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PDBsum entry 3i4m

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Top Page protein dna_rna metals Protein-protein interface(s) links
Transcription,transferase/DNA-RNA hybrid PDB id
3i4m
Jmol
Contents
Protein chains
1429 a.a.
1125 a.a.
270 a.a.
187 a.a.
214 a.a.
88 a.a.
171 a.a.
137 a.a.
116 a.a.
65 a.a.
116 a.a.
47 a.a.
DNA/RNA
Metals
_ZN ×8
_MG
HEADER    TRANSCRIPTION,TRANSFERASE/DNA-RNA HYBRID02-JUL-09   3I4M
TITLE     8-OXOGUANINE CONTAINING RNA POLYMERASE II ELONGATION COMPLEX D
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: RNA POLYMERASE II SUBUNIT B1, RNA POLYMERASE II SUBUNIT 1,
COMPND   5 DNA-DIRECTED RNA POLYMERASE III LARGEST SUBUNIT, RNA POLYMERASE II
COMPND   6 SUBUNIT B220;
COMPND   7 EC: 2.7.7.6;
COMPND   8 MOL_ID: 2;
COMPND   9 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2;
COMPND  10 CHAIN: B;
COMPND  11 SYNONYM: RNA POLYMERASE II SUBUNIT 2, DNA-DIRECTED RNA POLYMERASE II
COMPND  12 140 KDA POLYPEPTIDE, B150;
COMPND  13 EC: 2.7.7.6;
COMPND  14 MOL_ID: 3;
COMPND  15 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3;
COMPND  16 CHAIN: C;
COMPND  17 SYNONYM: RNA POLYMERASE II SUBUNIT B3, RNA POLYMERASE II SUBUNIT 3,
COMPND  18 DNA-DIRECTED RNA POLYMERASE II 45 KDA POLYPEPTIDE, B44.5;
COMPND  19 MOL_ID: 4;
COMPND  20 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB4;
COMPND  21 CHAIN: D;
COMPND  22 SYNONYM: RNA POLYMERASE II SUBUNIT B4, DNA-DIRECTED RNA POLYMERASE II
COMPND  23 32 KDA POLYPEPTIDE, B32;
COMPND  24 MOL_ID: 5;
COMPND  25 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC1;
COMPND  26 CHAIN: E;
COMPND  27 SYNONYM: RNA POLYMERASES I, II, AND III SUBUNIT ABC1, DNA-DIRECTED
COMPND  28 RNA POLYMERASES I, II, AND III 27 KDA POLYPEPTIDE, ABC27;
COMPND  29 MOL_ID: 6;
COMPND  30 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC2;
COMPND  31 CHAIN: F;
COMPND  32 SYNONYM: RNA POLYMERASES I, II, AND III SUBUNIT ABC2, DNA-DIRECTED
COMPND  33 RNA POLYMERASES I, II, AND III 23 KDA POLYPEPTIDE, ABC23;
COMPND  34 MOL_ID: 7;
COMPND  35 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB7;
COMPND  36 CHAIN: G;
COMPND  37 SYNONYM: RNA POLYMERASE II SUBUNIT B7, B16;
COMPND  38 MOL_ID: 8;
COMPND  39 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC3;
COMPND  40 CHAIN: H;
COMPND  41 SYNONYM: RNA POLYMERASES I, II, AND III SUBUNIT ABC3, DNA-DIRECTED
COMPND  42 RNA POLYMERASES I, II, AND III 14.5 KDA POLYPEPTIDE, ABC14.5,
COMPND  43 ABC14.4;
COMPND  44 MOL_ID: 9;
COMPND  45 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9;
COMPND  46 CHAIN: I;
COMPND  47 SYNONYM: RNA POLYMERASE II SUBUNIT B9, DNA-DIRECTED RNA POLYMERASE II
COMPND  48 SUBUNIT 9, DNA-DIRECTED RNA POLYMERASE II 14.2 KDA POLYPEPTIDE,
COMPND  49 B12.6;
COMPND  50 MOL_ID: 10;
COMPND  51 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5;
COMPND  52 CHAIN: J;
COMPND  53 SYNONYM: RNA POLYMERASES I, II, AND III SUBUNIT ABC5, DNA-DIRECTED
COMPND  54 RNA POLYMERASES I, II, AND III 8.3 KDA POLYPEPTIDE, ABC10-BETA, ABC8;
COMPND  55 MOL_ID: 11;
COMPND  56 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11;
COMPND  57 CHAIN: K;
COMPND  58 SYNONYM: RNA POLYMERASE II SUBUNIT B11, DNA-DIRECTED RNA POLYMERASE
COMPND  59 II 13.6 KDA POLYPEPTIDE, B13.6;
COMPND  60 MOL_ID: 12;
COMPND  61 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC4;
COMPND  62 CHAIN: L;
COMPND  63 SYNONYM: RNA POLYMERASES I, II, AND III SUBUNIT ABC4, ABC10-ALPHA;
COMPND  64 MOL_ID: 13;
COMPND  65 MOLECULE: DNA (5'-D(*AP*G*CP*TP*CP*AP*AP*GP*TP*AP*CP*TP*TP*AP*(8OG)
COMPND  66 P*GP*CP*CP*(BRU)P*GP*GP*TP*CP*AP*TP*T)-3');
COMPND  67 CHAIN: T;
COMPND  68 ENGINEERED: YES;
COMPND  69 MOL_ID: 14;
COMPND  70 MOLECULE: DNA (5'-D(*AP*GP*TP*AP*CP*TP*TP*GP*AP*GP*CP*T)-3');
COMPND  71 CHAIN: N;
COMPND  72 ENGINEERED: YES;
COMPND  73 MOL_ID: 15;
COMPND  74 MOLECULE: RNA (5'-R(*UP*GP*CP*AP*UP*C*UP*UP*CP*CP*AP*GP*GP*CP*CP*U)-
COMPND  75 3');
COMPND  76 CHAIN: P;
COMPND  77 ENGINEERED: YES
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE   4 ORGANISM_TAXID: 4932;
SOURCE   5 MOL_ID: 2;
SOURCE   6 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE   7 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE   8 ORGANISM_TAXID: 4932;
SOURCE   9 MOL_ID: 3;
SOURCE  10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  12 ORGANISM_TAXID: 4932;
SOURCE  13 MOL_ID: 4;
SOURCE  14 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  15 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  16 ORGANISM_TAXID: 4932;
SOURCE  17 MOL_ID: 5;
SOURCE  18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  20 ORGANISM_TAXID: 4932;
SOURCE  21 MOL_ID: 6;
SOURCE  22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  24 ORGANISM_TAXID: 4932;
SOURCE  25 MOL_ID: 7;
SOURCE  26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  27 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  28 ORGANISM_TAXID: 4932;
SOURCE  29 MOL_ID: 8;
SOURCE  30 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  31 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  32 ORGANISM_TAXID: 4932;
SOURCE  33 MOL_ID: 9;
SOURCE  34 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  35 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  36 ORGANISM_TAXID: 4932;
SOURCE  37 MOL_ID: 10;
SOURCE  38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  39 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  40 ORGANISM_TAXID: 4932;
SOURCE  41 MOL_ID: 11;
SOURCE  42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  44 ORGANISM_TAXID: 4932;
SOURCE  45 MOL_ID: 12;
SOURCE  46 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  47 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  48 ORGANISM_TAXID: 4932;
SOURCE  49 MOL_ID: 13;
SOURCE  50 SYNTHETIC: YES;
SOURCE  51 MOL_ID: 14;
SOURCE  52 SYNTHETIC: YES;
SOURCE  53 MOL_ID: 15;
SOURCE  54 SYNTHETIC: YES
KEYWDS    RNA POLYMERASE II, METAL-BINDING, TRANSCRIPTION BUBBLE, ELONGATION
KEYWDS   2 COMPLEX, TRANSCRIPTION, 8-OXOGUANINE, OXIDATIVE DAMAGE, DNA DAMAGE,
KEYWDS   3 DNA-BINDING, DNA-DIRECTED RNA POLYMERASE, ISOPEPTIDE BOND,
KEYWDS   4 MAGNESIUM, NUCLEOTIDYLTRANSFERASE, NUCLEUS, PHOSPHOPROTEIN,
KEYWDS   5 TRANSFERASE, ZINC-FINGER, DNA REPAIR, MRNA PROCESSING,
KEYWDS   6 TRANSCRIPTION,TRANSFERASE-DNA-RNA HYBRID COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    G.E.DAMSMA,P.CRAMER
REVDAT   2   16-JAN-13 3I4M    1       JRNL   VERSN
REVDAT   1   08-SEP-09 3I4M    0
JRNL        AUTH   G.E.DAMSMA,P.CRAMER
JRNL        TITL   MOLECULAR BASIS OF TRANSCRIPTIONAL MUTAGENESIS AT
JRNL        TITL 2 8-OXOGUANINE
JRNL        REF    J.BIOL.CHEM.                  V. 284 31658 2009
JRNL        REFN                   ISSN 0021-9258
JRNL        PMID   19758983
JRNL        DOI    10.1074/JBC.M109.022764
REMARK   2
REMARK   2 RESOLUTION.    3.70 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS 1.2
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK   3               : READ,RICE,SIMONSON,WARREN
REMARK   3
REMARK   3  REFINEMENT TARGET : NULL
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.70
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6
REMARK   3   NUMBER OF REFLECTIONS             : 250702
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : THE SAME SET OF REFLECTIONS
REMARK   3                                      THAT HAS BEEN EXCLUDED FROM
REMARK   3                                      PREVIOUS POL II STRUCTURE
REMARK   3                                      DETERMINATIONS HAVE BEEN USED.
REMARK   3                                      KETTENBERG ET AL. MOL. CELL
REMARK   3                                      16, 955-965 (2004)
REMARK   3   R VALUE            (WORKING SET) : 0.225
REMARK   3   FREE R VALUE                     : 0.258
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL
REMARK   3   BIN R VALUE           (WORKING SET) : NULL
REMARK   3   BIN FREE R VALUE                    : NULL
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 31491
REMARK   3   NUCLEIC ACID ATOMS       : 855
REMARK   3   HETEROGEN ATOMS          : 9
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : 0.008
REMARK   3   BOND ANGLES            (DEGREES) : 1.50
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELING.
REMARK   3   METHOD USED : NULL
REMARK   3   KSOL        : NULL
REMARK   3   BSOL        : NULL
REMARK   3
REMARK   3  NCS MODEL : NULL
REMARK   3
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  PARAMETER FILE  1  : NULL
REMARK   3  TOPOLOGY FILE  1   : NULL
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: NULL
REMARK   4
REMARK   4 3I4M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JUL-09.
REMARK 100 THE RCSB ID CODE IS RCSB053957.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 23-NOV-07
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 7.0
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SLS
REMARK 200  BEAMLINE                       : X06SA
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9188
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : PIXEL
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200  DATA SCALING SOFTWARE          : XSCALE
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 250702
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.700
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6
REMARK 200  DATA REDUNDANCY                : 3.800
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.08200
REMARK 200   FOR THE DATA SET  : 11.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.70
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.80
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.56700
REMARK 200   FOR SHELL         : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1Y1W WITHOUT NUCLEIC ACIDS
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 78.51
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM AMMONIUM ACETATE, 300MM SODIUM
REMARK 280  ACETATE, 50MM HEPES, 4%(W/V) PEG 6000, 5MM TCEP, PH 7.0, VAPOR
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z+1/2
REMARK 290       3555   -X,Y,-Z+1/2
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2
REMARK 290       8555   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        0.00000
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      140.72750
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      140.72750
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000      110.32300
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      196.00150
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000      110.32300
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      196.00150
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      140.72750
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000      110.32300
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      196.00150
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      140.72750
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000      110.32300
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      196.00150
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTADECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350                    AND CHAINS: J, K, L, T, N, P
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 A     1
REMARK 465     ASN A  1082
REMARK 465     THR A  1083
REMARK 465     PHE A  1084
REMARK 465     HIS A  1085
REMARK 465     PHE A  1086
REMARK 465     ALA A  1087
REMARK 465     GLY A  1088
REMARK 465     VAL A  1089
REMARK 465     ALA A  1090
REMARK 465     SER A  1091
REMARK 465     LYS A  1092
REMARK 465     GLU A  1180
REMARK 465     ALA A  1181
REMARK 465     GLU A  1182
REMARK 465     GLN A  1183
REMARK 465     SER A  1184
REMARK 465     PHE A  1185
REMARK 465     ASP A  1186
REMARK 465     SER A  1247
REMARK 465     LEU A  1248
REMARK 465     ASP A  1249
REMARK 465     ALA A  1250
REMARK 465     GLU A  1251
REMARK 465     THR A  1252
REMARK 465     GLU A  1253
REMARK 465     GLU A  1456
REMARK 465     GLN A  1457
REMARK 465     LYS A  1458
REMARK 465     ILE A  1459
REMARK 465     THR A  1460
REMARK 465     GLU A  1461
REMARK 465     ILE A  1462
REMARK 465     GLU A  1463
REMARK 465     ASP A  1464
REMARK 465     GLY A  1465
REMARK 465     GLN A  1466
REMARK 465     ASP A  1467
REMARK 465     GLY A  1468
REMARK 465     GLY A  1469
REMARK 465     VAL A  1470
REMARK 465     THR A  1471
REMARK 465     PRO A  1472
REMARK 465     TYR A  1473
REMARK 465     SER A  1474
REMARK 465     ASN A  1475
REMARK 465     GLU A  1476
REMARK 465     SER A  1477
REMARK 465     GLY A  1478
REMARK 465     LEU A  1479
REMARK 465     VAL A  1480
REMARK 465     ASN A  1481
REMARK 465     ALA A  1482
REMARK 465     ASP A  1483
REMARK 465     LEU A  1484
REMARK 465     ASP A  1485
REMARK 465     VAL A  1486
REMARK 465     LYS A  1487
REMARK 465     ASP A  1488
REMARK 465     GLU A  1489
REMARK 465     LEU A  1490
REMARK 465     MET A  1491
REMARK 465     PHE A  1492
REMARK 465     SER A  1493
REMARK 465     PRO A  1494
REMARK 465     LEU A  1495
REMARK 465     VAL A  1496
REMARK 465     ASP A  1497
REMARK 465     SER A  1498
REMARK 465     GLY A  1499
REMARK 465     SER A  1500
REMARK 465     ASN A  1501
REMARK 465     ASP A  1502
REMARK 465     ALA A  1503
REMARK 465     MET A  1504
REMARK 465     ALA A  1505
REMARK 465     GLY A  1506
REMARK 465     GLY A  1507
REMARK 465     PHE A  1508
REMARK 465     THR A  1509
REMARK 465     ALA A  1510
REMARK 465     TYR A  1511
REMARK 465     GLY A  1512
REMARK 465     GLY A  1513
REMARK 465     ALA A  1514
REMARK 465     ASP A  1515
REMARK 465     TYR A  1516
REMARK 465     GLY A  1517
REMARK 465     GLU A  1518
REMARK 465     ALA A  1519
REMARK 465     THR A  1520
REMARK 465     SER A  1521
REMARK 465     PRO A  1522
REMARK 465     PHE A  1523
REMARK 465     GLY A  1524
REMARK 465     ALA A  1525
REMARK 465     TYR A  1526
REMARK 465     GLY A  1527
REMARK 465     GLU A  1528
REMARK 465     ALA A  1529
REMARK 465     PRO A  1530
REMARK 465     THR A  1531
REMARK 465     SER A  1532
REMARK 465     PRO A  1533
REMARK 465     GLY A  1534
REMARK 465     PHE A  1535
REMARK 465     GLY A  1536
REMARK 465     VAL A  1537
REMARK 465     SER A  1538
REMARK 465     SER A  1539
REMARK 465     PRO A  1540
REMARK 465     GLY A  1541
REMARK 465     PHE A  1542
REMARK 465     SER A  1543
REMARK 465     PRO A  1544
REMARK 465     THR A  1545
REMARK 465     SER A  1546
REMARK 465     PRO A  1547
REMARK 465     THR A  1548
REMARK 465     TYR A  1549
REMARK 465     SER A  1550
REMARK 465     PRO A  1551
REMARK 465     THR A  1552
REMARK 465     SER A  1553
REMARK 465     PRO A  1554
REMARK 465     ALA A  1555
REMARK 465     TYR A  1556
REMARK 465     SER A  1557
REMARK 465     PRO A  1558
REMARK 465     THR A  1559
REMARK 465     SER A  1560
REMARK 465     PRO A  1561
REMARK 465     SER A  1562
REMARK 465     TYR A  1563
REMARK 465     SER A  1564
REMARK 465     PRO A  1565
REMARK 465     THR A  1566
REMARK 465     SER A  1567
REMARK 465     PRO A  1568
REMARK 465     SER A  1569
REMARK 465     TYR A  1570
REMARK 465     SER A  1571
REMARK 465     PRO A  1572
REMARK 465     THR A  1573
REMARK 465     SER A  1574
REMARK 465     PRO A  1575
REMARK 465     SER A  1576
REMARK 465     TYR A  1577
REMARK 465     SER A  1578
REMARK 465     PRO A  1579
REMARK 465     THR A  1580
REMARK 465     SER A  1581
REMARK 465     PRO A  1582
REMARK 465     SER A  1583
REMARK 465     TYR A  1584
REMARK 465     SER A  1585
REMARK 465     PRO A  1586
REMARK 465     THR A  1587
REMARK 465     SER A  1588
REMARK 465     PRO A  1589
REMARK 465     SER A  1590
REMARK 465     TYR A  1591
REMARK 465     SER A  1592
REMARK 465     PRO A  1593
REMARK 465     THR A  1594
REMARK 465     SER A  1595
REMARK 465     PRO A  1596
REMARK 465     SER A  1597
REMARK 465     TYR A  1598
REMARK 465     SER A  1599
REMARK 465     PRO A  1600
REMARK 465     THR A  1601
REMARK 465     SER A  1602
REMARK 465     PRO A  1603
REMARK 465     SER A  1604
REMARK 465     TYR A  1605
REMARK 465     SER A  1606
REMARK 465     PRO A  1607
REMARK 465     THR A  1608
REMARK 465     SER A  1609
REMARK 465     PRO A  1610
REMARK 465     SER A  1611
REMARK 465     TYR A  1612
REMARK 465     SER A  1613
REMARK 465     PRO A  1614
REMARK 465     THR A  1615
REMARK 465     SER A  1616
REMARK 465     PRO A  1617
REMARK 465     SER A  1618
REMARK 465     TYR A  1619
REMARK 465     SER A  1620
REMARK 465     PRO A  1621
REMARK 465     THR A  1622
REMARK 465     SER A  1623
REMARK 465     PRO A  1624
REMARK 465     SER A  1625
REMARK 465     TYR A  1626
REMARK 465     SER A  1627
REMARK 465     PRO A  1628
REMARK 465     THR A  1629
REMARK 465     SER A  1630
REMARK 465     PRO A  1631
REMARK 465     SER A  1632
REMARK 465     TYR A  1633
REMARK 465     SER A  1634
REMARK 465     PRO A  1635
REMARK 465     THR A  1636
REMARK 465     SER A  1637
REMARK 465     PRO A  1638
REMARK 465     SER A  1639
REMARK 465     TYR A  1640
REMARK 465     SER A  1641
REMARK 465     PRO A  1642
REMARK 465     THR A  1643
REMARK 465     SER A  1644
REMARK 465     PRO A  1645
REMARK 465     SER A  1646
REMARK 465     TYR A  1647
REMARK 465     SER A  1648
REMARK 465     PRO A  1649
REMARK 465     THR A  1650
REMARK 465     SER A  1651
REMARK 465     PRO A  1652
REMARK 465     SER A  1653
REMARK 465     TYR A  1654
REMARK 465     SER A  1655
REMARK 465     PRO A  1656
REMARK 465     THR A  1657
REMARK 465     SER A  1658
REMARK 465     PRO A  1659
REMARK 465     ALA A  1660
REMARK 465     TYR A  1661
REMARK 465     SER A  1662
REMARK 465     PRO A  1663
REMARK 465     THR A  1664
REMARK 465     SER A  1665
REMARK 465     PRO A  1666
REMARK 465     SER A  1667
REMARK 465     TYR A  1668
REMARK 465     SER A  1669
REMARK 465     PRO A  1670
REMARK 465     THR A  1671
REMARK 465     SER A  1672
REMARK 465     PRO A  1673
REMARK 465     SER A  1674
REMARK 465     TYR A  1675
REMARK 465     SER A  1676
REMARK 465     PRO A  1677
REMARK 465     THR A  1678
REMARK 465     SER A  1679
REMARK 465     PRO A  1680
REMARK 465     SER A  1681
REMARK 465     TYR A  1682
REMARK 465     SER A  1683
REMARK 465     PRO A  1684
REMARK 465     THR A  1685
REMARK 465     SER A  1686
REMARK 465     PRO A  1687
REMARK 465     SER A  1688
REMARK 465     TYR A  1689
REMARK 465     SER A  1690
REMARK 465     PRO A  1691
REMARK 465     THR A  1692
REMARK 465     SER A  1693
REMARK 465     PRO A  1694
REMARK 465     ASN A  1695
REMARK 465     TYR A  1696
REMARK 465     SER A  1697
REMARK 465     PRO A  1698
REMARK 465     THR A  1699
REMARK 465     SER A  1700
REMARK 465     PRO A  1701
REMARK 465     SER A  1702
REMARK 465     TYR A  1703
REMARK 465     SER A  1704
REMARK 465     PRO A  1705
REMARK 465     THR A  1706
REMARK 465     SER A  1707
REMARK 465     PRO A  1708
REMARK 465     GLY A  1709
REMARK 465     TYR A  1710
REMARK 465     SER A  1711
REMARK 465     PRO A  1712
REMARK 465     GLY A  1713
REMARK 465     SER A  1714
REMARK 465     PRO A  1715
REMARK 465     ALA A  1716
REMARK 465     TYR A  1717
REMARK 465     SER A  1718
REMARK 465     PRO A  1719
REMARK 465     LYS A  1720
REMARK 465     GLN A  1721
REMARK 465     ASP A  1722
REMARK 465     GLU A  1723
REMARK 465     GLN A  1724
REMARK 465     LYS A  1725
REMARK 465     HIS A  1726
REMARK 465     ASN A  1727
REMARK 465     GLU A  1728
REMARK 465     ASN A  1729
REMARK 465     GLU A  1730
REMARK 465     ASN A  1731
REMARK 465     SER A  1732
REMARK 465     ARG A  1733
REMARK 465     MET B     1
REMARK 465     SER B     2
REMARK 465     ASP B     3
REMARK 465     LEU B     4
REMARK 465     ALA B     5
REMARK 465     ASN B     6
REMARK 465     SER B     7
REMARK 465     GLU B     8
REMARK 465     LYS B     9
REMARK 465     TYR B    10
REMARK 465     TYR B    11
REMARK 465     ASP B    12
REMARK 465     GLU B    13
REMARK 465     ASP B    14
REMARK 465     PRO B    15
REMARK 465     TYR B    16
REMARK 465     GLY B    17
REMARK 465     PHE B    18
REMARK 465     GLU B    19
REMARK 465     LEU B    71
REMARK 465     GLU B    72
REMARK 465     GLN B    73
REMARK 465     LEU B    74
REMARK 465     ALA B    75
REMARK 465     GLN B    76
REMARK 465     HIS B    77
REMARK 465     THR B    78
REMARK 465     THR B    79
REMARK 465     GLU B    80
REMARK 465     SER B    81
REMARK 465     ASP B    82
REMARK 465     ASN B    83
REMARK 465     ILE B    84
REMARK 465     SER B    85
REMARK 465     ARG B    86
REMARK 465     LYS B    87
REMARK 465     TYR B    88
REMARK 465     GLU B    89
REMARK 465     ALA B   139
REMARK 465     ILE B   140
REMARK 465     ASP B   141
REMARK 465     VAL B   142
REMARK 465     PRO B   143
REMARK 465     GLY B   144
REMARK 465     ARG B   145
REMARK 465     GLU B   146
REMARK 465     LEU B   147
REMARK 465     LYS B   148
REMARK 465     TYR B   149
REMARK 465     GLU B   150
REMARK 465     LEU B   151
REMARK 465     ILE B   152
REMARK 465     ALA B   153
REMARK 465     GLU B   154
REMARK 465     GLU B   155
REMARK 465     SER B   156
REMARK 465     GLU B   157
REMARK 465     ASP B   158
REMARK 465     ASP B   159
REMARK 465     SER B   160
REMARK 465     GLU B   161
REMARK 465     SER B   162
REMARK 465     GLY B   163
REMARK 465     GLU B   438
REMARK 465     ALA B   439
REMARK 465     HIS B   440
REMARK 465     ASP B   441
REMARK 465     PHE B   442
REMARK 465     ASN B   443
REMARK 465     MET B   444
REMARK 465     LYS B   445
REMARK 465     ILE B   669
REMARK 465     GLU B   670
REMARK 465     GLY B   671
REMARK 465     GLY B   672
REMARK 465     PHE B   673
REMARK 465     GLU B   674
REMARK 465     ASP B   675
REMARK 465     VAL B   676
REMARK 465     GLU B   677
REMARK 465     ASN B   716
REMARK 465     GLU B   717
REMARK 465     GLU B   718
REMARK 465     ASN B   719
REMARK 465     ASP B   720
REMARK 465     LEU B   721
REMARK 465     PRO B   920
REMARK 465     ASP B   921
REMARK 465     GLU B   922
REMARK 465     GLU B   923
REMARK 465     GLU B   924
REMARK 465     LEU B   925
REMARK 465     GLY B   926
REMARK 465     GLN B   927
REMARK 465     ARG B   928
REMARK 465     THR B   929
REMARK 465     ALA B   930
REMARK 465     TYR B   931
REMARK 465     HIS B   932
REMARK 465     HIS C    -5
REMARK 465     HIS C    -4
REMARK 465     HIS C    -3
REMARK 465     HIS C    -2
REMARK 465     HIS C    -1
REMARK 465     HIS C     0
REMARK 465     ASN C   271
REMARK 465     PHE C   272
REMARK 465     ALA C   273
REMARK 465     SER C   274
REMARK 465     GLY C   275
REMARK 465     ASP C   276
REMARK 465     ASN C   277
REMARK 465     ASN C   278
REMARK 465     THR C   279
REMARK 465     ALA C   280
REMARK 465     SER C   281
REMARK 465     ASN C   282
REMARK 465     MET C   283
REMARK 465     LEU C   284
REMARK 465     GLY C   285
REMARK 465     SER C   286
REMARK 465     ASN C   287
REMARK 465     GLU C   288
REMARK 465     ASP C   289
REMARK 465     VAL C   290
REMARK 465     MET C   291
REMARK 465     MET C   292
REMARK 465     THR C   293
REMARK 465     GLY C   294
REMARK 465     ALA C   295
REMARK 465     GLU C   296
REMARK 465     GLN C   297
REMARK 465     ASP C   298
REMARK 465     PRO C   299
REMARK 465     TYR C   300
REMARK 465     SER C   301
REMARK 465     ASN C   302
REMARK 465     ALA C   303
REMARK 465     SER C   304
REMARK 465     GLN C   305
REMARK 465     MET C   306
REMARK 465     GLY C   307
REMARK 465     ASN C   308
REMARK 465     THR C   309
REMARK 465     GLY C   310
REMARK 465     SER C   311
REMARK 465     GLY C   312
REMARK 465     GLY C   313
REMARK 465     TYR C   314
REMARK 465     ASP C   315
REMARK 465     ASN C   316
REMARK 465     ALA C   317
REMARK 465     TRP C   318
REMARK 465     HIS D    77
REMARK 465     LYS D    78
REMARK 465     LYS D    79
REMARK 465     LYS D    80
REMARK 465     HIS D    81
REMARK 465     LEU D    82
REMARK 465     LYS D    83
REMARK 465     HIS D    84
REMARK 465     GLU D    85
REMARK 465     ASN D    86
REMARK 465     ALA D    87
REMARK 465     ASN D    88
REMARK 465     ASP D    89
REMARK 465     GLU D    90
REMARK 465     THR D    91
REMARK 465     THR D    92
REMARK 465     ALA D    93
REMARK 465     VAL D    94
REMARK 465     GLU D    95
REMARK 465     ASP D    96
REMARK 465     GLU D    97
REMARK 465     ASP D    98
REMARK 465     ASP D    99
REMARK 465     ASP D   100
REMARK 465     LEU D   101
REMARK 465     ASP D   102
REMARK 465     GLU D   103
REMARK 465     ASP D   104
REMARK 465     ASP D   105
REMARK 465     VAL D   106
REMARK 465     ASN D   107
REMARK 465     ALA D   108
REMARK 465     ASP D   109
REMARK 465     ASP D   110
REMARK 465     MET E     1
REMARK 465     MET F     1
REMARK 465     SER F     2
REMARK 465     ASP F     3
REMARK 465     TYR F     4
REMARK 465     GLU F     5
REMARK 465     GLU F     6
REMARK 465     ALA F     7
REMARK 465     PHE F     8
REMARK 465     ASN F     9
REMARK 465     ASP F    10
REMARK 465     GLY F    11
REMARK 465     ASN F    12
REMARK 465     GLU F    13
REMARK 465     ASN F    14
REMARK 465     PHE F    15
REMARK 465     GLU F    16
REMARK 465     ASP F    17
REMARK 465     PHE F    18
REMARK 465     ASP F    19
REMARK 465     VAL F    20
REMARK 465     GLU F    21
REMARK 465     HIS F    22
REMARK 465     PHE F    23
REMARK 465     SER F    24
REMARK 465     ASP F    25
REMARK 465     GLU F    26
REMARK 465     GLU F    27
REMARK 465     THR F    28
REMARK 465     TYR F    29
REMARK 465     GLU F    30
REMARK 465     GLU F    31
REMARK 465     LYS F    32
REMARK 465     PRO F    33
REMARK 465     GLN F    34
REMARK 465     PHE F    35
REMARK 465     LYS F    36
REMARK 465     ASP F    37
REMARK 465     GLY F    38
REMARK 465     GLU F    39
REMARK 465     THR F    40
REMARK 465     THR F    41
REMARK 465     ASP F    42
REMARK 465     ALA F    43
REMARK 465     ASN F    44
REMARK 465     GLY F    45
REMARK 465     LYS F    46
REMARK 465     THR F    47
REMARK 465     ILE F    48
REMARK 465     VAL F    49
REMARK 465     THR F    50
REMARK 465     GLY F    51
REMARK 465     GLY F    52
REMARK 465     ASN F    53
REMARK 465     GLY F    54
REMARK 465     PRO F    55
REMARK 465     GLU F    56
REMARK 465     ASP F    57
REMARK 465     PHE F    58
REMARK 465     GLN F    59
REMARK 465     GLN F    60
REMARK 465     HIS F    61
REMARK 465     GLU F    62
REMARK 465     GLN F    63
REMARK 465     ILE F    64
REMARK 465     ARG F    65
REMARK 465     ARG F    66
REMARK 465     LYS F    67
REMARK 465     ASP H    67
REMARK 465     THR H    68
REMARK 465     PRO H    69
REMARK 465     ALA H    70
REMARK 465     ASN H    71
REMARK 465     ASP H    72
REMARK 465     SER H    73
REMARK 465     SER H    74
REMARK 465     ALA H    75
REMARK 465     MET I     1
REMARK 465     ARG I   118
REMARK 465     THR I   119
REMARK 465     GLN I   120
REMARK 465     PHE I   121
REMARK 465     SER I   122
REMARK 465     LEU J    66
REMARK 465     GLU J    67
REMARK 465     LYS J    68
REMARK 465     ARG J    69
REMARK 465     ASP J    70
REMARK 465     ASP K   117
REMARK 465     ASP K   118
REMARK 465     ALA K   119
REMARK 465     PHE K   120
REMARK 465     MET L     1
REMARK 465     SER L     2
REMARK 465     ARG L     3
REMARK 465     GLU L     4
REMARK 465     GLY L     5
REMARK 465     PHE L     6
REMARK 465     GLN L     7
REMARK 465     ILE L     8
REMARK 465     PRO L     9
REMARK 465     THR L    10
REMARK 465     ASN L    11
REMARK 465     LEU L    12
REMARK 465     ASP L    13
REMARK 465     ALA L    14
REMARK 465     ALA L    15
REMARK 465     ALA L    16
REMARK 465     ALA L    17
REMARK 465     GLY L    18
REMARK 465     THR L    19
REMARK 465     SER L    20
REMARK 465     GLN L    21
REMARK 465     ALA L    22
REMARK 465     ARG L    23
REMARK 465      DA T     5
REMARK 465      DG T     6
REMARK 465      DA T    28
REMARK 465      DT T    29
REMARK 465      DT T    30
REMARK 465      DT N    12
REMARK 465       U P    -4
REMARK 465       G P    -3
REMARK 465       C P    -2
REMARK 465       A P    -1
REMARK 465       U P     0
REMARK 465       C P     1
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470     ASP D 111    CG   OD1  OD2
REMARK 470     ASP D 112    CG   OD1  OD2
REMARK 470      DC T   7    P    OP1  OP2
REMARK 470       U P   2    P    OP1  OP2
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    GLY A   665     N    GLY A   667              2.06
REMARK 500   O    ASP A    42     N    THR A    44              2.11
REMARK 500   O    THR A    69     N    GLN A    71              2.13
REMARK 500   O    ASP B   294     N    GLU B   296              2.17
REMARK 500   N    GLN B   843     O    TYR B   994              2.19
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    PRO A  56   C   -  N   -  CA  ANGL. DEV. = -10.5 DEGREES
REMARK 500    PRO A 172   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES
REMARK 500    PRO A 514   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES
REMARK 500     DC T  21   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES
REMARK 500     DG T  25   O4' -  C1' -  N9  ANGL. DEV. =   1.9 DEGREES
REMARK 500     DT N   3   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    GLN A   4      175.61     38.71
REMARK 500    GLN A   5      109.50     55.93
REMARK 500    SER A   8        6.61    -56.85
REMARK 500    ILE A  35       78.21     39.09
REMARK 500    MET A  41     -114.58    173.74
REMARK 500    ASP A  42      107.82     53.53
REMARK 500    GLU A  43       65.07    -54.33
REMARK 500    THR A  44       82.23     47.86
REMARK 500    GLN A  45      -52.34     78.76
REMARK 500    ALA A  48     -138.51    160.89
REMARK 500    ASN A  54       91.93     49.40
REMARK 500    ARG A  57      -44.02    170.95
REMARK 500    LEU A  58     -178.70    -40.54
REMARK 500    ASP A  62       88.68     62.52
REMARK 500    ARG A  63       78.78      1.85
REMARK 500    LYS A  66      134.33    -30.23
REMARK 500    CYS A  67       66.03    171.50
REMARK 500    THR A  69      -50.79     61.20
REMARK 500    CYS A  70      -22.06    -27.07
REMARK 500    GLN A  71     -143.61     39.32
REMARK 500    GLU A  72       69.18     64.68
REMARK 500    MET A  74      -84.19     22.59
REMARK 500    GLU A  76      -66.56    128.72
REMARK 500    CYS A  77       95.62    -69.38
REMARK 500    PRO A  78     -173.43    -66.42
REMARK 500    PHE A  81      146.30    -39.53
REMARK 500    ILE A  84       88.56   -165.90
REMARK 500    VAL A  93      -34.19    -26.33
REMARK 500    ILE A  96      -66.54    -26.45
REMARK 500    GLU A 104       -9.61    -58.72
REMARK 500    HIS A 109      -57.39     78.75
REMARK 500    LEU A 115       84.18   -156.76
REMARK 500    LEU A 126       12.50    -58.14
REMARK 500    ASP A 130      101.64    155.67
REMARK 500    SER A 131        4.47    -51.24
REMARK 500    LYS A 132      -52.84   -131.91
REMARK 500    CYS A 148       84.48    -60.72
REMARK 500    PRO A 153       97.24    -61.68
REMARK 500    SER A 154      171.78    -39.83
REMARK 500    GLU A 155       13.84    -65.65
REMARK 500    ASP A 156     -166.14   -124.90
REMARK 500    PRO A 158       19.47    -65.29
REMARK 500    ARG A 164     -116.95   -151.31
REMARK 500    CYS A 167      104.94     15.29
REMARK 500    ASN A 169      118.00    -20.93
REMARK 500    TRP A 185     -157.25    -77.35
REMARK 500    LYS A 186     -105.17   -156.54
REMARK 500    LYS A 187       86.72     88.67
REMARK 500    ASP A 188      170.27     62.44
REMARK 500    ARG A 189       88.56   -152.44
REMARK 500
REMARK 500 THIS ENTRY HAS     894 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        RMS     TYPE
REMARK 500    TYR A1035         0.07    SIDE CHAIN
REMARK 500    TYR B 797         0.07    SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
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                              ZN A2457  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  67   SG
REMARK 620 2 CYS A  70   SG  133.6
REMARK 620 3 CYS A  77   SG   80.1 104.4
REMARK 620 4 HIS A  80   NE2 126.3 100.1  85.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A2456  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 107   SG
REMARK 620 2 CYS A 110   SG  113.8
REMARK 620 3 CYS A 148   SG   97.8  92.6
REMARK 620 4 CYS A 167   SG  145.9  91.6 103.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A2458  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 481   OD1
REMARK 620 2 ASP A 483   OD2  91.3
REMARK 620 3 ASP A 485   OD2  59.0 118.2
REMARK 620 4   C P  10   O3' 120.0 129.1 112.4
REMARK 620 5   U P  11   OP2  59.8 119.3  92.3  61.7
REMARK 620 6 ASP A 485   OD1  92.0 159.6  48.4  65.2  79.4
REMARK 620 7   U P  11   O5'  99.1  85.9 145.5  52.5  53.4 113.4
REMARK 620 N                    1     2     3     4     5     6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B2225  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1163   SG
REMARK 620 2 CYS B1166   SG   82.8
REMARK 620 3 CYS B1182   SG   95.5 152.3
REMARK 620 4 CYS B1185   SG   75.0  79.0 127.5
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN C1269  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C  86   SG
REMARK 620 2 CYS C  88   SG  101.3
REMARK 620 3 CYS C  92   SG   99.6  81.2
REMARK 620 4 CYS C  95   SG  148.0  99.4 107.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN I1121  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I   7   SG
REMARK 620 2 CYS I  10   SG  105.1
REMARK 620 3 CYS I  29   SG  109.5 117.2
REMARK 620 4 CYS I  32   SG  121.0 114.2  89.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN I1122  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I  75   SG
REMARK 620 2 CYS I  78   SG   75.1
REMARK 620 3 CYS I 106   SG  151.1  77.5
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN J1066  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J   7   SG
REMARK 620 2 CYS J  10   SG  124.5
REMARK 620 3 CYS J  45   SG  130.0  83.5
REMARK 620 4 CYS J  46   SG  133.7  84.7  83.4
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN L1071  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L  31   SG
REMARK 620 2 CYS L  34   SG   75.9
REMARK 620 3 CYS L  48   SG  109.5  85.3
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2458
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2456
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2457
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2225
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 1269
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 1121
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 1122
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 1066
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 1071
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3I4N   RELATED DB: PDB
DBREF  3I4M A    1  1733  UNP    P04050   RPB1_YEAST       1   1733
DBREF  3I4M B    1  1224  UNP    P08518   RPB2_YEAST       1   1224
DBREF  3I4M C    1   318  UNP    P16370   RPB3_YEAST       1    318
DBREF  3I4M D    1   221  UNP    P20433   RPB4_YEAST       1    221
DBREF  3I4M E    1   215  UNP    P20434   RPAB1_YEAST      1    215
DBREF  3I4M F    1   155  UNP    P20435   RPAB2_YEAST      1    155
DBREF  3I4M G    1   171  UNP    P34087   RPB7_YEAST       1    171
DBREF  3I4M H    1   146  UNP    P20436   RPAB3_YEAST      1    146
DBREF  3I4M I    1   122  UNP    P27999   RPB9_YEAST       1    122
DBREF  3I4M J    1    70  UNP    P22139   RPAB5_YEAST      1     70
DBREF  3I4M K    1   120  UNP    P38902   RPB11_YEAST      1    120
DBREF  3I4M L    1    70  UNP    P40422   RPAB4_YEAST      1     70
DBREF  3I4M T    5    30  PDB    3I4M     3I4M             5     30
DBREF  3I4M N    1    12  PDB    3I4M     3I4M             1     12
DBREF  3I4M P   -4    11  PDB    3I4M     3I4M            -4     11
SEQADV 3I4M HIS C   -5  UNP  P16370              EXPRESSION TAG
SEQADV 3I4M HIS C   -4  UNP  P16370              EXPRESSION TAG
SEQADV 3I4M HIS C   -3  UNP  P16370              EXPRESSION TAG
SEQADV 3I4M HIS C   -2  UNP  P16370              EXPRESSION TAG
SEQADV 3I4M HIS C   -1  UNP  P16370              EXPRESSION TAG
SEQADV 3I4M HIS C    0  UNP  P16370              EXPRESSION TAG
SEQRES   1 A 1733  MET VAL GLY GLN GLN TYR SER SER ALA PRO LEU ARG THR
SEQRES   2 A 1733  VAL LYS GLU VAL GLN PHE GLY LEU PHE SER PRO GLU GLU
SEQRES   3 A 1733  VAL ARG ALA ILE SER VAL ALA LYS ILE ARG PHE PRO GLU
SEQRES   4 A 1733  THR MET ASP GLU THR GLN THR ARG ALA LYS ILE GLY GLY
SEQRES   5 A 1733  LEU ASN ASP PRO ARG LEU GLY SER ILE ASP ARG ASN LEU
SEQRES   6 A 1733  LYS CYS GLN THR CYS GLN GLU GLY MET ASN GLU CYS PRO
SEQRES   7 A 1733  GLY HIS PHE GLY HIS ILE ASP LEU ALA LYS PRO VAL PHE
SEQRES   8 A 1733  HIS VAL GLY PHE ILE ALA LYS ILE LYS LYS VAL CYS GLU
SEQRES   9 A 1733  CYS VAL CYS MET HIS CYS GLY LYS LEU LEU LEU ASP GLU
SEQRES  10 A 1733  HIS ASN GLU LEU MET ARG GLN ALA LEU ALA ILE LYS ASP
SEQRES  11 A 1733  SER LYS LYS ARG PHE ALA ALA ILE TRP THR LEU CYS LYS
SEQRES  12 A 1733  THR LYS MET VAL CYS GLU THR ASP VAL PRO SER GLU ASP
SEQRES  13 A 1733  ASP PRO THR GLN LEU VAL SER ARG GLY GLY CYS GLY ASN
SEQRES  14 A 1733  THR GLN PRO THR ILE ARG LYS ASP GLY LEU LYS LEU VAL
SEQRES  15 A 1733  GLY SER TRP LYS LYS ASP ARG ALA THR GLY ASP ALA ASP
SEQRES  16 A 1733  GLU PRO GLU LEU ARG VAL LEU SER THR GLU GLU ILE LEU
SEQRES  17 A 1733  ASN ILE PHE LYS HIS ILE SER VAL LYS ASP PHE THR SER
SEQRES  18 A 1733  LEU GLY PHE ASN GLU VAL PHE SER ARG PRO GLU TRP MET
SEQRES  19 A 1733  ILE LEU THR CYS LEU PRO VAL PRO PRO PRO PRO VAL ARG
SEQRES  20 A 1733  PRO SER ILE SER PHE ASN GLU SER GLN ARG GLY GLU ASP
SEQRES  21 A 1733  ASP LEU THR PHE LYS LEU ALA ASP ILE LEU LYS ALA ASN
SEQRES  22 A 1733  ILE SER LEU GLU THR LEU GLU HIS ASN GLY ALA PRO HIS
SEQRES  23 A 1733  HIS ALA ILE GLU GLU ALA GLU SER LEU LEU GLN PHE HIS
SEQRES  24 A 1733  VAL ALA THR TYR MET ASP ASN ASP ILE ALA GLY GLN PRO
SEQRES  25 A 1733  GLN ALA LEU GLN LYS SER GLY ARG PRO VAL LYS SER ILE
SEQRES  26 A 1733  ARG ALA ARG LEU LYS GLY LYS GLU GLY ARG ILE ARG GLY
SEQRES  27 A 1733  ASN LEU MET GLY LYS ARG VAL ASP PHE SER ALA ARG THR
SEQRES  28 A 1733  VAL ILE SER GLY ASP PRO ASN LEU GLU LEU ASP GLN VAL
SEQRES  29 A 1733  GLY VAL PRO LYS SER ILE ALA LYS THR LEU THR TYR PRO
SEQRES  30 A 1733  GLU VAL VAL THR PRO TYR ASN ILE ASP ARG LEU THR GLN
SEQRES  31 A 1733  LEU VAL ARG ASN GLY PRO ASN GLU HIS PRO GLY ALA LYS
SEQRES  32 A 1733  TYR VAL ILE ARG ASP SER GLY ASP ARG ILE ASP LEU ARG
SEQRES  33 A 1733  TYR SER LYS ARG ALA GLY ASP ILE GLN LEU GLN TYR GLY
SEQRES  34 A 1733  TRP LYS VAL GLU ARG HIS ILE MET ASP ASN ASP PRO VAL
SEQRES  35 A 1733  LEU PHE ASN ARG GLN PRO SER LEU HIS LYS MET SER MET
SEQRES  36 A 1733  MET ALA HIS ARG VAL LYS VAL ILE PRO TYR SER THR PHE
SEQRES  37 A 1733  ARG LEU ASN LEU SER VAL THR SER PRO TYR ASN ALA ASP
SEQRES  38 A 1733  PHE ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN SER
SEQRES  39 A 1733  GLU GLU THR ARG ALA GLU LEU SER GLN LEU CYS ALA VAL
SEQRES  40 A 1733  PRO LEU GLN ILE VAL SER PRO GLN SER ASN LYS PRO CYS
SEQRES  41 A 1733  MET GLY ILE VAL GLN ASP THR LEU CYS GLY ILE ARG LYS
SEQRES  42 A 1733  LEU THR LEU ARG ASP THR PHE ILE GLU LEU ASP GLN VAL
SEQRES  43 A 1733  LEU ASN MET LEU TYR TRP VAL PRO ASP TRP ASP GLY VAL
SEQRES  44 A 1733  ILE PRO THR PRO ALA ILE ILE LYS PRO LYS PRO LEU TRP
SEQRES  45 A 1733  SER GLY LYS GLN ILE LEU SER VAL ALA ILE PRO ASN GLY
SEQRES  46 A 1733  ILE HIS LEU GLN ARG PHE ASP GLU GLY THR THR LEU LEU
SEQRES  47 A 1733  SER PRO LYS ASP ASN GLY MET LEU ILE ILE ASP GLY GLN
SEQRES  48 A 1733  ILE ILE PHE GLY VAL VAL GLU LYS LYS THR VAL GLY SER
SEQRES  49 A 1733  SER ASN GLY GLY LEU ILE HIS VAL VAL THR ARG GLU LYS
SEQRES  50 A 1733  GLY PRO GLN VAL CYS ALA LYS LEU PHE GLY ASN ILE GLN
SEQRES  51 A 1733  LYS VAL VAL ASN PHE TRP LEU LEU HIS ASN GLY PHE SER
SEQRES  52 A 1733  THR GLY ILE GLY ASP THR ILE ALA ASP GLY PRO THR MET
SEQRES  53 A 1733  ARG GLU ILE THR GLU THR ILE ALA GLU ALA LYS LYS LYS
SEQRES  54 A 1733  VAL LEU ASP VAL THR LYS GLU ALA GLN ALA ASN LEU LEU
SEQRES  55 A 1733  THR ALA LYS HIS GLY MET THR LEU ARG GLU SER PHE GLU
SEQRES  56 A 1733  ASP ASN VAL VAL ARG PHE LEU ASN GLU ALA ARG ASP LYS
SEQRES  57 A 1733  ALA GLY ARG LEU ALA GLU VAL ASN LEU LYS ASP LEU ASN
SEQRES  58 A 1733  ASN VAL LYS GLN MET VAL MET ALA GLY SER LYS GLY SER
SEQRES  59 A 1733  PHE ILE ASN ILE ALA GLN MET SER ALA CYS VAL GLY GLN
SEQRES  60 A 1733  GLN SER VAL GLU GLY LYS ARG ILE ALA PHE GLY PHE VAL
SEQRES  61 A 1733  ASP ARG THR LEU PRO HIS PHE SER LYS ASP ASP TYR SER
SEQRES  62 A 1733  PRO GLU SER LYS GLY PHE VAL GLU ASN SER TYR LEU ARG
SEQRES  63 A 1733  GLY LEU THR PRO GLN GLU PHE PHE PHE HIS ALA MET GLY
SEQRES  64 A 1733  GLY ARG GLU GLY LEU ILE ASP THR ALA VAL LYS THR ALA
SEQRES  65 A 1733  GLU THR GLY TYR ILE GLN ARG ARG LEU VAL LYS ALA LEU
SEQRES  66 A 1733  GLU ASP ILE MET VAL HIS TYR ASP ASN THR THR ARG ASN
SEQRES  67 A 1733  SER LEU GLY ASN VAL ILE GLN PHE ILE TYR GLY GLU ASP
SEQRES  68 A 1733  GLY MET ASP ALA ALA HIS ILE GLU LYS GLN SER LEU ASP
SEQRES  69 A 1733  THR ILE GLY GLY SER ASP ALA ALA PHE GLU LYS ARG TYR
SEQRES  70 A 1733  ARG VAL ASP LEU LEU ASN THR ASP HIS THR LEU ASP PRO
SEQRES  71 A 1733  SER LEU LEU GLU SER GLY SER GLU ILE LEU GLY ASP LEU
SEQRES  72 A 1733  LYS LEU GLN VAL LEU LEU ASP GLU GLU TYR LYS GLN LEU
SEQRES  73 A 1733  VAL LYS ASP ARG LYS PHE LEU ARG GLU VAL PHE VAL ASP
SEQRES  74 A 1733  GLY GLU ALA ASN TRP PRO LEU PRO VAL ASN ILE ARG ARG
SEQRES  75 A 1733  ILE ILE GLN ASN ALA GLN GLN THR PHE HIS ILE ASP HIS
SEQRES  76 A 1733  THR LYS PRO SER ASP LEU THR ILE LYS ASP ILE VAL LEU
SEQRES  77 A 1733  GLY VAL LYS ASP LEU GLN GLU ASN LEU LEU VAL LEU ARG
SEQRES  78 A 1733  GLY LYS ASN GLU ILE ILE GLN ASN ALA GLN ARG ASP ALA
SEQRES  79 A 1733  VAL THR LEU PHE CYS CYS LEU LEU ARG SER ARG LEU ALA
SEQRES  80 A 1733  THR ARG ARG VAL LEU GLN GLU TYR ARG LEU THR LYS GLN
SEQRES  81 A 1733  ALA PHE ASP TRP VAL LEU SER ASN ILE GLU ALA GLN PHE
SEQRES  82 A 1733  LEU ARG SER VAL VAL HIS PRO GLY GLU MET VAL GLY VAL
SEQRES  83 A 1733  LEU ALA ALA GLN SER ILE GLY GLU PRO ALA THR GLN MET
SEQRES  84 A 1733  THR LEU ASN THR PHE HIS PHE ALA GLY VAL ALA SER LYS
SEQRES  85 A 1733  LYS VAL THR SER GLY VAL PRO ARG LEU LYS GLU ILE LEU
SEQRES  86 A 1733  ASN VAL ALA LYS ASN MET LYS THR PRO SER LEU THR VAL
SEQRES  87 A 1733  TYR LEU GLU PRO GLY HIS ALA ALA ASP GLN GLU GLN ALA
SEQRES  88 A 1733  LYS LEU ILE ARG SER ALA ILE GLU HIS THR THR LEU LYS
SEQRES  89 A 1733  SER VAL THR ILE ALA SER GLU ILE TYR TYR ASP PRO ASP
SEQRES  90 A 1733  PRO ARG SER THR VAL ILE PRO GLU ASP GLU GLU ILE ILE
SEQRES  91 A 1733  GLN LEU HIS PHE SER LEU LEU ASP GLU GLU ALA GLU GLN
SEQRES  92 A 1733  SER PHE ASP GLN GLN SER PRO TRP LEU LEU ARG LEU GLU
SEQRES  93 A 1733  LEU ASP ARG ALA ALA MET ASN ASP LYS ASP LEU THR MET
SEQRES  94 A 1733  GLY GLN VAL GLY GLU ARG ILE LYS GLN THR PHE LYS ASN
SEQRES  95 A 1733  ASP LEU PHE VAL ILE TRP SER GLU ASP ASN ASP GLU LYS
SEQRES  96 A 1733  LEU ILE ILE ARG CYS ARG VAL VAL ARG PRO LYS SER LEU
SEQRES  97 A 1733  ASP ALA GLU THR GLU ALA GLU GLU ASP HIS MET LEU LYS
SEQRES  98 A 1733  LYS ILE GLU ASN THR MET LEU GLU ASN ILE THR LEU ARG
SEQRES  99 A 1733  GLY VAL GLU ASN ILE GLU ARG VAL VAL MET MET LYS TYR
SEQRES 100 A 1733  ASP ARG LYS VAL PRO SER PRO THR GLY GLU TYR VAL LYS
SEQRES 101 A 1733  GLU PRO GLU TRP VAL LEU GLU THR ASP GLY VAL ASN LEU
SEQRES 102 A 1733  SER GLU VAL MET THR VAL PRO GLY ILE ASP PRO THR ARG
SEQRES 103 A 1733  ILE TYR THR ASN SER PHE ILE ASP ILE MET GLU VAL LEU
SEQRES 104 A 1733  GLY ILE GLU ALA GLY ARG ALA ALA LEU TYR LYS GLU VAL
SEQRES 105 A 1733  TYR ASN VAL ILE ALA SER ASP GLY SER TYR VAL ASN TYR
SEQRES 106 A 1733  ARG HIS MET ALA LEU LEU VAL ASP VAL MET THR THR GLN
SEQRES 107 A 1733  GLY GLY LEU THR SER VAL THR ARG HIS GLY PHE ASN ARG
SEQRES 108 A 1733  SER ASN THR GLY ALA LEU MET ARG CYS SER PHE GLU GLU
SEQRES 109 A 1733  THR VAL GLU ILE LEU PHE GLU ALA GLY ALA SER ALA GLU
SEQRES 110 A 1733  LEU ASP ASP CYS ARG GLY VAL SER GLU ASN VAL ILE LEU
SEQRES 111 A 1733  GLY GLN MET ALA PRO ILE GLY THR GLY ALA PHE ASP VAL
SEQRES 112 A 1733  MET ILE ASP GLU GLU SER LEU VAL LYS TYR MET PRO GLU
SEQRES 113 A 1733  GLN LYS ILE THR GLU ILE GLU ASP GLY GLN ASP GLY GLY
SEQRES 114 A 1733  VAL THR PRO TYR SER ASN GLU SER GLY LEU VAL ASN ALA
SEQRES 115 A 1733  ASP LEU ASP VAL LYS ASP GLU LEU MET PHE SER PRO LEU
SEQRES 116 A 1733  VAL ASP SER GLY SER ASN ASP ALA MET ALA GLY GLY PHE
SEQRES 117 A 1733  THR ALA TYR GLY GLY ALA ASP TYR GLY GLU ALA THR SER
SEQRES 118 A 1733  PRO PHE GLY ALA TYR GLY GLU ALA PRO THR SER PRO GLY
SEQRES 119 A 1733  PHE GLY VAL SER SER PRO GLY PHE SER PRO THR SER PRO
SEQRES 120 A 1733  THR TYR SER PRO THR SER PRO ALA TYR SER PRO THR SER
SEQRES 121 A 1733  PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO THR
SEQRES 122 A 1733  SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 123 A 1733  THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 124 A 1733  PRO THR SER PRO SER TYR SER PRO THR SER PRO SER TYR
SEQRES 125 A 1733  SER PRO THR SER PRO SER TYR SER PRO THR SER PRO SER
SEQRES 126 A 1733  TYR SER PRO THR SER PRO SER TYR SER PRO THR SER PRO
SEQRES 127 A 1733  SER TYR SER PRO THR SER PRO SER TYR SER PRO THR SER
SEQRES 128 A 1733  PRO SER TYR SER PRO THR SER PRO ALA TYR SER PRO THR
SEQRES 129 A 1733  SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 130 A 1733  THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 131 A 1733  PRO THR SER PRO ASN TYR SER PRO THR SER PRO SER TYR
SEQRES 132 A 1733  SER PRO THR SER PRO GLY TYR SER PRO GLY SER PRO ALA
SEQRES 133 A 1733  TYR SER PRO LYS GLN ASP GLU GLN LYS HIS ASN GLU ASN
SEQRES 134 A 1733  GLU ASN SER ARG
SEQRES   1 B 1224  MET SER ASP LEU ALA ASN SER GLU LYS TYR TYR ASP GLU
SEQRES   2 B 1224  ASP PRO TYR GLY PHE GLU ASP GLU SER ALA PRO ILE THR
SEQRES   3 B 1224  ALA GLU ASP SER TRP ALA VAL ILE SER ALA PHE PHE ARG
SEQRES   4 B 1224  GLU LYS GLY LEU VAL SER GLN GLN LEU ASP SER PHE ASN
SEQRES   5 B 1224  GLN PHE VAL ASP TYR THR LEU GLN ASP ILE ILE CYS GLU
SEQRES   6 B 1224  ASP SER THR LEU ILE LEU GLU GLN LEU ALA GLN HIS THR
SEQRES   7 B 1224  THR GLU SER ASP ASN ILE SER ARG LYS TYR GLU ILE SER
SEQRES   8 B 1224  PHE GLY LYS ILE TYR VAL THR LYS PRO MET VAL ASN GLU
SEQRES   9 B 1224  SER ASP GLY VAL THR HIS ALA LEU TYR PRO GLN GLU ALA
SEQRES  10 B 1224  ARG LEU ARG ASN LEU THR TYR SER SER GLY LEU PHE VAL
SEQRES  11 B 1224  ASP VAL LYS LYS ARG THR TYR GLU ALA ILE ASP VAL PRO
SEQRES  12 B 1224  GLY ARG GLU LEU LYS TYR GLU LEU ILE ALA GLU GLU SER
SEQRES  13 B 1224  GLU ASP ASP SER GLU SER GLY LYS VAL PHE ILE GLY ARG
SEQRES  14 B 1224  LEU PRO ILE MET LEU ARG SER LYS ASN CYS TYR LEU SER
SEQRES  15 B 1224  GLU ALA THR GLU SER ASP LEU TYR LYS LEU LYS GLU CYS
SEQRES  16 B 1224  PRO PHE ASP MET GLY GLY TYR PHE ILE ILE ASN GLY SER
SEQRES  17 B 1224  GLU LYS VAL LEU ILE ALA GLN GLU ARG SER ALA GLY ASN
SEQRES  18 B 1224  ILE VAL GLN VAL PHE LYS LYS ALA ALA PRO SER PRO ILE
SEQRES  19 B 1224  SER HIS VAL ALA GLU ILE ARG SER ALA LEU GLU LYS GLY
SEQRES  20 B 1224  SER ARG PHE ILE SER THR LEU GLN VAL LYS LEU TYR GLY
SEQRES  21 B 1224  ARG GLU GLY SER SER ALA ARG THR ILE LYS ALA THR LEU
SEQRES  22 B 1224  PRO TYR ILE LYS GLN ASP ILE PRO ILE VAL ILE ILE PHE
SEQRES  23 B 1224  ARG ALA LEU GLY ILE ILE PRO ASP GLY GLU ILE LEU GLU
SEQRES  24 B 1224  HIS ILE CYS TYR ASP VAL ASN ASP TRP GLN MET LEU GLU
SEQRES  25 B 1224  MET LEU LYS PRO CYS VAL GLU ASP GLY PHE VAL ILE GLN
SEQRES  26 B 1224  ASP ARG GLU THR ALA LEU ASP PHE ILE GLY ARG ARG GLY
SEQRES  27 B 1224  THR ALA LEU GLY ILE LYS LYS GLU LYS ARG ILE GLN TYR
SEQRES  28 B 1224  ALA LYS ASP ILE LEU GLN LYS GLU PHE LEU PRO HIS ILE
SEQRES  29 B 1224  THR GLN LEU GLU GLY PHE GLU SER ARG LYS ALA PHE PHE
SEQRES  30 B 1224  LEU GLY TYR MET ILE ASN ARG LEU LEU LEU CYS ALA LEU
SEQRES  31 B 1224  ASP ARG LYS ASP GLN ASP ASP ARG ASP HIS PHE GLY LYS
SEQRES  32 B 1224  LYS ARG LEU ASP LEU ALA GLY PRO LEU LEU ALA GLN LEU
SEQRES  33 B 1224  PHE LYS THR LEU PHE LYS LYS LEU THR LYS ASP ILE PHE
SEQRES  34 B 1224  ARG TYR MET GLN ARG THR VAL GLU GLU ALA HIS ASP PHE
SEQRES  35 B 1224  ASN MET LYS LEU ALA ILE ASN ALA LYS THR ILE THR SER
SEQRES  36 B 1224  GLY LEU LYS TYR ALA LEU ALA THR GLY ASN TRP GLY GLU
SEQRES  37 B 1224  GLN LYS LYS ALA MET SER SER ARG ALA GLY VAL SER GLN
SEQRES  38 B 1224  VAL LEU ASN ARG TYR THR TYR SER SER THR LEU SER HIS
SEQRES  39 B 1224  LEU ARG ARG THR ASN THR PRO ILE GLY ARG ASP GLY LYS
SEQRES  40 B 1224  LEU ALA LYS PRO ARG GLN LEU HIS ASN THR HIS TRP GLY
SEQRES  41 B 1224  LEU VAL CYS PRO ALA GLU THR PRO GLU GLY GLN ALA CYS
SEQRES  42 B 1224  GLY LEU VAL LYS ASN LEU SER LEU MET SER CYS ILE SER
SEQRES  43 B 1224  VAL GLY THR ASP PRO MET PRO ILE ILE THR PHE LEU SER
SEQRES  44 B 1224  GLU TRP GLY MET GLU PRO LEU GLU ASP TYR VAL PRO HIS
SEQRES  45 B 1224  GLN SER PRO ASP ALA THR ARG VAL PHE VAL ASN GLY VAL
SEQRES  46 B 1224  TRP HIS GLY VAL HIS ARG ASN PRO ALA ARG LEU MET GLU
SEQRES  47 B 1224  THR LEU ARG THR LEU ARG ARG LYS GLY ASP ILE ASN PRO
SEQRES  48 B 1224  GLU VAL SER MET ILE ARG ASP ILE ARG GLU LYS GLU LEU
SEQRES  49 B 1224  LYS ILE PHE THR ASP ALA GLY ARG VAL TYR ARG PRO LEU
SEQRES  50 B 1224  PHE ILE VAL GLU ASP ASP GLU SER LEU GLY HIS LYS GLU
SEQRES  51 B 1224  LEU LYS VAL ARG LYS GLY HIS ILE ALA LYS LEU MET ALA
SEQRES  52 B 1224  THR GLU TYR GLN ASP ILE GLU GLY GLY PHE GLU ASP VAL
SEQRES  53 B 1224  GLU GLU TYR THR TRP SER SER LEU LEU ASN GLU GLY LEU
SEQRES  54 B 1224  VAL GLU TYR ILE ASP ALA GLU GLU GLU GLU SER ILE LEU
SEQRES  55 B 1224  ILE ALA MET GLN PRO GLU ASP LEU GLU PRO ALA GLU ALA
SEQRES  56 B 1224  ASN GLU GLU ASN ASP LEU ASP VAL ASP PRO ALA LYS ARG
SEQRES  57 B 1224  ILE ARG VAL SER HIS HIS ALA THR THR PHE THR HIS CYS
SEQRES  58 B 1224  GLU ILE HIS PRO SER MET ILE LEU GLY VAL ALA ALA SER
SEQRES  59 B 1224  ILE ILE PRO PHE PRO ASP HIS ASN GLN SER PRO ARG ASN
SEQRES  60 B 1224  THR TYR GLN SER ALA MET GLY LYS GLN ALA MET GLY VAL
SEQRES  61 B 1224  PHE LEU THR ASN TYR ASN VAL ARG MET ASP THR MET ALA
SEQRES  62 B 1224  ASN ILE LEU TYR TYR PRO GLN LYS PRO LEU GLY THR THR
SEQRES  63 B 1224  ARG ALA MET GLU TYR LEU LYS PHE ARG GLU LEU PRO ALA
SEQRES  64 B 1224  GLY GLN ASN ALA ILE VAL ALA ILE ALA CYS TYR SER GLY
SEQRES  65 B 1224  TYR ASN GLN GLU ASP SER MET ILE MET ASN GLN SER SER
SEQRES  66 B 1224  ILE ASP ARG GLY LEU PHE ARG SER LEU PHE PHE ARG SER
SEQRES  67 B 1224  TYR MET ASP GLN GLU LYS LYS TYR GLY MET SER ILE THR
SEQRES  68 B 1224  GLU THR PHE GLU LYS PRO GLN ARG THR ASN THR LEU ARG
SEQRES  69 B 1224  MET LYS HIS GLY THR TYR ASP LYS LEU ASP ASP ASP GLY
SEQRES  70 B 1224  LEU ILE ALA PRO GLY VAL ARG VAL SER GLY GLU ASP VAL
SEQRES  71 B 1224  ILE ILE GLY LYS THR THR PRO ILE SER PRO ASP GLU GLU
SEQRES  72 B 1224  GLU LEU GLY GLN ARG THR ALA TYR HIS SER LYS ARG ASP
SEQRES  73 B 1224  ALA SER THR PRO LEU ARG SER THR GLU ASN GLY ILE VAL
SEQRES  74 B 1224  ASP GLN VAL LEU VAL THR THR ASN GLN ASP GLY LEU LYS
SEQRES  75 B 1224  PHE VAL LYS VAL ARG VAL ARG THR THR LYS ILE PRO GLN
SEQRES  76 B 1224  ILE GLY ASP LYS PHE ALA SER ARG HIS GLY GLN LYS GLY
SEQRES  77 B 1224  THR ILE GLY ILE THR TYR ARG ARG GLU ASP MET PRO PHE
SEQRES  78 B 1224  THR ALA GLU GLY ILE VAL PRO ASP LEU ILE ILE ASN PRO
SEQRES  79 B 1224  HIS ALA ILE PRO SER ARG MET THR VAL ALA HIS LEU ILE
SEQRES  80 B 1224  GLU CYS LEU LEU SER LYS VAL ALA ALA LEU SER GLY ASN
SEQRES  81 B 1224  GLU GLY ASP ALA SER PRO PHE THR ASP ILE THR VAL GLU
SEQRES  82 B 1224  GLY ILE SER LYS LEU LEU ARG GLU HIS GLY TYR GLN SER
SEQRES  83 B 1224  ARG GLY PHE GLU VAL MET TYR ASN GLY HIS THR GLY LYS
SEQRES  84 B 1224  LYS LEU MET ALA GLN ILE PHE PHE GLY PRO THR TYR TYR
SEQRES  85 B 1224  GLN ARG LEU ARG HIS MET VAL ASP ASP LYS ILE HIS ALA
SEQRES  86 B 1224  ARG ALA ARG GLY PRO MET GLN VAL LEU THR ARG GLN PRO
SEQRES  87 B 1224  VAL GLU GLY ARG SER ARG ASP GLY GLY LEU ARG PHE GLY
SEQRES  88 B 1224  GLU MET GLU ARG ASP CYS MET ILE ALA HIS GLY ALA ALA
SEQRES  89 B 1224  SER PHE LEU LYS GLU ARG LEU MET GLU ALA SER ASP ALA
SEQRES  90 B 1224  PHE ARG VAL HIS ILE CYS GLY ILE CYS GLY LEU MET THR
SEQRES  91 B 1224  VAL ILE ALA LYS LEU ASN HIS ASN GLN PHE GLU CYS LYS
SEQRES  92 B 1224  GLY CYS ASP ASN LYS ILE ASP ILE TYR GLN ILE HIS ILE
SEQRES  93 B 1224  PRO TYR ALA ALA LYS LEU LEU PHE GLN GLU LEU MET ALA
SEQRES  94 B 1224  MET ASN ILE THR PRO ARG LEU TYR THR ASP ARG SER ARG
SEQRES  95 B 1224  ASP PHE
SEQRES   1 C  324  HIS HIS HIS HIS HIS HIS MET SER GLU GLU GLY PRO GLN
SEQRES   2 C  324  VAL LYS ILE ARG GLU ALA SER LYS ASP ASN VAL ASP PHE
SEQRES   3 C  324  ILE LEU SER ASN VAL ASP LEU ALA MET ALA ASN SER LEU
SEQRES   4 C  324  ARG ARG VAL MET ILE ALA GLU ILE PRO THR LEU ALA ILE
SEQRES   5 C  324  ASP SER VAL GLU VAL GLU THR ASN THR THR VAL LEU ALA
SEQRES   6 C  324  ASP GLU PHE ILE ALA HIS ARG LEU GLY LEU ILE PRO LEU
SEQRES   7 C  324  GLN SER MET ASP ILE GLU GLN LEU GLU TYR SER ARG ASP
SEQRES   8 C  324  CYS PHE CYS GLU ASP HIS CYS ASP LYS CYS SER VAL VAL
SEQRES   9 C  324  LEU THR LEU GLN ALA PHE GLY GLU SER GLU SER THR THR
SEQRES  10 C  324  ASN VAL TYR SER LYS ASP LEU VAL ILE VAL SER ASN LEU
SEQRES  11 C  324  MET GLY ARG ASN ILE GLY HIS PRO ILE ILE GLN ASP LYS
SEQRES  12 C  324  GLU GLY ASN GLY VAL LEU ILE CYS LYS LEU ARG LYS GLY
SEQRES  13 C  324  GLN GLU LEU LYS LEU THR CYS VAL ALA LYS LYS GLY ILE
SEQRES  14 C  324  ALA LYS GLU HIS ALA LYS TRP GLY PRO ALA ALA ALA ILE
SEQRES  15 C  324  GLU PHE GLU TYR ASP PRO TRP ASN LYS LEU LYS HIS THR
SEQRES  16 C  324  ASP TYR TRP TYR GLU GLN ASP SER ALA LYS GLU TRP PRO
SEQRES  17 C  324  GLN SER LYS ASN CYS GLU TYR GLU ASP PRO PRO ASN GLU
SEQRES  18 C  324  GLY ASP PRO PHE ASP TYR LYS ALA GLN ALA ASP THR PHE
SEQRES  19 C  324  TYR MET ASN VAL GLU SER VAL GLY SER ILE PRO VAL ASP
SEQRES  20 C  324  GLN VAL VAL VAL ARG GLY ILE ASP THR LEU GLN LYS LYS
SEQRES  21 C  324  VAL ALA SER ILE LEU LEU ALA LEU THR GLN MET ASP GLN
SEQRES  22 C  324  ASP LYS VAL ASN PHE ALA SER GLY ASP ASN ASN THR ALA
SEQRES  23 C  324  SER ASN MET LEU GLY SER ASN GLU ASP VAL MET MET THR
SEQRES  24 C  324  GLY ALA GLU GLN ASP PRO TYR SER ASN ALA SER GLN MET
SEQRES  25 C  324  GLY ASN THR GLY SER GLY GLY TYR ASP ASN ALA TRP
SEQRES   1 D  221  MET ASN VAL SER THR SER THR PHE GLN THR ARG ARG ARG
SEQRES   2 D  221  ARG LEU LYS LYS VAL GLU GLU GLU GLU ASN ALA ALA THR
SEQRES   3 D  221  LEU GLN LEU GLY GLN GLU PHE GLN LEU LYS GLN ILE ASN
SEQRES   4 D  221  HIS GLN GLY GLU GLU GLU GLU LEU ILE ALA LEU ASN LEU
SEQRES   5 D  221  SER GLU ALA ARG LEU VAL ILE LYS GLU ALA LEU VAL GLU
SEQRES   6 D  221  ARG ARG ARG ALA PHE LYS ARG SER GLN LYS LYS HIS LYS
SEQRES   7 D  221  LYS LYS HIS LEU LYS HIS GLU ASN ALA ASN ASP GLU THR
SEQRES   8 D  221  THR ALA VAL GLU ASP GLU ASP ASP ASP LEU ASP GLU ASP
SEQRES   9 D  221  ASP VAL ASN ALA ASP ASP ASP ASP PHE MET HIS SER GLU
SEQRES  10 D  221  THR ARG GLU LYS GLU LEU GLU SER ILE ASP VAL LEU LEU
SEQRES  11 D  221  GLU GLN THR THR GLY GLY ASN ASN LYS ASP LEU LYS ASN
SEQRES  12 D  221  THR MET GLN TYR LEU THR ASN PHE SER ARG PHE ARG ASP
SEQRES  13 D  221  GLN GLU THR VAL GLY ALA VAL ILE GLN LEU LEU LYS SER
SEQRES  14 D  221  THR GLY LEU HIS PRO PHE GLU VAL ALA GLN LEU GLY SER
SEQRES  15 D  221  LEU ALA CYS ASP THR ALA ASP GLU ALA LYS THR LEU ILE
SEQRES  16 D  221  PRO SER LEU ASN ASN LYS ILE SER ASP ASP GLU LEU GLU
SEQRES  17 D  221  ARG ILE LEU LYS GLU LEU SER ASN LEU GLU THR LEU TYR
SEQRES   1 E  215  MET ASP GLN GLU ASN GLU ARG ASN ILE SER ARG LEU TRP
SEQRES   2 E  215  ARG ALA PHE ARG THR VAL LYS GLU MET VAL LYS ASP ARG
SEQRES   3 E  215  GLY TYR PHE ILE THR GLN GLU GLU VAL GLU LEU PRO LEU
SEQRES   4 E  215  GLU ASP PHE LYS ALA LYS TYR CYS ASP SER MET GLY ARG
SEQRES   5 E  215  PRO GLN ARG LYS MET MET SER PHE GLN ALA ASN PRO THR
SEQRES   6 E  215  GLU GLU SER ILE SER LYS PHE PRO ASP MET GLY SER LEU
SEQRES   7 E  215  TRP VAL GLU PHE CYS ASP GLU PRO SER VAL GLY VAL LYS
SEQRES   8 E  215  THR MET LYS THR PHE VAL ILE HIS ILE GLN GLU LYS ASN
SEQRES   9 E  215  PHE GLN THR GLY ILE PHE VAL TYR GLN ASN ASN ILE THR
SEQRES  10 E  215  PRO SER ALA MET LYS LEU VAL PRO SER ILE PRO PRO ALA
SEQRES  11 E  215  THR ILE GLU THR PHE ASN GLU ALA ALA LEU VAL VAL ASN
SEQRES  12 E  215  ILE THR HIS HIS GLU LEU VAL PRO LYS HIS ILE ARG LEU
SEQRES  13 E  215  SER SER ASP GLU LYS ARG GLU LEU LEU LYS ARG TYR ARG
SEQRES  14 E  215  LEU LYS GLU SER GLN LEU PRO ARG ILE GLN ARG ALA ASP
SEQRES  15 E  215  PRO VAL ALA LEU TYR LEU GLY LEU LYS ARG GLY GLU VAL
SEQRES  16 E  215  VAL LYS ILE ILE ARG LYS SER GLU THR SER GLY ARG TYR
SEQRES  17 E  215  ALA SER TYR ARG ILE CYS MET
SEQRES   1 F  155  MET SER ASP TYR GLU GLU ALA PHE ASN ASP GLY ASN GLU
SEQRES   2 F  155  ASN PHE GLU ASP PHE ASP VAL GLU HIS PHE SER ASP GLU
SEQRES   3 F  155  GLU THR TYR GLU GLU LYS PRO GLN PHE LYS ASP GLY GLU
SEQRES   4 F  155  THR THR ASP ALA ASN GLY LYS THR ILE VAL THR GLY GLY
SEQRES   5 F  155  ASN GLY PRO GLU ASP PHE GLN GLN HIS GLU GLN ILE ARG
SEQRES   6 F  155  ARG LYS THR LEU LYS GLU LYS ALA ILE PRO LYS ASP GLN
SEQRES   7 F  155  ARG ALA THR THR PRO TYR MET THR LYS TYR GLU ARG ALA
SEQRES   8 F  155  ARG ILE LEU GLY THR ARG ALA LEU GLN ILE SER MET ASN
SEQRES   9 F  155  ALA PRO VAL PHE VAL ASP LEU GLU GLY GLU THR ASP PRO
SEQRES  10 F  155  LEU ARG ILE ALA MET LYS GLU LEU ALA GLU LYS LYS ILE
SEQRES  11 F  155  PRO LEU VAL ILE ARG ARG TYR LEU PRO ASP GLY SER PHE
SEQRES  12 F  155  GLU ASP TRP SER VAL GLU GLU LEU ILE VAL ASP LEU
SEQRES   1 G  171  MET PHE PHE ILE LYS ASP LEU SER LEU ASN ILE THR LEU
SEQRES   2 G  171  HIS PRO SER PHE PHE GLY PRO ARG MET LYS GLN TYR LEU
SEQRES   3 G  171  LYS THR LYS LEU LEU GLU GLU VAL GLU GLY SER CYS THR
SEQRES   4 G  171  GLY LYS PHE GLY TYR ILE LEU CYS VAL LEU ASP TYR ASP
SEQRES   5 G  171  ASN ILE ASP ILE GLN ARG GLY ARG ILE LEU PRO THR ASP
SEQRES   6 G  171  GLY SER ALA GLU PHE ASN VAL LYS TYR ARG ALA VAL VAL
SEQRES   7 G  171  PHE LYS PRO PHE LYS GLY GLU VAL VAL ASP GLY THR VAL
SEQRES   8 G  171  VAL SER CYS SER GLN HIS GLY PHE GLU VAL GLN VAL GLY
SEQRES   9 G  171  PRO MET LYS VAL PHE VAL THR LYS HIS LEU MET PRO GLN
SEQRES  10 G  171  ASP LEU THR PHE ASN ALA GLY SER ASN PRO PRO SER TYR
SEQRES  11 G  171  GLN SER SER GLU ASP VAL ILE THR ILE LYS SER ARG ILE
SEQRES  12 G  171  ARG VAL LYS ILE GLU GLY CYS ILE SER GLN VAL SER SER
SEQRES  13 G  171  ILE HIS ALA ILE GLY SER ILE LYS GLU ASP TYR LEU GLY
SEQRES  14 G  171  ALA ILE
SEQRES   1 H  146  MET SER ASN THR LEU PHE ASP ASP ILE PHE GLN VAL SER
SEQRES   2 H  146  GLU VAL ASP PRO GLY ARG TYR ASN LYS VAL CYS ARG ILE
SEQRES   3 H  146  GLU ALA ALA SER THR THR GLN ASP GLN CYS LYS LEU THR
SEQRES   4 H  146  LEU ASP ILE ASN VAL GLU LEU PHE PRO VAL ALA ALA GLN
SEQRES   5 H  146  ASP SER LEU THR VAL THR ILE ALA SER SER LEU ASN LEU
SEQRES   6 H  146  GLU ASP THR PRO ALA ASN ASP SER SER ALA THR ARG SER
SEQRES   7 H  146  TRP ARG PRO PRO GLN ALA GLY ASP ARG SER LEU ALA ASP
SEQRES   8 H  146  ASP TYR ASP TYR VAL MET TYR GLY THR ALA TYR LYS PHE
SEQRES   9 H  146  GLU GLU VAL SER LYS ASP LEU ILE ALA VAL TYR TYR SER
SEQRES  10 H  146  PHE GLY GLY LEU LEU MET ARG LEU GLU GLY ASN TYR ARG
SEQRES  11 H  146  ASN LEU ASN ASN LEU LYS GLN GLU ASN ALA TYR LEU LEU
SEQRES  12 H  146  ILE ARG ARG
SEQRES   1 I  122  MET THR THR PHE ARG PHE CYS ARG ASP CYS ASN ASN MET
SEQRES   2 I  122  LEU TYR PRO ARG GLU ASP LYS GLU ASN ASN ARG LEU LEU
SEQRES   3 I  122  PHE GLU CYS ARG THR CYS SER TYR VAL GLU GLU ALA GLY
SEQRES   4 I  122  SER PRO LEU VAL TYR ARG HIS GLU LEU ILE THR ASN ILE
SEQRES   5 I  122  GLY GLU THR ALA GLY VAL VAL GLN ASP ILE GLY SER ASP
SEQRES   6 I  122  PRO THR LEU PRO ARG SER ASP ARG GLU CYS PRO LYS CYS
SEQRES   7 I  122  HIS SER ARG GLU ASN VAL PHE PHE GLN SER GLN GLN ARG
SEQRES   8 I  122  ARG LYS ASP THR SER MET VAL LEU PHE PHE VAL CYS LEU
SEQRES   9 I  122  SER CYS SER HIS ILE PHE THR SER ASP GLN LYS ASN LYS
SEQRES  10 I  122  ARG THR GLN PHE SER
SEQRES   1 J   70  MET ILE VAL PRO VAL ARG CYS PHE SER CYS GLY LYS VAL
SEQRES   2 J   70  VAL GLY ASP LYS TRP GLU SER TYR LEU ASN LEU LEU GLN
SEQRES   3 J   70  GLU ASP GLU LEU ASP GLU GLY THR ALA LEU SER ARG LEU
SEQRES   4 J   70  GLY LEU LYS ARG TYR CYS CYS ARG ARG MET ILE LEU THR
SEQRES   5 J   70  HIS VAL ASP LEU ILE GLU LYS PHE LEU ARG TYR ASN PRO
SEQRES   6 J   70  LEU GLU LYS ARG ASP
SEQRES   1 K  120  MET ASN ALA PRO ASP ARG PHE GLU LEU PHE LEU LEU GLY
SEQRES   2 K  120  GLU GLY GLU SER LYS LEU LYS ILE ASP PRO ASP THR LYS
SEQRES   3 K  120  ALA PRO ASN ALA VAL VAL ILE THR PHE GLU LYS GLU ASP
SEQRES   4 K  120  HIS THR LEU GLY ASN LEU ILE ARG ALA GLU LEU LEU ASN
SEQRES   5 K  120  ASP ARG LYS VAL LEU PHE ALA ALA TYR LYS VAL GLU HIS
SEQRES   6 K  120  PRO PHE PHE ALA ARG PHE LYS LEU ARG ILE GLN THR THR
SEQRES   7 K  120  GLU GLY TYR ASP PRO LYS ASP ALA LEU LYS ASN ALA CYS
SEQRES   8 K  120  ASN SER ILE ILE ASN LYS LEU GLY ALA LEU LYS THR ASN
SEQRES   9 K  120  PHE GLU THR GLU TRP ASN LEU GLN THR LEU ALA ALA ASP
SEQRES  10 K  120  ASP ALA PHE
SEQRES   1 L   70  MET SER ARG GLU GLY PHE GLN ILE PRO THR ASN LEU ASP
SEQRES   2 L   70  ALA ALA ALA ALA GLY THR SER GLN ALA ARG THR ALA THR
SEQRES   3 L   70  LEU LYS TYR ILE CYS ALA GLU CYS SER SER LYS LEU SER
SEQRES   4 L   70  LEU SER ARG THR ASP ALA VAL ARG CYS LYS ASP CYS GLY
SEQRES   5 L   70  HIS ARG ILE LEU LEU LYS ALA ARG THR LYS ARG LEU VAL
SEQRES   6 L   70  GLN PHE GLU ALA ARG
SEQRES   1 T   26   DA  DG  DC  DT  DC  DA  DA  DG  DT  DA  DC  DT  DT
SEQRES   2 T   26   DA 8OG  DG  DC  DC BRU  DG  DG  DT  DC  DA  DT  DT
SEQRES   1 N   12   DA  DG  DT  DA  DC  DT  DT  DG  DA  DG  DC  DT
SEQRES   1 P   16    U   G   C   A   U   C   U   U   C   C   A   G   G
SEQRES   2 P   16    C   C   U
MODRES 3I4M 8OG T   19   DG
MODRES 3I4M BRU T   23   DU
HET    8OG  T  19      23
HET    BRU  T  23      20
HET     MG  A2458       1
HET     ZN  A2456       1
HET     ZN  A2457       1
HET     ZN  B2225       1
HET     ZN  C1269       1
HET     ZN  I1121       1
HET     ZN  I1122       1
HET     ZN  J1066       1
HET     ZN  L1071       1
HETNAM     8OG 8-OXO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE
HETNAM     BRU 5-BROMO-2'-DEOXYURIDINE-5'-MONOPHOSPHATE
HETNAM      MG MAGNESIUM ION
HETNAM      ZN ZINC ION
HETSYN     8OG 8-OXO-7,8-DIHYDRO-2'-DEOXY-GUANOSINE-5'-MONOPHOSPHATE
FORMUL  13  8OG    C10 H14 N5 O8 P
FORMUL  13  BRU    C9 H12 BR N2 O8 P
FORMUL  16   MG    MG 2+
FORMUL  17   ZN    8(ZN 2+)
HELIX    1   1 SER A   23  SER A   31  1                                   9
HELIX    2   2 PHE A   95  GLU A  104  1                                  10
HELIX    3   3 ASN A  119  LEU A  126  1                                   8
HELIX    4   4 LYS A  132  LYS A  143  1                                  12
HELIX    5   5 SER A  203  ILE A  214  1                                  12
HELIX    6   6 SER A  215  GLY A  223  1                                   9
HELIX    7   7 ARG A  230  TRP A  233  5                                   4
HELIX    8   8 PRO A  243  ARG A  247  5                                   5
HELIX    9   9 ASP A  260  ASN A  282  1                                  23
HELIX   10  10 ILE A  289  SER A  294  1                                   6
HELIX   11  11 LEU A  295  TYR A  303  1                                   9
HELIX   12  12 SER A  324  LYS A  330  1                                   7
HELIX   13  13 LYS A  368  LYS A  372  1                                   5
HELIX   14  14 ASN A  384  GLY A  395  1                                  12
HELIX   15  15 HIS A  451  MET A  453  5                                   3
HELIX   16  16 LEU A  472  ASN A  479  5                                   8
HELIX   17  17 SER A  494  CYS A  505  1                                  12
HELIX   18  18 ALA A  506  ILE A  511  1                                   6
HELIX   19  19 VAL A  524  LEU A  536  1                                  13
HELIX   20  20 LEU A  543  VAL A  553  1                                  11
HELIX   21  21 GLY A  574  SER A  579  1                                   6
HELIX   22  22 GLY A  628  GLY A  638  1                                  11
HELIX   23  23 GLY A  638  GLY A  661  1                                  24
HELIX   24  24 GLY A  665  THR A  669  5                                   5
HELIX   25  25 ASP A  672  GLU A  696  1                                  25
HELIX   26  26 THR A  709  VAL A  735  1                                  27
HELIX   27  27 ASN A  741  GLY A  750  1                                  10
HELIX   28  28 SER A  754  ALA A  763  1                                  10
HELIX   29  29 THR A  809  ALA A  828  1                                  20
HELIX   30  30 THR A  831  GLU A  846  1                                  16
HELIX   31  31 ILE A  867  ASP A  871  5                                   5
HELIX   32  32 ASP A  884  GLY A  887  5                                   4
HELIX   33  33 SER A  889  ARG A  898  1                                  10
HELIX   34  34 LYS A  924  PHE A  947  1                                  24
HELIX   35  35 ASN A  959  PHE A  971  1                                  13
HELIX   36  36 LYS A  984  ASN A  996  1                                  13
HELIX   37  37 ASN A 1004  THR A 1016  1                                  13
HELIX   38  38 THR A 1016  LEU A 1026  1                                  11
HELIX   39  39 ALA A 1027  GLU A 1034  1                                   8
HELIX   40  40 THR A 1038  VAL A 1057  1                                  20
HELIX   41  41 MET A 1063  GLU A 1074  1                                  12
HELIX   42  42 SER A 1096  ASN A 1106  1                                  11
HELIX   43  43 ASP A 1127  ALA A 1137  1                                  11
HELIX   44  44 THR A 1142  VAL A 1146  1                                   5
HELIX   45  45 ASP A 1166  ILE A 1170  5                                   5
HELIX   46  46 ALA A 1200  LYS A 1205  1                                   6
HELIX   47  47 THR A 1208  LYS A 1221  1                                  14
HELIX   48  48 LYS A 1261  GLU A 1269  1                                   9
HELIX   49  49 SER A 1331  LEU A 1339  1                                   9
HELIX   50  50 GLY A 1340  SER A 1358  1                                  19
HELIX   51  51 TYR A 1365  THR A 1377  1                                  13
HELIX   52  52 GLY A 1395  SER A 1401  1                                   7
HELIX   53  53 GLU A 1404  SER A 1415  1                                  12
HELIX   54  54 GLY A 1423  GLY A 1431  1                                   9
HELIX   55  55 ILE A 1436  GLY A 1439  5                                   4
HELIX   56  56 GLU A 1448  TYR A 1453  1                                   6
HELIX   57  57 THR B   26  LYS B   41  1                                  16
HELIX   58  58 VAL B   44  TYR B   57  1                                  14
HELIX   59  59 TYR B   57  CYS B   64  1                                   8
HELIX   60  60 TYR B  113  ARG B  120  1                                   8
HELIX   61  61 CYS B  179  ALA B  184  1                                   6
HELIX   62  62 GLU B  186  LYS B  193  1                                   8
HELIX   63  63 ILE B  282  LEU B  289  1                                   8
HELIX   64  64 GLU B  296  CYS B  302  1                                   7
HELIX   65  65 ASP B  307  ASP B  320  1                                  14
HELIX   66  66 ASP B  326  PHE B  333  1                                   8
HELIX   67  67 GLU B  346  GLU B  359  1                                  14
HELIX   68  68 PHE B  370  LEU B  390  1                                  21
HELIX   69  69 HIS B  400  GLY B  402  5                                   3
HELIX   70  70 LEU B  408  LYS B  426  1                                  19
HELIX   71  71 LYS B  426  GLN B  433  1                                   8
HELIX   72  72 ALA B  450  GLY B  464  1                                  15
HELIX   73  73 THR B  487  ARG B  496  1                                  10
HELIX   74  74 PRO B  551  SER B  559  1                                   9
HELIX   75  75 PRO B  565  TYR B  569  5                                   5
HELIX   76  76 ASN B  592  ARG B  605  1                                  14
HELIX   77  77 ILE B  619  LYS B  622  5                                   4
HELIX   78  78 ARG B  654  GLN B  667  1                                  14
HELIX   79  79 THR B  680  GLU B  687  1                                   8
HELIX   80  80 ASP B  694  GLU B  699  1                                   6
HELIX   81  81 HIS B  744  ILE B  748  5                                   5
HELIX   82  82 GLY B  750  ILE B  755  1                                   6
HELIX   83  83 PRO B  765  GLY B  774  1                                  10
HELIX   84  84 ASN B  784  ARG B  788  5                                   5
HELIX   85  85 ALA B  808  LYS B  813  1                                   6
HELIX   86  86 GLN B  843  ARG B  848  1                                   6
HELIX   87  87 ASN B 1013  ILE B 1017  5                                   5
HELIX   88  88 THR B 1022  GLY B 1039  1                                  18
HELIX   89  89 THR B 1051  LEU B 1059  1                                   9
HELIX   90  90 ARG B 1060  GLY B 1063  5                                   4
HELIX   91  91 MET B 1098  LYS B 1102  5                                   5
HELIX   92  92 GLY B 1131  GLY B 1142  1                                  12
HELIX   93  93 ALA B 1143  MET B 1152  1                                  10
HELIX   94  94 PRO B 1197  ALA B 1209  1                                  13
HELIX   95  95 ASP C   26  GLU C   40  1                                  15
HELIX   96  96 ALA C   59  ILE C   70  1                                  12
HELIX   97  97 LYS C  116  LEU C  118  5                                   3
HELIX   98  98 HIS C  167  GLY C  171  5                                   5
HELIX   99  99 ASP C  196  TRP C  201  1                                   6
HELIX  100 100 ASP C  241  ASP C  268  1                                  28
HELIX  101 101 GLY D   30  GLN D   34  5                                   5
HELIX  102 102 SER D   53  SER D   73  1                                  21
HELIX  103 103 ARG D  119  THR D  134  1                                  16
HELIX  104 104 ASN D  138  PHE D  151  1                                  14
HELIX  105 105 ASP D  156  LYS D  168  1                                  13
HELIX  106 106 HIS D  173  LEU D  183  1                                  11
HELIX  107 107 THR D  187  ILE D  195  1                                   9
HELIX  108 108 SER D  203  GLU D  218  1                                  16
HELIX  109 109 GLU E    4  ARG E   26  1                                  23
HELIX  110 110 THR E   31  GLU E   36  1                                   6
HELIX  111 111 LEU E   39  ALA E   44  1                                   6
HELIX  112 112 GLN E   54  MET E   58  5                                   5
HELIX  113 113 THR E   65  SER E   70  5                                   6
HELIX  114 114 THR E   92  LYS E  103  1                                  12
HELIX  115 115 GLU E  137  VAL E  141  1                                   5
HELIX  116 116 SER E  157  ARG E  167  1                                  11
HELIX  117 117 ASP E  182  LEU E  188  1                                   7
HELIX  118 118 THR F   86  SER F  102  1                                  17
HELIX  119 119 ASP F  116  LEU F  125  1                                  10
HELIX  120 120 ARG G   21  GLU G   33  1                                  13
HELIX  121 121 ASP G   50  ILE G   54  5                                   5
HELIX  122 122 VAL I   59  SER I   64  5                                   6
HELIX  123 123 ASP J   16  GLU J   27  1                                  12
HELIX  124 124 ASP J   31  LEU J   39  1                                   9
HELIX  125 125 ARG J   43  HIS J   53  1                                  11
HELIX  126 126 LEU J   56  ARG J   62  1                                   7
HELIX  127 127 ASP K    5  PHE K   10  5                                   6
HELIX  128 128 LEU K   42  LEU K   51  1                                  10
HELIX  129 129 ASP K   82  ASN K  110  1                                  29
SHEET    1   A 3 LEU A  11  ARG A  12  0
SHEET    2   A 3 ILE B1191  ILE B1196  1  O  GLN B1193   N  ARG A  12
SHEET    3   A 3 PHE B1158  CYS B1163 -1  N  PHE B1158   O  ILE B1196
SHEET    1   B 3 LEU A1418  ASP A1419  0
SHEET    2   B 3 GLU A  16  LEU A  21 -1  N  VAL A  17   O  ASP A1419
SHEET    3   B 3 ILE B1212  TYR B1217 -1  O  ARG B1215   N  GLN A  18
SHEET    1   C 2 ASP A  85  PHE A  91  0
SHEET    2   C 2 ILE A 235  CYS A 238 -1  O  THR A 237   N  LEU A  86
SHEET    1   D 2 ASP A 151  VAL A 152  0
SHEET    2   D 2 VAL A 162  SER A 163 -1  O  VAL A 162   N  VAL A 152
SHEET    1   E 3 ARG A 175  ASP A 177  0
SHEET    2   E 3 LYS A 180  SER A 184 -1  O  LYS A 180   N  ASP A 177
SHEET    3   E 3 LEU A 199  LEU A 202 -1  O  LEU A 202   N  LEU A 181
SHEET    1   F 2 LYS A 343  ARG A 344  0
SHEET    2   F 2 ARG B1129  PHE B1130 -1  O  PHE B1130   N  LYS A 343
SHEET    1   G 7 ARG A 469  LEU A 470  0
SHEET    2   G 7 GLN A 363  PRO A 367 -1  N  GLY A 365   O  ARG A 469
SHEET    3   G 7 MET A 455  ILE A 463  1  O  ILE A 463   N  VAL A 366
SHEET    4   G 7 PRO A 441  ASN A 445 -1  N  PHE A 444   O  MET A 456
SHEET    5   G 7 GLU A 486  HIS A 490 -1  O  ASN A 488   N  ASN A 445
SHEET    6   G 7 SER A 348  VAL A 352 -1  N  ALA A 349   O  LEU A 489
SHEET    7   G 7 HIS B1104  ARG B1106 -1  O  HIS B1104   N  ARG A 350
SHEET    1   H 2 THR A 375  TYR A 376  0
SHEET    2   H 2 ARG A 434  HIS A 435 -1  O  ARG A 434   N  TYR A 376
SHEET    1   I 2 TYR A 404  ILE A 406  0
SHEET    2   I 2 ARG A 412  ASP A 414 -1  O  ILE A 413   N  VAL A 405
SHEET    1   J 2 VAL A 512  SER A 513  0
SHEET    2   J 2 LYS A 518  PRO A 519 -1  O  LYS A 518   N  SER A 513
SHEET    1   K 2 PHE A 540  GLU A 542  0
SHEET    2   K 2 LEU A 571  SER A 573 -1  O  TRP A 572   N  ILE A 541
SHEET    1   L 3 LEU A 588  GLN A 589  0
SHEET    2   L 3 LEU A 606  ILE A 608 -1  O  ILE A 607   N  LEU A 588
SHEET    3   L 3 GLN A 611  PHE A 614 -1  O  ILE A 613   N  LEU A 606
SHEET    1   M 2 GLY A 766  GLN A 767  0
SHEET    2   M 2 PHE A 799  VAL A 800 -1  O  VAL A 800   N  GLY A 766
SHEET    1   N 2 SER A 769  VAL A 770  0
SHEET    2   N 2 LYS A 773  ARG A 774 -1  O  LYS A 773   N  VAL A 770
SHEET    1   O 3 MET A 849  VAL A 850  0
SHEET    2   O 3 THR A 856  ARG A 857 -1  O  ARG A 857   N  MET A 849
SHEET    3   O 3 VAL A 863  GLN A 865 -1  O  ILE A 864   N  THR A 856
SHEET    1   P 2 GLU A 879  SER A 882  0
SHEET    2   P 2 ASN A 953  LEU A 956 -1  O  TRP A 954   N  GLN A 881
SHEET    1   Q 3 VAL A1118  TYR A1119  0
SHEET    2   Q 3 GLU A1303  GLU A1307 -1  O  LEU A1306   N  VAL A1118
SHEET    3   Q 3 VAL A1283  TYR A1287 -1  N  MET A1285   O  VAL A1305
SHEET    1   R 3 ARG A1194  LEU A1197  0
SHEET    2   R 3 THR A1147  TYR A1153 -1  N  ILE A1148   O  GLU A1196
SHEET    3   R 3 LEU I  42  ARG I  45 -1  O  TYR I  44   N  ILE A1152
SHEET    1   S 2 PHE A1225  VAL A1226  0
SHEET    2   S 2 CYS A1240  ARG A1241 -1  O  ARG A1241   N  PHE A1225
SHEET    1   T 2 LYS A1290  PRO A1292  0
SHEET    2   T 2 TYR A1298  LYS A1300 -1  O  VAL A1299   N  VAL A1291
SHEET    1   U 6 PHE F 143  SER F 147  0
SHEET    2   U 6 LEU F 132  TYR F 137 -1  N  ILE F 134   O  TRP F 146
SHEET    3   U 6 PHE A1441  ILE A1445 -1  N  MET A1444   O  VAL F 133
SHEET    4   U 6 GLY G  59  ILE G  61 -1  O  ILE G  61   N  VAL A1443
SHEET    5   U 6 ALA G  68  ASN G  71 -1  O  GLU G  69   N  ARG G  60
SHEET    6   U 6 ASN G  10  LEU G  13 -1  N  ILE G  11   O  PHE G  70
SHEET    1   V 3 PHE B  92  VAL B  97  0
SHEET    2   V 3 GLY B 127  VAL B 132 -1  O  PHE B 129   N  TYR B  96
SHEET    3   V 3 VAL B 165  ARG B 169 -1  O  ILE B 167   N  LEU B 128
SHEET    1   W 3 PHE B 203  ILE B 205  0
SHEET    2   W 3 SER B 208  VAL B 211 -1  O  LYS B 210   N  PHE B 203
SHEET    3   W 3 GLN B 481  VAL B 482 -1  O  GLN B 481   N  VAL B 211
SHEET    1   X 4 LYS B 404  ASP B 407  0
SHEET    2   X 4 ALA B 214  SER B 218 -1  N  ARG B 217   O  ARG B 405
SHEET    3   X 4 ARG B 497  ASN B 499  1  O  ASN B 499   N  ALA B 214
SHEET    4   X 4 VAL B 536  ASN B 538 -1  O  LYS B 537   N  THR B 498
SHEET    1   Y 5 VAL B 223  LYS B 227  0
SHEET    2   Y 5 HIS B 236  ALA B 243 -1  O  GLU B 239   N  GLN B 224
SHEET    3   Y 5 ILE B 251  VAL B 256 -1  O  LEU B 254   N  ILE B 240
SHEET    4   Y 5 LYS B 270  THR B 272 -1  O  THR B 272   N  GLN B 255
SHEET    5   Y 5 ASP B 279  PRO B 281 -1  O  ILE B 280   N  ALA B 271
SHEET    1   Z 3 CYS B 544  ILE B 545  0
SHEET    2   Z 3 VAL B 633  ILE B 639 -1  O  TYR B 634   N  CYS B 544
SHEET    3   Z 3 VAL B 690  ILE B 693 -1  O  GLU B 691   N  LEU B 637
SHEET    1  AA 4 CYS B 544  ILE B 545  0
SHEET    2  AA 4 VAL B 633  ILE B 639 -1  O  TYR B 634   N  CYS B 544
SHEET    3  AA 4 HIS B 740  GLU B 742 -1  O  CYS B 741   N  PHE B 638
SHEET    4  AA 4 ILE B 703  ALA B 704  1  N  ALA B 704   O  GLU B 742
SHEET    1  AB 4 VAL B 585  GLY B 588  0
SHEET    2  AB 4 VAL B 580  VAL B 582 -1  N  VAL B 582   O  VAL B 585
SHEET    3  AB 4 LEU B 624  PHE B 627  1  O  LEU B 624   N  PHE B 581
SHEET    4  AB 4 SER B 614  ARG B 617 -1  N  SER B 614   O  PHE B 627
SHEET    1  AC 3 LEU B1010  ILE B1012  0
SHEET    2  AC 3 GLN B 821  ILE B 827  1  N  ALA B 826   O  LEU B1010
SHEET    3  AC 3 PHE B1086  TYR B1092 -1  O  TYR B1092   N  GLN B 821
SHEET    1  AD 2 ILE B 840  ASN B 842  0
SHEET    2  AD 2 ILE B 992  TYR B 994  1  O  ILE B 992   N  MET B 841
SHEET    1  AE 4 PHE B 856  GLN B 862  0
SHEET    2  AE 4 PHE B 963  ARG B 969 -1  O  VAL B 966   N  TYR B 859
SHEET    3  AE 4 GLY B 947  THR B 955 -1  N  ASP B 950   O  ARG B 967
SHEET    4  AE 4 ARG B 904  VAL B 905 -1  N  VAL B 905   O  GLY B 947
SHEET    1  AF 2 THR B 915  THR B 916  0
SHEET    2  AF 2 ARG B 935  ASP B 936 -1  O  ARG B 935   N  THR B 916
SHEET    1  AG 2 LYS B 979  PHE B 980  0
SHEET    2  AG 2 GLY B 988  THR B 989 -1  O  GLY B 988   N  PHE B 980
SHEET    1  AH 2 VAL C  18  LEU C  22  0
SHEET    2  AH 2 PHE C 228  VAL C 232 -1  O  PHE C 228   N  LEU C  22
SHEET    1  AI 4 THR C  53  ASN C  54  0
SHEET    2  AI 4 GLU C 152  LYS C 160 -1  O  LYS C 154   N  THR C  53
SHEET    3  AI 4 VAL C  97  PHE C 104 -1  N  LEU C  99   O  CYS C 157
SHEET    4  AI 4 VAL C 119  ILE C 120 -1  O  VAL C 119   N  THR C 100
SHEET    1  AJ 4 THR C  53  ASN C  54  0
SHEET    2  AJ 4 GLU C 152  LYS C 160 -1  O  LYS C 154   N  THR C  53
SHEET    3  AJ 4 ALA C  45  VAL C  49 -1  N  SER C  48   O  VAL C 158
SHEET    4  AJ 4 PHE L  67  GLU L  68 -1  O  PHE L  67   N  VAL C  49
SHEET    1  AK 2 THR C 111  TYR C 114  0
SHEET    2  AK 2 LEU C 143  LEU C 147 -1  O  CYS C 145   N  VAL C 113
SHEET    1  AL 2 LYS D  36  ILE D  38  0
SHEET    2  AL 2 GLU D  44  GLU D  46 -1  O  GLU D  45   N  GLN D  37
SHEET    1  AM 4 GLN E  61  ALA E  62  0
SHEET    2  AM 4 LEU E  78  TRP E  79 -1  O  LEU E  78   N  ALA E  62
SHEET    3  AM 4 THR E 107  GLY E 108  1  O  THR E 107   N  TRP E  79
SHEET    4  AM 4 THR E 131  ILE E 132  1  O  THR E 131   N  GLY E 108
SHEET    1  AN 2 VAL E 111  TYR E 112  0
SHEET    2  AN 2 PHE E 135  ASN E 136  1  O  PHE E 135   N  TYR E 112
SHEET    1  AO 3 ARG E 177  ILE E 178  0
SHEET    2  AO 3 GLY E 206  CYS E 214  1  O  ILE E 213   N  ILE E 178
SHEET    3  AO 3 VAL E 195  SER E 202 -1  N  ARG E 200   O  TYR E 208
SHEET    1  AP 3 PHE G   3  LEU G   7  0
SHEET    2  AP 3 TYR G  74  PHE G  79 -1  O  VAL G  78   N  PHE G   3
SHEET    3  AP 3 TYR G  44  VAL G  48 -1  N  CYS G  47   O  VAL G  77
SHEET    1  AQ 7 GLY G 169  ALA G 170  0
SHEET    2  AQ 7 ARG G 142  ILE G 151 -1  N  ARG G 144   O  GLY G 169
SHEET    3  AQ 7 HIS G 158  SER G 162 -1  O  HIS G 158   N  ILE G 151
SHEET    4  AQ 7 MET G 106  THR G 111  1  N  PHE G 109   O  GLY G 161
SHEET    5  AQ 7 GLY G  98  VAL G 103 -1  N  PHE G  99   O  VAL G 110
SHEET    6  AQ 7 GLU G  85  CYS G  94 -1  N  THR G  90   O  GLN G 102
SHEET    7  AQ 7 ARG G 142  ILE G 151 -1  O  ILE G 143   N  GLY G  89
SHEET    1  AR 2 TYR G 130  SER G 132  0
SHEET    2  AR 2 ASP G 135  ILE G 137 -1  O  ILE G 137   N  TYR G 130
SHEET    1  AS 7 SER H  54  THR H  56  0
SHEET    2  AS 7 ILE H   9  ASP H  16 -1  N  PHE H  10   O  LEU H  55
SHEET    3  AS 7 VAL H  23  SER H  30 -1  O  GLU H  27   N  SER H  13
SHEET    4  AS 7 LEU H  38  ASN H  43 -1  O  LEU H  40   N  ILE H  26
SHEET    5  AS 7 LEU H 121  ARG H 124 -1  O  ARG H 124   N  THR H  39
SHEET    6  AS 7 TYR H 115  PHE H 118 -1  N  PHE H 118   O  LEU H 121
SHEET    7  AS 7 THR H 100  ALA H 101 -1  N  THR H 100   O  SER H 117
SHEET    1  AT 2 THR H  58  ALA H  60  0
SHEET    2  AT 2 TYR H 141  LEU H 143 -1  O  TYR H 141   N  ALA H  60
SHEET    1  AU 2 GLU H 106  VAL H 107  0
SHEET    2  AU 2 LEU H 111  ILE H 112 -1  O  LEU H 111   N  VAL H 107
SHEET    1  AV 3 PRO I  16  GLU I  18  0
SHEET    2  AV 3 LEU I  25  GLU I  28 -1  O  LEU I  26   N  ARG I  17
SHEET    3  AV 3 VAL I  35  GLU I  37 -1  O  GLU I  36   N  PHE I  27
SHEET    1  AW 3 ASN I  83  VAL I  84  0
SHEET    2  AW 3 PHE I 100  CYS I 103 -1  O  VAL I 102   N  VAL I  84
SHEET    3  AW 3 ILE I 109  THR I 111 -1  O  PHE I 110   N  PHE I 101
SHEET    1  AX 4 ILE K  21  ASP K  22  0
SHEET    2  AX 4 ALA K  30  GLU K  36 -1  O  VAL K  32   N  ASP K  22
SHEET    3  AX 4 ARG K  70  THR K  77 -1  O  LEU K  73   N  ILE K  33
SHEET    4  AX 4 VAL K  56  LYS K  62 -1  N  ALA K  60   O  ARG K  74
SSBOND   1 CYS I   78    CYS I  103                          1555   1555  2.99
LINK         O3'  DA T  18                 P   8OG T  19     1555   1555  1.61
LINK         O3' 8OG T  19                 P    DG T  20     1555   1555  1.59
LINK         O3'  DC T  22                 P   BRU T  23     1555   1555  1.61
LINK         O3' BRU T  23                 P    DG T  24     1555   1555  1.60
LINK         SG  CYS A  67                ZN    ZN A2457     1555   1555  2.41
LINK         SG  CYS A  70                ZN    ZN A2457     1555   1555  2.31
LINK         SG  CYS A  77                ZN    ZN A2457     1555   1555  2.29
LINK         NE2 HIS A  80                ZN    ZN A2457     1555   1555  2.20
LINK         SG  CYS A 107                ZN    ZN A2456     1555   1555  2.72
LINK         SG  CYS A 110                ZN    ZN A2456     1555   1555  2.37
LINK         SG  CYS A 148                ZN    ZN A2456     1555   1555  2.59
LINK         SG  CYS A 167                ZN    ZN A2456     1555   1555  2.54
LINK         OD1 ASP A 481                MG    MG A2458     1555   1555  2.42
LINK         OD2 ASP A 483                MG    MG A2458     1555   1555  2.30
LINK         OD2 ASP A 485                MG    MG A2458     1555   1555  2.39
LINK         SG  CYS B1163                ZN    ZN B2225     1555   1555  2.66
LINK         SG  CYS B1166                ZN    ZN B2225     1555   1555  2.32
LINK         SG  CYS B1182                ZN    ZN B2225     1555   1555  2.52
LINK         SG  CYS B1185                ZN    ZN B2225     1555   1555  2.55
LINK         SG  CYS C  86                ZN    ZN C1269     1555   1555  2.36
LINK         SG  CYS C  88                ZN    ZN C1269     1555   1555  2.21
LINK         SG  CYS C  92                ZN    ZN C1269     1555   1555  2.49
LINK         SG  CYS C  95                ZN    ZN C1269     1555   1555  2.50
LINK         SG  CYS I   7                ZN    ZN I1121     1555   1555  2.38
LINK         SG  CYS I  10                ZN    ZN I1121     1555   1555  2.20
LINK         SG  CYS I  29                ZN    ZN I1121     1555   1555  2.46
LINK         SG  CYS I  32                ZN    ZN I1121     1555   1555  2.29
LINK         SG  CYS I  75                ZN    ZN I1122     1555   1555  2.44
LINK         SG  CYS I  78                ZN    ZN I1122     1555   1555  2.89
LINK         SG  CYS I 106                ZN    ZN I1122     1555   1555  2.57
LINK         SG  CYS J   7                ZN    ZN J1066     1555   1555  2.37
LINK         SG  CYS J  10                ZN    ZN J1066     1555   1555  2.38
LINK         SG  CYS J  45                ZN    ZN J1066     1555   1555  2.45
LINK         SG  CYS J  46                ZN    ZN J1066     1555   1555  2.46
LINK         SG  CYS L  31                ZN    ZN L1071     1555   1555  2.60
LINK         SG  CYS L  34                ZN    ZN L1071     1555   1555  2.28
LINK         SG  CYS L  48                ZN    ZN L1071     1555   1555  2.51
LINK         O3'   C P  10                MG    MG A2458     1555   1555  2.44
LINK         OP2   U P  11                MG    MG A2458     1555   1555  2.49
LINK         OD1 ASP A 485                MG    MG A2458     1555   1555  2.85
LINK         O5'   U P  11                MG    MG A2458     1555   1555  2.99
CISPEP   1 GLN A  447    PRO A  448          0         0.09
CISPEP   2 ARG A 1244    PRO A 1245          0         0.36
CISPEP   3 PRO E  128    PRO E  129          0         0.28
CISPEP   4 ASN G  126    PRO G  127          0         0.01
SITE     1 AC1  5 ASP A 481  ASP A 483  ASP A 485    C P  10
SITE     2 AC1  5   U P  11
SITE     1 AC2  5 CYS A 107  MET A 108  CYS A 110  CYS A 148
SITE     2 AC2  5 CYS A 167
SITE     1 AC3  4 CYS A  67  CYS A  70  CYS A  77  HIS A  80
SITE     1 AC4  4 CYS B1163  CYS B1166  CYS B1182  CYS B1185
SITE     1 AC5  4 CYS C  86  CYS C  88  CYS C  92  CYS C  95
SITE     1 AC6  5 CYS I   7  CYS I  10  CYS I  29  THR I  31
SITE     2 AC6  5 CYS I  32
SITE     1 AC7  5 CYS I  75  CYS I  78  CYS I 103  CYS I 106
SITE     2 AC7  5 HIS I 108
SITE     1 AC8  4 CYS J   7  CYS J  10  CYS J  45  CYS J  46
SITE     1 AC9  4 CYS L  31  CYS L  34  CYS L  48  CYS L  51
CRYST1  220.646  392.003  281.455  90.00  90.00  90.00 C 2 2 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      0.004532  0.000000  0.000000        0.00000
SCALE2      0.000000  0.002551  0.000000        0.00000
SCALE3      0.000000  0.000000  0.003553        0.00000
      
PROCHECK
Go to PROCHECK summary
 References