARG G  17  GLY G  22  PEK G 265
SITE     2 EC2 13 MET N 271  GLN O  59  GLU O  62  THR O  63
SITE     3 EC2 13 THR O  66  HOH O2446  HOH O3605  HOH O4248
SITE     4 EC2 13 HOH O4721
SITE     1 EC3 13 PHE N 346  ASN N 422  PHE N 426  PHE N 430
SITE     2 EC3 13 LEU N 433  LEU O   7  LEU O  28  VAL O  31
SITE     3 EC3 13 PHE O  32  SER O  35  LEU O  39  HOH O4440
SITE     4 EC3 13 HOH Q3606
SITE     1 EC4 11 CDL G 269  HIS N 233  ASP N 300  THR N 301
SITE     2 EC4 11 TYR N 304  TRP P  99  HIS P 103  PGV P1268
SITE     3 EC4 11 HOH P3155  HOH P4255  HOH P4413
SITE     1 EC5 19 HIS N 151  VAL N 155  LEU N 210  PGV N1266
SITE     2 EC5 19 HOH N4647  TYR P 181  TYR P 182  ALA P 184
SITE     3 EC5 19 PHE P 186  THR P 187  ILE P 188  PHE P 198
SITE     4 EC5 19 GLY P 202  THR T  68  PHE T  69  PHE T  70
SITE     5 EC5 19 HIS T  71  ASN T  76  HOH T3350
SITE     1 EC6 12 GLN B  59  CHD B1085  LYS P 157  HIS P 158
SITE     2 EC6 12 GLN P 161  THR P 168  TYR P 172  HOH P4459
SITE     3 EC6 12 ALA S   1  ARG T  17  CDL T1269  HOH T4897
SITE     1 EC7 17 MET P  54  TRP P  58  VAL P  61  SER P  65
SITE     2 EC7 17 THR P  66  HIS P 207  ILE P 210  PHE P 214
SITE     3 EC7 17 ARG P 221  HIS P 226  PHE P 227  HIS P 231
SITE     4 EC7 17 PHE P 233  GLY P 234  CDL P1270  HOH P3065
SITE     5 EC7 17 HOH P3253
SITE     1 EC8 10 ASP N 298  THR P  95  TRP P  99  TYR P 102
SITE     2 EC8 10 HIS P 103  CHD P1525  HOH P4372  HOH P4567
SITE     3 EC8 10 ASN U  22  HOH U4545
SITE     1 EC9 13 MET P  51  MET P  54  TYR P  55  ARG P  59
SITE     2 EC9 13 ILE P  62  ARG P  63  PHE P  67  THR P 213
SITE     3 EC9 13 LYS P 224  HIS P 226  PGV P1267  LYS W   8
SITE     4 EC9 13 THR W  27
SITE     1 FC1  5 ARG P 156  PHE P 164  LEU P 223  HOH P4601
SITE     2 FC1  5 PHE W   1
SITE     1 FC2  6 TRP P  34  MET P  40  SER T  61  TRP T  62
SITE     2 FC2  6 GLY T  63  PHE T  69
SITE     1 FC3  9 TRP N 334  GLY N 343  LEU O  39  ILE O  42
SITE     2 FC3  9 LYS O  49  ARG Q  73  THR Q  75  TRP Q  78
SITE     3 FC3  9 ARG V  16
SITE     1 FC4 18 PHE N 321  HIS N 328  HOH N4328  ILE O  41
SITE     2 FC4 18 HIS O  52  MET O  56  ASP O  57  GLU O  60
SITE     3 FC4 18 HOH O4198  HIS R   5  GLU R   6  ASP R   8
SITE     4 FC4 18 PHE R  11  ASP R  40  LEU R  41  HOH R3042
SITE     5 FC4 18 HOH R3664  ARG V  10
SITE     1 FC5  4 CYS S  60  CYS S  62  CYS S  82  CYS S  85
SITE     1 FC6 13 LYS C  77  ARG C  80  TYR C  81  ILE C  84
SITE     2 FC6 13 VAL C  91  PHE C  98  TRP C 240  VAL C 247
SITE     3 FC6 13 SER T   2  ALA T   3  LYS T   5  GLY T   6
SITE     4 FC6 13 HIS T   8
SITE     1 FC7 21 PHE A 282  ASP A 300  TYR A 304  SER A 307
SITE     2 FC7 21 ALA B  77  LEU B  78  LEU B  81  TYR B  85
SITE     3 FC7 21 CHD C 525  LEU P 127  LEU P 131  VAL P 142
SITE     4 FC7 21 PEK P1265  SER T  27  LEU T  30  CYS T  31
SITE     5 FC7 21 LEU T  33  ASN T  34  LEU T  37  HIS T  38
SITE     6 FC7 21 ARG T  42
SITE     1 FC8  4 TYR W  32  ARG W  33  MET W  36  THR W  37
SITE     1 FC9 10 LEU Q  95  TRP Q  98  TYR Q 102  LEU Z  27
SITE     2 FC9 10 LEU Z  28  GLY Z  31  TRP Z  32  TYR Z  35
SITE     3 FC9 10 HIS Z  36  HOH Z4487
CRYST1  182.289  208.358  177.916  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      0.005486  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004799  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005621        0.00000
      
PROCHECK
Go to PROCHECK summary
 References