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PDBsum entry 3ag4

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Top Page protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
3ag4
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-CYN ×2
TGL ×6
PGV ×8
CUA ×2
CHD ×8
UNX ×2
PEK ×6
CDL ×4
PSC ×2
DMU
Metals
_ZN
_CU ×2
_MG ×2
_NA ×2
Waters ×1588
HEADER    OXIDOREDUCTASE                          19-MAR-10   3AG4
TITLE     BOVINE HEART CYTOCHROME C OXIDASE IN THE CYANIDE ION-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 3AG4    1       JRNL
REVDAT   1   28-APR-10 3AG4    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.    2.05 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) : 2.05
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             : 398409
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) : 0.186
REMARK   3   FREE R VALUE                     : 0.219
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            : 1588
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 3AG4 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 RCSB029210.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 07-JUL-02
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : NULL
REMARK 200  NUMBER OF CRYSTALS USED        : 5
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   : 430029
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050
REMARK 200  RESOLUTION RANGE LOW       (A) : 52.600
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   (%): 70.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.11
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       91.68200
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       89.06850
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      103.32400
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       89.06850
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       91.68200
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      103.32400
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  2701     O    HOH A  2702              1.95
REMARK 500   O    HOH A  2027     O    HOH A  2494              1.98
REMARK 500   O    ILE S    52     CE1  HIS S    94              2.07
REMARK 500  UNK   UNX P   262     O    HOH P  3259              2.08
REMARK 500   NE2  HIS C   148    UNK   UNX C   262              2.11
REMARK 500   NE2  HIS P   148    UNK   UNX P   262              2.13
REMARK 500   OE1  GLU P   236    UNK   UNX P   262              2.15
REMARK 500   NE2  HIS P   232    UNK   UNX P   262              2.17
REMARK 500   OE1  GLU C   236    UNK   UNX C   262              2.17
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    PHE A  68   CE2   PHE A  68   CD2     0.154
REMARK 500    MET A  74   CB    MET A  74   CG      0.221
REMARK 500    TRP A  81   CE3   TRP A  81   CZ3     0.143
REMARK 500    VAL A 193   CB    VAL A 193   CG2     0.132
REMARK 500    TRP A 236   CB    TRP A 236   CG      0.111
REMARK 500    PHE A 238   CZ    PHE A 238   CE2     0.126
REMARK 500    TYR A 244   CE1   TYR A 244   CZ      0.080
REMARK 500    TYR A 244   CE2   TYR A 244   CD2     0.102
REMARK 500    TYR A 261   CZ    TYR A 261   OH      0.103
REMARK 500    TYR A 261   CZ    TYR A 261   CE2     0.088
REMARK 500    TRP A 288   CE3   TRP A 288   CZ3     0.139
REMARK 500    GLY A 352   N     GLY A 352   CA      0.094
REMARK 500    TYR A 371   CD1   TYR A 371   CE1     0.095
REMARK 500    ALA A 388   CA    ALA A 388   CB      0.185
REMARK 500    ARG A 438   CB    ARG A 438   CG     -0.253
REMARK 500    SER A 458   CB    SER A 458   OG      0.078
REMARK 500    VAL A 469   CB    VAL A 469   CG2     0.162
REMARK 500    PHE A 470   CZ    PHE A 470   CE2     0.141
REMARK 500    GLU B  18   CG    GLU B  18   CD      0.092
REMARK 500    GLU B 198   C     GLU B 198   O       0.137
REMARK 500    SER C  29   CB    SER C  29   OG     -0.080
REMARK 500    TRP C  57   CB    TRP C  57   CG      0.124
REMARK 500    TYR C 193   CD1   TYR C 193   CE1     0.091
REMARK 500    TYR D  11   CB    TYR D  11   CG      0.111
REMARK 500    LYS D 100   CD    LYS D 100   CE      0.166
REMARK 500    LYS D 100   CE    LYS D 100   NZ      0.200
REMARK 500    TYR D 104   CE2   TYR D 104   CD2     0.105
REMARK 500    LYS D 127   CB    LYS D 127   CG      0.165
REMARK 500    TRP G  36   CB    TRP G  36   CG      0.121
REMARK 500    TYR I  47   CZ    TYR I  47   CE2     0.084
REMARK 500    SER K  20   CB    SER K  20   OG     -0.085
REMARK 500    TRP K  29   CB    TRP K  29   CG      0.120
REMARK 500    GLU L   4   CG    GLU L   4   CD      0.097
REMARK 500    GLU L  16   CB    GLU L  16   CG      0.114
REMARK 500    GLU L  16   CG    GLU L  16   CD      0.099
REMARK 500    PHE N  63   CG    PHE N  63   CD1     0.098
REMARK 500    MET N  74   CB    MET N  74   CG      0.253
REMARK 500    ALA N 139   CA    ALA N 139   CB      0.178
REMARK 500    LEU N 195   C     LEU N 195   O       0.114
REMARK 500    TYR N 270   CE2   TYR N 270   CD2     0.123
REMARK 500    TRP N 288   CB    TRP N 288   CG      0.110
REMARK 500    VAL N 299   CB    VAL N 299   CG1     0.131
REMARK 500    TYR N 372   CD1   TYR N 372   CE1     0.093
REMARK 500    PHE N 397   CZ    PHE N 397   CE2     0.114
REMARK 500    PHE N 414   CE1   PHE N 414   CZ      0.129
REMARK 500    GLU O 198   C     GLU O 198   O       0.145
REMARK 500    SER P  29   CB    SER P  29   OG     -0.114
REMARK 500    ALA P  74   CA    ALA P  74   CB      0.134
REMARK 500    GLU P 180   CD    GLU P 180   OE1     0.079
REMARK 500    TYR P 181   CD1   TYR P 181   CE1     0.147
REMARK 500
REMARK 500 THIS ENTRY HAS      54 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  96   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES
REMARK 500    LEU A 113   CB  -  CG  -  CD2 ANGL. DEV. =  11.3 DEGREES
REMARK 500    LEU A 136   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES
REMARK 500    MET A 189   CG  -  SD  -  CE  ANGL. DEV. = -13.0 DEGREES
REMARK 500    LEU A 194   CB  -  CG  -  CD2 ANGL. DEV. =  12.6 DEGREES
REMARK 500    ARG A 213   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG A 213   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES
REMARK 500    ASP A 227   CB  -  CG  -  OD2 ANGL. DEV. =   7.5 DEGREES
REMARK 500    MET A 278   CA  -  CB  -  CG  ANGL. DEV. = -10.6 DEGREES
REMARK 500    MET A 278   CG  -  SD  -  CE  ANGL. DEV. = -22.4 DEGREES
REMARK 500    MET A 297   CG  -  SD  -  CE  ANGL. DEV. = -14.2 DEGREES
REMARK 500    ASP A 298   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES
REMARK 500    MET A 310   CG  -  SD  -  CE  ANGL. DEV. = -23.7 DEGREES
REMARK 500    VAL A 380   CB  -  CA  -  C   ANGL. DEV. = -13.1 DEGREES
REMARK 500    VAL A 380   CG1 -  CB  -  CG2 ANGL. DEV. =  11.4 DEGREES
REMARK 500    MET A 383   CB  -  CA  -  C   ANGL. DEV. = -13.3 DEGREES
REMARK 500    ARG A 438   CB  -  CA  -  C   ANGL. DEV. = -14.0 DEGREES
REMARK 500    MET A 449   CA  -  CB  -  CG  ANGL. DEV. = -12.8 DEGREES
REMARK 500    ASN A 512   CB  -  CA  -  C   ANGL. DEV. = -12.3 DEGREES
REMARK 500    MET B  29   CG  -  SD  -  CE  ANGL. DEV. =  10.4 DEGREES
REMARK 500    ILE B  42   CG1 -  CB  -  CG2 ANGL. DEV. = -13.6 DEGREES
REMARK 500    LEU C  31   CB  -  CG  -  CD2 ANGL. DEV. = -10.4 DEGREES
REMARK 500    MET C  44   CG  -  SD  -  CE  ANGL. DEV. =   9.7 DEGREES
REMARK 500    ARG C  80   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES
REMARK 500    ARG C  80   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES
REMARK 500    ARG D  20   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES
REMARK 500    ARG D  20   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.5 DEGREES
REMARK 500    ASP E  40   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES
REMARK 500    ARG F  18   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES
REMARK 500    ARG F  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES
REMARK 500    ARG G  54   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG H  38   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    ARG H  38   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES
REMARK 500    ARG K  54   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.7 DEGREES
REMARK 500    LEU M  34   CB  -  CG  -  CD1 ANGL. DEV. =  14.4 DEGREES
REMARK 500    LEU N 113   CB  -  CG  -  CD1 ANGL. DEV. =  11.4 DEGREES
REMARK 500    HIS N 240   N   -  CA  -  CB  ANGL. DEV. =  11.0 DEGREES
REMARK 500    MET N 278   CG  -  SD  -  CE  ANGL. DEV. = -20.7 DEGREES
REMARK 500    MET N 383   CA  -  CB  -  CG  ANGL. DEV. =  11.1 DEGREES
REMARK 500    ASP O  11   CB  -  CG  -  OD2 ANGL. DEV. =   7.5 DEGREES
REMARK 500    ARG P  80   CG  -  CD  -  NE  ANGL. DEV. = -13.4 DEGREES
REMARK 500    ARG P  80   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES
REMARK 500    LEU P 163   CB  -  CG  -  CD1 ANGL. DEV. =  10.6 DEGREES
REMARK 500    ASP Q  10   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG Q  20   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES
REMARK 500    ARG Q  20   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.7 DEGREES
REMARK 500    ARG S  56   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES
REMARK 500    HIS S  94   N   -  CA  -  C   ANGL. DEV. =  16.2 DEGREES
REMARK 500    ARG T  17   NE  -  CZ  -  NH1 ANGL. DEV. =   5.4 DEGREES
REMARK 500    ARG T  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS      53 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  91     -167.04   -174.08
REMARK 500    GLU A 119     -130.01     45.02
REMARK 500    VAL A 318      -38.63    -36.71
REMARK 500    LEU A 381      -68.82   -100.14
REMARK 500    SER A 382      -71.16    -48.61
REMARK 500    LEU B  33      -71.21    -25.04
REMARK 500    HIS B  52       96.57   -160.87
REMARK 500    GLU B  60      -68.06    162.61
REMARK 500    ASN B  92       86.43     66.66
REMARK 500    TYR B 113      -55.88   -132.20
REMARK 500    LEU B 135       -7.44     75.11
REMARK 500    ASP B 158     -101.25   -146.49
REMARK 500    LYS B 171      111.10   -164.57
REMARK 500    ASN C  38       46.75     39.42
REMARK 500    SER C  65      -70.15   -105.55
REMARK 500    GLU C 128     -113.99   -100.49
REMARK 500    HIS C 232       56.16   -159.12
REMARK 500    TRP C 258      -73.17    -93.51
REMARK 500    GLN D 132      -34.56   -144.24
REMARK 500    PHE D 134      -75.89   -142.64
REMARK 500    GLU E   6      156.44    179.97
REMARK 500    SER F   2     -157.47   -151.18
REMARK 500    ASP F  65       -7.22     84.25
REMARK 500    HIS F  94      155.73     96.17
REMARK 500    GLN F  95     -102.42     92.54
REMARK 500    LEU F  96      -51.81     72.19
REMARK 500    ALA G   3      -84.84     74.91
REMARK 500    ALA G   4       28.54    153.87
REMARK 500    LYS G   5     -131.59   -133.11
REMARK 500    ASP G   7      -90.44      4.43
REMARK 500    HIS G   8       -5.50     45.77
REMARK 500    LEU G  23      -55.94   -129.47
REMARK 500    LEU G  37      -59.53   -163.31
REMARK 500    SER G  39      -94.91    -69.74
REMARK 500    PRO G  49       49.58    -71.21
REMARK 500    SER G  61       32.51    -87.15
REMARK 500    ILE H   8        8.71     84.63
REMARK 500    LYS H   9     -142.88    -91.36
REMARK 500    ASN H  10        6.70    101.47
REMARK 500    TYR H  11      111.23     -4.59
REMARK 500    GLN H  12      -67.69    -90.13
REMARK 500    ASN H  22     -169.66   -105.37
REMARK 500    MET H  43      -71.35    -73.71
REMARK 500    ALA H  45      -97.34    -72.03
REMARK 500    LYS H  46       14.77    -43.02
REMARK 500    VAL I  39      -60.42   -131.14
REMARK 500    ASP J  15       62.14    -68.66
REMARK 500    HIS J  57       76.63   -108.01
REMARK 500    ASN L  10       33.88    -92.47
REMARK 500    ASP N  91     -159.28   -169.57
REMARK 500
REMARK 500 THIS ENTRY HAS      97 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                  142.12
REMARK 500 HIS J   57     LYS J   58                 -135.98
REMARK 500 HIS L    2     TYR L    3                 -149.92
REMARK 500 PRO S   93     HIS S   94                  107.45
REMARK 500 HIS W   57     LYS W   58                 -147.31
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS
REMARK 500    PHE A 377        24.7      L          L   OUTSIDE RANGE
REMARK 500    ASN C  38        24.5      L          L   OUTSIDE RANGE
REMARK 500    HIS F  94        22.4      L          L   OUTSIDE RANGE
REMARK 500    GLN F  95        20.2      L          L   OUTSIDE RANGE
REMARK 500    ASP G   7        23.6      L          L   OUTSIDE RANGE
REMARK 500    HIS G   8        22.1      L          L   OUTSIDE RANGE
REMARK 500    LYS J  58        23.5      L          L   OUTSIDE RANGE
REMARK 500    TRP N 103        24.5      L          L   OUTSIDE RANGE
REMARK 500    HIS N 240        23.3      L          L   OUTSIDE RANGE
REMARK 500    TRP O  65        24.0      L          L   OUTSIDE RANGE
REMARK 500    ASN O  92        17.1      L          L   OUTSIDE RANGE
REMARK 500    HIS S  94        22.3      L          L   OUTSIDE RANGE
REMARK 500    ASP T   7        22.1      L          L   OUTSIDE RANGE
REMARK 500    HIS T   8        24.8      L          L   OUTSIDE RANGE
REMARK 500    ILE U   8        24.7      L          L   OUTSIDE RANGE
REMARK 500    LYS W  58        20.2      L          L   OUTSIDE RANGE
REMARK 500    ARG X  47        21.8      L          L   OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525  M RES CSSEQI
REMARK 525    HOH Z4266        DISTANCE =  6.08 ANGSTROMS
REMARK 525    HOH J4651        DISTANCE =  6.25 ANGSTROMS
REMARK 525    HOH T4375        DISTANCE =  6.70 ANGSTROMS
REMARK 525    HOH I4746        DISTANCE =  8.26 ANGSTROMS
REMARK 525    HOH Q4357        DISTANCE =  5.29 ANGSTROMS
REMARK 525    HOH D4517        DISTANCE =  7.12 ANGSTROMS
REMARK 525    HOH P4315        DISTANCE =  8.98 ANGSTROMS
REMARK 525    HOH P4798        DISTANCE =  6.89 ANGSTROMS
REMARK 525    HOH C4671        DISTANCE =  8.12 ANGSTROMS
REMARK 525    HOH N4389        DISTANCE =  5.38 ANGSTROMS
REMARK 525    HOH A4341        DISTANCE =  5.40 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 A 515  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 378   NE2
REMARK 620 2 HEA A 515   NA   83.3
REMARK 620 3 HEA A 515   NB   89.4  89.2
REMARK 620 4 HEA A 515   NC   90.0 173.3  90.4
REMARK 620 5 HEA A 515   ND   89.3  89.6 178.3  90.6
REMARK 620 6 HIS A  61   NE2 176.9  99.6  89.4  87.1  92.0
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              CU A 517  CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 240   ND1
REMARK 620 2 HIS A 291   NE2 155.9
REMARK 620 3 CYN A 520   N   101.4 101.7
REMARK 620 N                    1     2
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 158.7
REMARK 620 3 CYN N 520   N    96.5 104.9
REMARK 620 4 HIS N 290   NE2 105.1  76.8  84.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             CUA B 228  CU1
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 161   ND1
REMARK 620 2 CUA B 228  CU2  130.1
REMARK 620 3 MET B 207   SD  101.1 127.6
REMARK 620 4 CYS B 200   SG  101.3  55.9 110.0
REMARK 620 5 CYS B 196   SG  116.7  55.2 115.7 110.8
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  124.9
REMARK 620 3 CYS O 196   SG  110.3  54.7
REMARK 620 4 CYS O 200   SG  102.2  53.9 108.1
REMARK 620 5 MET O 207   SD  110.1 124.0 116.8 108.2
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  161.6
REMARK 620 3 CYS B 196   SG  125.7  59.1
REMARK 620 4 CYS B 200   SG  115.6  58.6 117.3
REMARK 620 5 GLU B 198   O    85.5 112.3  95.5 101.0
REMARK 620 N                    1     2     3     4
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  163.9
REMARK 620 3 GLU O 198   O    85.8 110.3
REMARK 620 4 CYS O 196   SG  126.1  55.5  93.7
REMARK 620 5 CYS O 200   SG  120.4  57.7 101.0 112.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEA N 515  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 378   NE2
REMARK 620 2 HEA N 515   NA   85.9
REMARK 620 3 HEA N 515   NB   90.5  93.4
REMARK 620 4 HEA N 515   NC   89.0 174.5  88.6
REMARK 620 5 HEA N 515   ND   88.9  89.3 177.2  88.7
REMARK 620 6 HIS N  61   NE2 175.2  99.0  88.9  86.2  91.6
REMARK 620 N                    1     2     3     4     5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEA A 516  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 376   NE2
REMARK 620 2 HEA A 516   NA   92.7
REMARK 620 3 HEA A 516   NB   93.4  86.6
REMARK 620 4 HEA A 516   NC   94.0 171.5  98.2
REMARK 620 5 HEA A 516   ND   90.5  95.6 175.5  79.2
REMARK 620 6 CYN A 520   N   160.7  82.8 105.0  89.2  71.4
REMARK 620 N                    1     2     3     4     5
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 GLU B 198   OE1
REMARK 620 2 ASP A 369   OD1  85.1
REMARK 620 3 HOH B2267   O    86.2  92.0
REMARK 620 4 HOH B2266   O    89.8 174.9  87.9
REMARK 620 5 HOH B2268   O    91.0  94.6 172.7  85.3
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 GLU O 198   OE1  93.3
REMARK 620 3 HOH O3266   O   177.2  87.5
REMARK 620 4 HOH O3267   O    88.5  84.6  88.9
REMARK 620 5 HOH O3268   O    96.6  96.7  85.9 174.6
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                             HEA N 516  FE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS N 376   NE2
REMARK 620 2 HEA N 516   NA   92.1
REMARK 620 3 HEA N 516   NB   86.5  81.4
REMARK 620 4 HEA N 516   NC   94.2 172.4  94.8
REMARK 620 5 HEA N 516   ND   99.2 100.3 173.9  82.8
REMARK 620 6 CYN N 520   N   171.5  79.5  92.8  94.2  81.8
REMARK 620 N                    1     2     3     4     5
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 GLY N  45   O    88.9
REMARK 620 3 GLU N  40   OE1 174.0  97.1
REMARK 620 4 GLU N  40   O    88.0 134.7  87.1
REMARK 620 5 SER N 441   O    95.0 113.4  83.5 111.9
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 SER A 441   O    96.4
REMARK 620 3 GLU A  40   O    89.4 114.9
REMARK 620 4 GLU A  40   OE1 177.0  86.2  88.1
REMARK 620 5 GLY A  45   O    85.8 113.7 131.4  94.5
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  105.9
REMARK 620 3 CYS F  62   SG  119.1 107.7
REMARK 620 4 CYS F  85   SG  106.4 108.1 109.2
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  62   SG
REMARK 620 2 CYS S  82   SG  110.6
REMARK 620 3 CYS S  85   SG  105.3 107.4
REMARK 620 4 CYS S  60   SG  116.5 108.7 108.0
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 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 CYN 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 524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV A 522
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA B 228
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 PSC E 229
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 99
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK G 265
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL G 269
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU G 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK G 1263
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD J 60
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL L 522
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 CYN 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 1521
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL N 1522
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV N 1524
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV N 1266
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CUA O 228
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD O 229
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 PGV P 1267
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PGV P 1268
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDL P 1270
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CHD P 1271
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMU P 1272
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TGL Q 1523
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PSC R 1229
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN S 99
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK S 1265
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK T 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEK T 1264
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: 3AG3   RELATED DB: PDB
DBREF  3AG4 A    1   514  UNP    P00396   COX1_BOVIN       1    514
DBREF  3AG4 B    1   227  UNP    P68530   COX2_BOVIN       1    227
DBREF  3AG4 C    1   261  UNP    P00415   COX3_BOVIN       1    261
DBREF  3AG4 D    1   147  UNP    P00423   COX41_BOVIN     23    169
DBREF  3AG4 E    1   109  UNP    P00426   COX5A_BOVIN     44    152
DBREF  3AG4 F    1    98  UNP    P00428   COX5B_BOVIN     32    129
DBREF  3AG4 G    1    85  UNP    P07471   CX6A2_BOVIN     13     97
DBREF  3AG4 H    1    85  UNP    P00429   CX6B1_BOVIN      2     86
DBREF  3AG4 I    1    73  UNP    P04038   COX6C_BOVIN      2     74
DBREF  3AG4 J    1    59  UNP    P07470   CX7A1_BOVIN     22     80
DBREF  3AG4 K    1    56  UNP    P13183   COX7B_BOVIN     25     80
DBREF  3AG4 L    1    47  UNP    P00430   COX7C_BOVIN     17     63
DBREF  3AG4 M    1    46  UNP    P10175   COX8B_BOVIN     25     70
DBREF  3AG4 N    1   514  UNP    P00396   COX1_BOVIN       1    514
DBREF  3AG4 O    1   227  UNP    P68530   COX2_BOVIN       1    227
DBREF  3AG4 P    1   261  UNP    P00415   COX3_BOVIN       1    261
DBREF  3AG4 Q    1   147  UNP    P00423   COX41_BOVIN     23    169
DBREF  3AG4 R    1   109  UNP    P00426   COX5A_BOVIN     44    152
DBREF  3AG4 S    1    98  UNP    P00428   COX5B_BOVIN     32    129
DBREF  3AG4 T    1    85  UNP    P07471   CX6A2_BOVIN     13     97
DBREF  3AG4 U    1    85  UNP    P00429   CX6B1_BOVIN      2     86
DBREF  3AG4 V    1    73  UNP    P04038   COX6C_BOVIN      2     74
DBREF  3AG4 W    1    59  UNP    P07470   CX7A1_BOVIN     22     80
DBREF  3AG4 X    1    56  UNP    P13183   COX7B_BOVIN     25     80
DBREF  3AG4 Y    1    47  UNP    P00430   COX7C_BOVIN     17     63
DBREF  3AG4 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 3AG4 FME A    1  MET  N-FORMYLMETHIONINE
MODRES 3AG4 FME B    1  MET  N-FORMYLMETHIONINE
MODRES 3AG4 TPO G   11  THR  PHOSPHOTHREONINE
MODRES 3AG4 SAC I    1  SER  N-ACETYL-SERINE
MODRES 3AG4 FME N    1  MET  N-FORMYLMETHIONINE
MODRES 3AG4 FME O    1  MET  N-FORMYLMETHIONINE
MODRES 3AG4 TPO T   11  THR  PHOSPHOTHREONINE
MODRES 3AG4 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    CYN  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 524      51
HET    PGV  A 522      51
HET    CUA  B 228       2
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    PSC  E 229      52
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    DMU  M 526      33
HET    HEA  N 515      60
HET    HEA  N 516      60
HET    CYN  N 520       2
HET     CU  N 517       1
HET     MG  N 518       1
HET     NA  N 519       1
HET    TGL  N1521      63
HET    TGL  N1522      63
HET    PGV  N1524      51
HET    PGV  N1266      51
HET    CUA  O 228       2
HET    CHD  O 229      29
HET    UNX  P 262       1
HET    CHD  P1525      29
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  S1265      53
HET    PEK  T 263      53
HET    PEK  T1264      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     CYN CYANIDE ION
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     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     PSC (7R,17E,20E)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-
HETNAM   2 PSC  [(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSA-
HETNAM   3 PSC  17,20-DIEN-1-AMINIUM 4-OXIDE
HETNAM      ZN ZINC ION
HETNAM     DMU DECYL-BETA-D-MALTOPYRANOSIDE
HETSYN     TPO PHOSPHONOTHREONINE
HETSYN     TGL TRIACYLGLYCEROL
HETSYN     PGV PHOSPHATIDYLGLYCEROL, 2-VACCENOYL-1-PALMITOYL-SN-
HETSYN   2 PGV  GLYCEROL-3-PHOSPHOGLYCEROL
HETSYN     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     PSC PHOSPHATIDYLCHOLINE, 2-LINOLEOYL-1-PALMITOYL-SN-
HETSYN   2 PSC  GYCEROL-3-PHOSPHOCHOLINE
HETSYN     DMU DECYLMALTOSIDE
FORMUL   1  FME    4(C6 H11 N O3 S)
FORMUL   7  TPO    2(C4 H10 N O6 P)
FORMUL   9  SAC    2(C5 H9 N O4)
FORMUL  27  HEA    4(C49 H56 FE N4 O6)
FORMUL  29  CYN    2(C N 1-)
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  36  CUA    2(CU2)
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  PSC    2(C42 H81 N O8 P 1+)
FORMUL  47   ZN    2(ZN 2+)
FORMUL  50  DMU    4(C22 H42 O11)
FORMUL  83  HOH   *1588(H2 O)
HELIX    1   1 FME A    1  LEU A    7  1                                   7
HELIX    2   2 ASN A   11  LEU A   41  1                                  31
HELIX    3   3 ASP A   50  PHE A   68  1                                  19
HELIX    4   4 MET A   69  ILE A   75  1                                   7
HELIX    5   5 GLY A   77  ILE A   87  1                                  11
HELIX    6   6 ARG A   96  LEU A  104  1                                   9
HELIX    7   7 LEU A  104  VAL A  118  1                                  15
HELIX    8   8 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  HIS A  328  1                                  31
HELIX   17  17 SER A  335  ASN A  360  1                                  26
HELIX   18  18 ASN A  360  HIS A  368  1                                   9
HELIX   19  19 THR A  370  LEU A  381  1                                  12
HELIX   20  20 LEU A  381  GLY A  402  1                                  22
HELIX   21  21 ASN A  406  SER A  434  1                                  29
HELIX   22  22 PRO A  444  ALA A  446  5                                   3
HELIX   23  23 TYR A  447  LYS A  479  1                                  33
HELIX   24  24 LEU A  487  LEU A  495  5                                   9
HELIX   25  25 SER B   14  LEU B   46  1                                  33
HELIX   26  26 GLU B   60  GLU B   89  1                                  30
HELIX   27  27 PRO B  124  LEU B  128  5                                   5
HELIX   28  28 PRO B  166  GLY B  169  5                                   4
HELIX   29  29 ASN B  203  PHE B  206  5                                   4
HELIX   30  30 PRO B  215  MET B  226  1                                  12
HELIX   31  31 PRO C   15  PHE C   37  1                                  23
HELIX   32  32 MET C   40  THR C   66  1                                  27
HELIX   33  33 THR C   72  ALA C  107  1                                  36
HELIX   34  34 THR C  109  GLY C  113  5                                   5
HELIX   35  35 GLU C  128  GLU C  153  1                                  26
HELIX   36  36 ASP C  155  ALA C  184  1                                  30
HELIX   37  37 ASP C  190  LYS C  224  1                                  35
HELIX   38  38 HIS C  232  ILE C  256  1                                  25
HELIX   39  39 LYS D    7  TYR D   11  5                                   5
HELIX   40  40 SER D   34  LYS D   45  1                                  12
HELIX   41  41 ALA D   46  LEU D   51  5                                   6
HELIX   42  42 SER D   52  PHE D   64  1                                  13
HELIX   43  43 SER D   67  ASN D   72  1                                   6
HELIX   44  44 ASN D   76  VAL D  103  1                                  28
HELIX   45  45 PRO D  108  PHE D  111  5                                   4
HELIX   46  46 GLU D  112  MET D  126  1                                  15
HELIX   47  47 PHE D  134  ALA D  136  5                                   3
HELIX   48  48 THR E    7  LYS E   21  1                                  15
HELIX   49  49 ASP E   25  VAL E   37  1                                  13
HELIX   50  50 GLU E   44  LEU E   58  1                                  15
HELIX   51  51 ASP E   60  ALA E   75  1                                  16
HELIX   52  52 GLU E   80  GLY E   97  1                                  18
HELIX   53  53 THR F    8  ALA F   13  1                                   6
HELIX   54  54 THR F   14  LYS F   26  1                                  13
HELIX   55  55 GLY G   12  LEU G   23  1                                  12
HELIX   56  56 LEU G   23  SER G   39  1                                  17
HELIX   57  57 GLN H   25  GLY H   47  1                                  23
HELIX   58  58 ASP H   49  VAL H   52  5                                   4
HELIX   59  59 CYS H   53  CYS H   64  1                                  12
HELIX   60  60 PRO H   65  GLY H   79  1                                  15
HELIX   61  61 GLY I   11  VAL I   39  1                                  29
HELIX   62  62 VAL I   39  ASN I   53  1                                  15
HELIX   63  63 ASP I   55  GLY I   67  1                                  13
HELIX   64  64 ARG J    4  GLU J   14  1                                  11
HELIX   65  65 PRO J   19  LYS J   23  5                                   5
HELIX   66  66 GLY J   25  SER J   54  1                                  30
HELIX   67  67 ASP K    8  GLN K   35  1                                  28
HELIX   68  68 ASN L   17  LYS L   47  1                                  31
HELIX   69  69 SER M   11  HIS M   36  1                                  26
HELIX   70  70 HIS M   36  LYS M   42  1                                   7
HELIX   71  71 FME N    1  LEU N    7  1                                   7
HELIX   72  72 ASN N   11  GLY N   42  1                                  32
HELIX   73  73 ASP N   50  PHE N   68  1                                  19
HELIX   74  74 MET N   69  ILE N   75  1                                   7
HELIX   75  75 GLY N   77  ILE N   87  1                                  11
HELIX   76  76 ARG N   96  LEU N  104  1                                   9
HELIX   77  77 LEU N  104  VAL N  118  1                                  15
HELIX   78  78 ALA N  141  MET N  171  1                                  31
HELIX   79  79 SER N  177  THR N  181  5                                   5
HELIX   80  80 PRO N  182  LEU N  215  1                                  34
HELIX   81  81 ASP N  221  GLY N  225  5                                   5
HELIX   82  82 ASP N  227  SER N  262  1                                  36
HELIX   83  83 GLY N  269  GLY N  284  1                                  16
HELIX   84  84 PHE N  285  ILE N  286  5                                   2
HELIX   85  85 VAL N  287  MET N  292  5                                   6
HELIX   86  86 ASP N  298  ILE N  312  1                                  15
HELIX   87  87 ILE N  312  HIS N  328  1                                  17
HELIX   88  88 SER N  335  ASN N  360  1                                  26
HELIX   89  89 ASN N  360  HIS N  368  1                                   9
HELIX   90  90 THR N  370  LEU N  381  1                                  12
HELIX   91  91 LEU N  381  GLY N  402  1                                  22
HELIX   92  92 ASN N  406  PHE N  426  1                                  21
HELIX   93  93 PRO N  427  SER N  434  1                                   8
HELIX   94  94 PRO N  444  ALA N  446  5                                   3
HELIX   95  95 TYR N  447  LYS N  479  1                                  33
HELIX   96  96 LEU N  487  LEU N  495  5                                   9
HELIX   97  97 SER O   14  THR O   47  1                                  34
HELIX   98  98 GLU O   60  GLU O   89  1                                  30
HELIX   99  99 PRO O  124  LEU O  128  5                                   5
HELIX  100 100 PRO O  166  GLY O  169  5                                   4
HELIX  101 101 ASN O  203  MET O  207  5                                   5
HELIX  102 102 PRO O  215  MET O  226  1                                  12
HELIX  103 103 PRO P   15  PHE P   37  1                                  23
HELIX  104 104 MET P   40  THR P   66  1                                  27
HELIX  105 105 THR P   72  ALA P  107  1                                  36
HELIX  106 106 THR P  109  GLY P  113  5                                   5
HELIX  107 107 GLU P  128  GLU P  153  1                                  26
HELIX  108 108 ASP P  155  ALA P  184  1                                  30
HELIX  109 109 ASP P  190  LYS P  224  1                                  35
HELIX  110 110 HIS P  232  ILE P  256  1                                  25
HELIX  111 111 LYS Q    7  TYR Q   11  5                                   5
HELIX  112 112 SER Q   34  GLU Q   44  1                                  11
HELIX  113 113 LYS Q   45  ALA Q   46  5                                   2
HELIX  114 114 SER Q   47  LEU Q   51  5                                   5
HELIX  115 115 SER Q   52  PHE Q   64  1                                  13
HELIX  116 116 SER Q   67  ASN Q   72  1                                   6
HELIX  117 117 ASN Q   76  VAL Q  103  1                                  28
HELIX  118 118 PRO Q  108  PHE Q  111  5                                   4
HELIX  119 119 GLU Q  112  MET Q  126  1                                  15
HELIX  120 120 PHE Q  134  ALA Q  136  5                                   3
HELIX  121 121 THR R    7  LYS R   21  1                                  15
HELIX  122 122 ASP R   25  VAL R   37  1                                  13
HELIX  123 123 GLU R   44  LEU R   58  1                                  15
HELIX  124 124 ASP R   60  ALA R   75  1                                  16
HELIX  125 125 GLU R   80  GLY R   97  1                                  18
HELIX  126 126 THR S    8  ALA S   13  1                                   6
HELIX  127 127 THR S   14  LYS S   26  1                                  13
HELIX  128 128 GLY T   12  LEU T   23  1                                  12
HELIX  129 129 LEU T   23  TRP T   36  1                                  14
HELIX  130 130 GLN U   25  GLY U   47  1                                  23
HELIX  131 131 ASP U   49  VAL U   52  5                                   4
HELIX  132 132 CYS U   53  CYS U   64  1                                  12
HELIX  133 133 PRO U   65  GLY U   79  1                                  15
HELIX  134 134 GLY V   11  VAL V   39  1                                  29
HELIX  135 135 VAL V   39  ASN V   53  1                                  15
HELIX  136 136 ASP V   55  ALA V   66  1                                  12
HELIX  137 137 ARG W    4  GLU W   14  1                                  11
HELIX  138 138 PRO W   19  LYS W   23  5                                   5
HELIX  139 139 GLY W   25  SER W   54  1                                  30
HELIX  140 140 ASP X    8  ILE X   36  1                                  29
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 5 LEU B 116  SER B 120  0
SHEET    2   B 5 TYR B 105  TYR B 110 -1  N  TYR B 110   O  LEU B 116
SHEET    3   B 5 LEU B  95  HIS B 102 -1  N  MET B 100   O  SER B 107
SHEET    4   B 5 ILE B 150  SER B 156  1  O  ARG B 151   N  LEU B  95
SHEET    5   B 5 ASN B 180  LEU B 184 -1  O  ASN B 180   N  VAL B 154
SHEET    1   C 3 VAL B 142  PRO B 145  0
SHEET    2   C 3 PRO B 208  VAL B 214  1  O  GLU B 212   N  VAL B 142
SHEET    3   C 3 GLY B 190  GLN B 195 -1  N  TYR B 192   O  LEU B 211
SHEET    1   D 2 HIS B 161  VAL B 165  0
SHEET    2   D 2 LEU B 170  ALA B 174 -1  O  ALA B 174   N  HIS B 161
SHEET    1   E 2 TRP D 138  ASP D 139  0
SHEET    2   E 2 GLU D 144  TRP D 145 -1  O  GLU D 144   N  ASP D 139
SHEET    1   F 3 ASN F  47  SER F  51  0
SHEET    2   F 3 HIS F  88  PRO F  93  1  O  LYS F  90   N  ASN F  47
SHEET    3   F 3 GLN F  80  ARG F  81 -1  N  GLN F  80   O  TYR F  89
SHEET    1   G 2 LYS F  55  CYS F  60  0
SHEET    2   G 2 ILE F  70  HIS F  75 -1  O  ILE F  70   N  CYS F  60
SHEET    1   H 5 LEU O 116  SER O 120  0
SHEET    2   H 5 TYR O 105  TYR O 110 -1  N  TYR O 110   O  LEU O 116
SHEET    3   H 5 LEU O  95  HIS O 102 -1  N  MET O 100   O  SER O 107
SHEET    4   H 5 ILE O 150  SER O 156  1  O  ARG O 151   N  LEU O  95
SHEET    5   H 5 ASN O 180  LEU O 184 -1  O  ASN O 180   N  VAL O 154
SHEET    1   I 3 VAL O 142  PRO O 145  0
SHEET    2   I 3 ILE O 209  VAL O 214  1  O  GLU O 212   N  VAL O 142
SHEET    3   I 3 GLY O 190  GLY O 194 -1  N  TYR O 192   O  LEU O 211
SHEET    1   J 2 HIS O 161  VAL O 165  0
SHEET    2   J 2 LEU O 170  ALA O 174 -1  O  ALA O 174   N  HIS O 161
SHEET    1   K 2 TRP Q 138  ASP Q 139  0
SHEET    2   K 2 GLU Q 144  TRP Q 145 -1  O  GLU Q 144   N  ASP Q 139
SHEET    1   L 3 ASN S  47  SER S  51  0
SHEET    2   L 3 HIS S  88  PRO S  93  1  O  LYS S  90   N  ASN S  47
SHEET    3   L 3 GLN S  80  ARG S  81 -1  N  GLN S  80   O  TYR S  89
SHEET    1   M 2 LYS S  55  CYS S  60  0
SHEET    2   M 2 ILE S  70  HIS S  75 -1  O  LEU S  74   N  ARG S  56
SSBOND   1 CYS H   29    CYS H   64                          1555   1555  2.12
SSBOND   2 CYS H   39    CYS H   53                          1555   1555  2.04
SSBOND   3 CYS U   29    CYS U   64                          1555   1555  2.13
SSBOND   4 CYS U   39    CYS U   53                          1555   1555  2.05
LINK         NE2 HIS A 240                 CE2 TYR A 244     1555   1555  1.37
LINK         NE2 HIS N 240                 CE2 TYR N 244     1555   1555  1.33
LINK         C   FME A   1                 N   PHE A   2     1555   1555  1.33
LINK         C   FME B   1                 N   ALA B   2     1555   1555  1.32
LINK         C   GLY G  10                 N   TPO G  11     1555   1555  1.34
LINK         C   TPO G  11                 N   GLY G  12     1555   1555  1.37
LINK         C   SAC I   1                 N   THR I   2     1555   1555  1.32
LINK         C   FME N   1                 N   PHE N   2     1555   1555  1.33
LINK         C   FME O   1                 N   ALA O   2     1555   1555  1.32
LINK         C   GLY T  10                 N   TPO T  11     1555   1555  1.35
LINK         C   TPO T  11                 N   GLY T  12     1555   1555  1.37
LINK         C   SAC V   1                 N   THR V   2     1555   1555  1.34
LINK         NE2 HIS A 378                FE   HEA A 515     1555   1555  1.95
LINK         ND1 HIS A 240                CU    CU A 517     1555   1555  1.97
LINK         ND1 HIS N 240                CU    CU N 517     1555   1555  1.98
LINK         NE2 HIS A  61                FE   HEA A 515     1555   1555  1.98
LINK         NE2 HIS N 291                CU    CU N 517     1555   1555  1.99
LINK         ND1 HIS B 161                CU1  CUA B 228     1555   1555  1.99
LINK         ND1 HIS O 161                CU1  CUA O 228     1555   1555  1.99
LINK         ND1 HIS B 204                CU2  CUA B 228     1555   1555  2.01
LINK         ND1 HIS O 204                CU2  CUA O 228     1555   1555  2.02
LINK         NE2 HIS N 378                FE   HEA N 515     1555   1555  2.02
LINK         NE2 HIS A 291                CU    CU A 517     1555   1555  2.03
LINK         NE2 HIS N  61                FE   HEA N 515     1555   1555  2.06
LINK         NE2 HIS A 376                FE   HEA A 516     1555   1555  2.09
LINK         OE1 GLU B 198                MG    MG A 518     1555   1555  2.11
LINK         OD1 ASP A 369                MG    MG A 518     1555   1555  2.13
LINK         OD1 ASP N 369                MG    MG N 518     1555   1555  2.13
LINK         NE2 HIS N 376                FE   HEA N 516     1555   1555  2.18
LINK         OE1 GLU O 198                MG    MG N 518     1555   1555  2.18
LINK        NA    NA N 519                 O   HOH N3258     1555   1555  2.21
LINK        NA    NA A 519                 O   HOH A2258     1555   1555  2.23
LINK         O   GLU O 198                CU2  CUA O 228     1555   1555  2.24
LINK         O   GLY N  45                NA    NA N 519     1555   1555  2.24
LINK         OE1 GLU N  40                NA    NA N 519     1555   1555  2.25
LINK        MG    MG A 518                 O   HOH B2267     1555   1555  2.26
LINK         N   CYN A 520                CU    CU A 517     1555   1555  2.26
LINK         O   GLU N  40                NA    NA N 519     1555   1555  2.27
LINK        MG    MG A 518                 O   HOH B2266     1555   1555  2.27
LINK         SG  CYS F  60                ZN    ZN F  99     1555   1555  2.28
LINK         SG  CYS B 196                CU2  CUA B 228     1555   1555  2.28
LINK        MG    MG A 518                 O   HOH B2268     1555   1555  2.28
LINK         SG  CYS O 196                CU2  CUA O 228     1555   1555  2.28
LINK         SG  CYS O 200                CU2  CUA O 228     1555   1555  2.28
LINK         O   SER A 441                NA    NA A 519     1555   1555  2.28
LINK        MG    MG N 518                 O   HOH O3266     1555   1555  2.28
LINK         O   GLU A  40                NA    NA A 519     1555   1555  2.29
LINK         OE1 GLU A  40                NA    NA A 519     1555   1555  2.29
LINK         O   GLY A  45                NA    NA A 519     1555   1555  2.29
LINK         O   SER N 441                NA    NA N 519     1555   1555  2.30
LINK         SG  CYS B 200                CU2  CUA B 228     1555   1555  2.30
LINK         SG  CYS O 196                CU1  CUA O 228     1555   1555  2.30
LINK        MG    MG N 518                 O   HOH O3267     1555   1555  2.32
LINK        MG    MG N 518                 O   HOH O3268     1555   1555  2.32
LINK         SG  CYS F  82                ZN    ZN F  99     1555   1555  2.33
LINK         O   GLU B 198                CU2  CUA B 228     1555   1555  2.34
LINK         SD  MET B 207                CU1  CUA B 228     1555   1555  2.35
LINK         SG  CYS F  62                ZN    ZN F  99     1555   1555  2.36
LINK         SG  CYS S  62                ZN    ZN S  99     1555   1555  2.36
LINK         SG  CYS S  82                ZN    ZN S  99     1555   1555  2.37
LINK         SG  CYS B 200                CU1  CUA B 228     1555   1555  2.37
LINK         SG  CYS S  85                ZN    ZN S  99     1555   1555  2.38
LINK         SG  CYS B 196                CU1  CUA B 228     1555   1555  2.38
LINK         SG  CYS O 200                CU1  CUA O 228     1555   1555  2.39
LINK         SD  MET O 207                CU1  CUA O 228     1555   1555  2.40
LINK         SG  CYS F  85                ZN    ZN F  99     1555   1555  2.41
LINK         SG  CYS S  60                ZN    ZN S  99     1555   1555  2.41
LINK         N   CYN N 520                CU    CU N 517     1555   1555  2.44
LINK        FE   HEA N 516                 N   CYN N 520     1555   1555  2.59
LINK         NE2 HIS N 290                CU    CU N 517     1555   1555  2.64
LINK        FE   HEA A 516                 N   CYN A 520     1555   1555  2.78
CISPEP   1 PRO A  130    PRO A  131          0        -0.28
CISPEP   2 CYS A  498    PRO A  499          0        -8.01
CISPEP   3 GLN B  103    TRP B  104          0       -12.70
CISPEP   4 TRP C  116    PRO C  117          0        -6.08
CISPEP   5 PRO N  130    PRO N  131          0        -0.08
CISPEP   6 CYS N  498    PRO N  499          0        -8.81
CISPEP   7 GLN O  103    TRP O  104          0       -12.09
CISPEP   8 TRP P  116    PRO P  117          0        -9.69
SITE     1 AC1 29 MET A  28  THR A  31  SER A  34  ILE A  37
SITE     2 AC1 29 ARG A  38  TYR A  54  VAL A  58  HIS A  61
SITE     3 AC1 29 ALA A  62  MET A  65  VAL A  70  ILE A  73
SITE     4 AC1 29 GLY A 125  TRP A 126  TYR A 371  PHE A 377
SITE     5 AC1 29 HIS A 378  SER A 382  VAL A 386  MET A 417
SITE     6 AC1 29 PHE A 425  GLN A 428  ARG A 438  ARG A 439
SITE     7 AC1 29 TYR A 440  VAL A 465  HOH A2045  HOH A2283
SITE     8 AC1 29 HOH A2700
SITE     1 AC2 29 TRP A 126  VAL A 243  TYR A 244  ILE A 247
SITE     2 AC2 29 HIS A 290  HIS A 291  THR A 309  ILE A 312
SITE     3 AC2 29 THR A 316  GLY A 317  GLY A 352  GLY A 355
SITE     4 AC2 29 ILE A 356  LEU A 358  ALA A 359  ASP A 364
SITE     5 AC2 29 HIS A 368  VAL A 373  HIS A 376  PHE A 377
SITE     6 AC2 29 VAL A 380  LEU A 381  ARG A 438  CYN A 520
SITE     7 AC2 29 HOH A2081  HOH A2183  HOH A2272  HOH A2341
SITE     8 AC2 29 PRO B  69
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  CYN 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  8 ASN A 422  PHE A 426  PHE A 430  LEU A 433
SITE     2 AC7  8 LEU B   7  LEU B  28  VAL B  31  SER B  35
SITE     1 AC8 16 ASN A 406  THR A 408  TRP A 409  HOH A2668
SITE     2 AC8 16 HOH A4140  HOH A4452  HOH A4691  ALA D  84
SITE     3 AC8 16 PHE D  87  HIS K  10  GLN M  15  ALA M  16
SITE     4 AC8 16 LEU M  19  SER M  20  HOH M2126  HOH M4486
SITE     1 AC9 15 PHE A  94  PRO A  95  ARG A  96  MET A  97
SITE     2 AC9 15 HOH A2085  HOH A2289  HOH A4723  HIS C   9
SITE     3 AC9 15 ASN C  50  TRP C  57  TRP C  58  GLU C  64
SITE     4 AC9 15 HIS C  71  GLY C  82  PEK C 264
SITE     1 BC1  6 HIS B 161  CYS B 196  GLU B 198  CYS B 200
SITE     2 BC1  6 HIS B 204  MET B 207
SITE     1 BC2 12 MET A 271  GLN B  59  GLU B  62  THR B  63
SITE     2 BC2 12 THR B  66  HOH B2605  HOH B3446  PEK S1265
SITE     3 BC2 12 ARG T  14  ARG T  17  PHE T  18  GLY T  22
SITE     1 BC3  9 HIS A 233  ASP A 300  THR A 301  TYR A 304
SITE     2 BC3  9 TRP C  99  HIS C 103  HOH C2155  HOH C4204
SITE     3 BC3  9 HOH C4556
SITE     1 BC4 18 HIS A 151  PGV A 522  HOH A4723  TRP C  34
SITE     2 BC4 18 TYR C 181  TYR C 182  ALA C 184  PHE C 186
SITE     3 BC4 18 THR C 187  ILE C 188  PHE C 198  HOH C2350
SITE     4 BC4 18 TRP G  62  THR G  68  PHE G  69  PHE G  70
SITE     5 BC4 18 HIS G  71  ASN G  76
SITE     1 BC5 20 MET C  54  TRP C  58  VAL C  61  SER C  65
SITE     2 BC5 20 THR C  66  HIS C 207  ILE C 210  PHE C 214
SITE     3 BC5 20 ARG C 221  HIS C 226  PHE C 227  HIS C 231
SITE     4 BC5 20 HIS C 232  PHE C 233  GLY C 234  CDL C 270
SITE     5 BC5 20 HOH C2253  HOH C2559  HOH C4710  HOH F2065
SITE     1 BC6 11 THR C  95  TRP C  99  TYR C 102  HIS C 103
SITE     2 BC6 11 LEU C 106  ALA C 107  HOH C4295  HOH C4316
SITE     3 BC6 11 HOH C4671  HOH C4773  HOH H4234
SITE     1 BC7 16 MET C  51  TYR C  55  TRP C  58  ARG C  59
SITE     2 BC7 16 ILE C  62  ARG C  63  PHE C  67  THR C 213
SITE     3 BC7 16 VAL C 217  ARG C 221  LYS C 224  HIS C 226
SITE     4 BC7 16 PGV C 267  HOH C2144  HOH C4143  LYS J   8
SITE     1 BC8  5 ARG C 156  LEU C 160  PHE C 164  LEU C 223
SITE     2 BC8  5 PHE J   1
SITE     1 BC9 14 TRP A 334  GLY A 343  PHE A 414  VAL A 419
SITE     2 BC9 14 THR B  47  LYS B  49  HOH B2562  ARG D  73
SITE     3 BC9 14 THR D  75  GLU D  77  TRP D  78  VAL D  81
SITE     4 BC9 14 HOH D4445  ARG I  16
SITE     1 CC1 18 PHE A 321  HIS A 328  ILE B  41  HIS B  52
SITE     2 CC1 18 MET B  56  ASP B  57  VAL B  61  TRP B  65
SITE     3 CC1 18 LEU B  68  HOH B4201  HIS E   5  ASP E   8
SITE     4 CC1 18 PHE E  11  LEU E  41  HOH E2664  ARG I  10
SITE     5 CC1 18 ALA I  14  HOH I4186
SITE     1 CC2  4 CYS F  60  CYS F  62  CYS F  82  CYS F  85
SITE     1 CC3 11 LYS C 157  HIS C 158  GLN C 161  TYR C 172
SITE     2 CC3 11 HOH C4167  ALA F   1  ARG G  17  PHE G  21
SITE     3 CC3 11 CDL G 269  THR O  66  CHD O 229
SITE     1 CC4 23 LEU C 127  LEU C 131  LEU C 138  VAL C 254
SITE     2 CC4 23 LEU G  23  SER G  27  LEU G  30  CYS G  31
SITE     3 CC4 23 ASN G  34  LEU G  37  HIS G  38  ARG G  42
SITE     4 CC4 23 PEK G 265  PHE N 282  LEU N 283  ILE N 286
SITE     5 CC4 23 ASP N 300  TYR N 304  SER N 307  ILE N 311
SITE     6 CC4 23 ALA O  77  LEU O  78  LEU O  81
SITE     1 CC5  5 TRP C  34  MET C  40  SER G  61  TRP G  62
SITE     2 CC5  5 GLY G  63
SITE     1 CC6 13 SER G   2  ALA G   3  LYS G   5  GLY G   6
SITE     2 CC6 13 HIS G   8  LYS P  77  ARG P  80  ILE P  84
SITE     3 CC6 13 THR P  95  PHE P  98  TRP P 240  PHE P 244
SITE     4 CC6 13 VAL P 247
SITE     1 CC7  5 TYR J  32  ARG J  33  MET J  36  THR J  37
SITE     2 CC7  5 LEU J  40
SITE     1 CC8 15 THR A  17  LEU A  18  LEU A  20  LEU A  21
SITE     2 CC8 15 TRP A  25  LEU A 113  PHE A 400  ILE L  11
SITE     3 CC8 15 PRO L  12  PHE L  13  SER L  14  ARG L  20
SITE     4 CC8 15 MET L  24  PHE L  29  SER L  31
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  GLY N 125  TRP N 126
SITE     4 DC1 26 TYR N 371  PHE N 377  HIS N 378  SER N 382
SITE     5 DC1 26 PHE N 393  PHE N 425  GLN N 428  ARG N 438
SITE     6 DC1 26 ARG N 439  TYR N 440  VAL N 465  HOH N3045
SITE     7 DC1 26 HOH N3283  HOH N3700
SITE     1 DC2 30 TRP N 126  VAL N 243  TYR N 244  ILE N 247
SITE     2 DC2 30 HIS N 290  HIS N 291  ILE N 312  THR N 316
SITE     3 DC2 30 GLY N 317  VAL N 320  PHE N 321  GLY N 352
SITE     4 DC2 30 GLY N 355  ILE N 356  LEU N 358  ALA N 359
SITE     5 DC2 30 ASP N 364  HIS N 368  VAL N 373  HIS N 376
SITE     6 DC2 30 PHE N 377  VAL N 380  LEU N 381  ARG N 438
SITE     7 DC2 30 CYN N 520  HOH N3081  HOH N3183  HOH N3272
SITE     8 DC2 30 HOH N3341  PRO O  69
SITE     1 DC3  6 HIS N 240  HIS N 290  HIS N 291  HEA N 516
SITE     2 DC3  6  CU N 517  HOH N4406
SITE     1 DC4  4 HIS N 240  HIS N 290  HIS N 291  CYN 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 12 PHE N 346  ASN N 422  PHE N 426  PHE N 430
SITE     2 DC7 12 LEU N 433  LEU O   7  LEU O  28  PHE O  32
SITE     3 DC7 12 SER O  35  HOH Q3606  HOH Q4357  ARG V  43
SITE     1 DC8 20 THR N  17  LEU N  18  LEU N  20  LEU N  21
SITE     2 DC8 20 PHE N  22  TRP N  25  TRP N  81  PRO N 106
SITE     3 DC8 20 LEU N 113  PHE N 400  ILE Y  11  PRO Y  12
SITE     4 DC8 20 PHE Y  13  SER Y  14  ARG Y  20  MET Y  24
SITE     5 DC8 20 MET Y  25  PHE Y  28  PHE Y  29  HOH Y4623
SITE     1 DC9  9 ASN N 406  THR N 408  TRP N 409  ILE N 412
SITE     2 DC9  9 PHE Q  87  PRO Z  12  GLN Z  15  ALA Z  16
SITE     3 DC9  9 SER Z  20
SITE     1 EC1 16 PHE N  94  PRO N  95  ARG N  96  MET N  97
SITE     2 EC1 16 MET N 100  HOH N3085  HIS P   9  ALA P  24
SITE     3 EC1 16 ASN P  50  TRP P  57  TRP P  58  GLU P  64
SITE     4 EC1 16 HIS P  71  LEU P  79  GLY P  82  GLU P  90
SITE     1 EC2  6 HIS O 161  CYS O 196  GLU O 198  CYS O 200
SITE     2 EC2  6 HIS O 204  MET O 207
SITE     1 EC3 10 ARG G  14  ARG G  17  PHE G  21  PEK G 265
SITE     2 EC3 10 MET N 271  GLU O  62  THR O  63  THR O  66
SITE     3 EC3 10 HOH O2446  HOH O3605
SITE     1 EC4  8 HIS N 233  ASP N 300  THR N 301  TYR N 304
SITE     2 EC4  8 TRP P  99  HIS P 103  PGV P1268  HOH P3155
SITE     1 EC5 20 MET P  54  TRP P  58  VAL P  61  SER P  65
SITE     2 EC5 20 THR P  66  HIS P  71  HIS P 207  ILE P 210
SITE     3 EC5 20 PHE P 214  ARG P 221  HIS P 226  PHE P 227
SITE     4 EC5 20 HIS P 231  HIS P 232  PHE P 233  GLY P 234
SITE     5 EC5 20 CDL P1270  HOH P3253  HOH P3559  HOH S3065
SITE     1 EC6 12 ALA G   1  ASP N 298  THR P  95  TRP P  99
SITE     2 EC6 12 TYR P 102  HIS P 103  ALA P 107  CHD P1525
SITE     3 EC6 12 HOH P4315  HOH P4392  HOH P4561  ASN U  22
SITE     1 EC7 15 MET P  51  LEU P  52  TYR P  55  TRP P  58
SITE     2 EC7 15 ARG P  59  ARG P  63  PHE P  67  VAL P 217
SITE     3 EC7 15 PHE P 220  ARG P 221  LYS P 224  HIS P 226
SITE     4 EC7 15 PGV P1267  HOH P4810  LYS W   8
SITE     1 EC8  8 ARG P 156  LEU P 160  PHE P 164  PHE P 219
SITE     2 EC8  8 LEU P 223  HOH P4578  HOH P4657  PHE W   1
SITE     1 EC9  6 TRP P  34  MET P  40  HOH P4255  SER T  61
SITE     2 EC9  6 TRP T  62  GLY T  63
SITE     1 FC1 11 TRP N 334  LEU O  39  ILE O  42  THR O  47
SITE     2 FC1 11 LYS O  49  ARG Q  73  GLU Q  77  TRP Q  78
SITE     3 FC1 11 VAL Q  81  HOH Q4776  ARG V  16
SITE     1 FC2 14 PHE N 321  ILE O  41  MET O  45  HIS O  52
SITE     2 FC2 14 MET O  56  ASP O  57  HIS R   5  GLU R   6
SITE     3 FC2 14 ASP R   8  PHE R  11  ASP R  40  HOH R3664
SITE     4 FC2 14 ARG V  10  ALA V  14
SITE     1 FC3  4 CYS S  60  CYS S  62  CYS S  82  CYS S  85
SITE     1 FC4 10 GLN B  59  CHD B1085  LYS P 157  HIS P 158
SITE     2 FC4 10 GLN P 161  THR P 168  TYR P 172  ALA S   1
SITE     3 FC4 10 ARG T  17  CDL T1269
SITE     1 FC5 11 LYS C  77  ARG C  80  TYR C  81  ILE C  84
SITE     2 FC5 11 PHE C  98  TRP C 240  SER T   2  ALA T   3
SITE     3 FC5 11 LYS T   5  GLY T   6  HIS T   8
SITE     1 FC6 17 HIS N 151  TRP P  34  TYR P 181  TYR P 182
SITE     2 FC6 17 ALA P 184  PHE P 186  THR P 187  ILE P 188
SITE     3 FC6 17 PHE P 198  GLY P 202  TRP T  62  THR T  68
SITE     4 FC6 17 PHE T  69  PHE T  70  HIS T  71  ASN T  76
SITE     5 FC6 17 HOH T3350
SITE     1 FC7 25 PHE A 282  ASP A 300  TYR A 304  SER A 307
SITE     2 FC7 25 ILE A 311  ILE B  74  ALA B  77  LEU B  78
SITE     3 FC7 25 LEU B  81  TYR B  85  ASN P 125  LEU P 127
SITE     4 FC7 25 LEU P 131  LEU P 138  LEU P 250  TYR P 253
SITE     5 FC7 25 VAL P 254  PEK S1265  SER T  27  LEU T  30
SITE     6 FC7 25 CYS T  31  ASN T  34  LEU T  37  HIS T  38
SITE     7 FC7 25 HOH T4401
SITE     1 FC8  4 TYR W  32  ARG W  33  MET W  36  THR W  37
SITE     1 FC9  9 PHE N 459  TRP Q  98  LEU Z  27  LEU Z  28
SITE     2 FC9  9 GLY Z  31  TRP Z  32  LEU Z  34  TYR Z  35
SITE     3 FC9  9 HIS Z  36
CRYST1  183.364  206.648  178.137  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      0.005454  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004839  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005614        0.00000
      
PROCHECK
Go to PROCHECK summary
 References