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PDBsum entry 1twg

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Top Page protein ligands metals Protein-protein interface(s) links
Transcription PDB id
1twg
Jmol
Contents
Protein chains
1349 a.a.
1091 a.a.
266 a.a.
215 a.a.
83 a.a.
133 a.a.
121 a.a.
64 a.a.
114 a.a.
46 a.a.
Ligands
CTP
Metals
_ZN ×8
_MN ×2
Waters ×5
HEADER    TRANSCRIPTION                           30-JUN-04   1TWG
TITLE     RNA POLYMERASE II COMPLEXED WITH CTP
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT;
COMPND   3 CHAIN: A;
COMPND   4 SYNONYM: B220;
COMPND   5 EC: 2.7.7.6;
COMPND   6 MOL_ID: 2;
COMPND   7 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 140 KDA
COMPND   8 POLYPEPTIDE;
COMPND   9 CHAIN: B;
COMPND  10 SYNONYM: B150, RNA POLYMERASE II SUBUNIT 2;
COMPND  11 EC: 2.7.7.6;
COMPND  12 MOL_ID: 3;
COMPND  13 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 45 KDA
COMPND  14 POLYPEPTIDE;
COMPND  15 CHAIN: C;
COMPND  16 SYNONYM: B44.5;
COMPND  17 EC: 2.7.7.6;
COMPND  18 MOL_ID: 4;
COMPND  19 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 27
COMPND  20 KDA POLYPEPTIDE;
COMPND  21 CHAIN: E;
COMPND  22 SYNONYM: ABC27;
COMPND  23 EC: 2.7.7.6;
COMPND  24 MOL_ID: 5;
COMPND  25 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 23
COMPND  26 KDA POLYPEPTIDE;
COMPND  27 CHAIN: F;
COMPND  28 SYNONYM: ABC23;
COMPND  29 EC: 2.7.7.6;
COMPND  30 MOL_ID: 6;
COMPND  31 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 14.5
COMPND  32 KDA POLYPEPTIDE;
COMPND  33 CHAIN: H;
COMPND  34 SYNONYM: ABC14.4;
COMPND  35 EC: 2.7.7.6;
COMPND  36 MOL_ID: 7;
COMPND  37 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 14.2 KDA
COMPND  38 POLYPEPTIDE;
COMPND  39 CHAIN: I;
COMPND  40 SYNONYM: B12.6;
COMPND  41 EC: 2.7.7.6;
COMPND  42 MOL_ID: 8;
COMPND  43 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 8.3
COMPND  44 KDA POLYPEPTIDE;
COMPND  45 CHAIN: J;
COMPND  46 SYNONYM: ABC10-BETA, ABC8;
COMPND  47 EC: 2.7.7.6;
COMPND  48 MOL_ID: 9;
COMPND  49 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 13.6 KDA
COMPND  50 POLYPEPTIDE;
COMPND  51 CHAIN: K;
COMPND  52 SYNONYM: B13.6;
COMPND  53 EC: 2.7.7.6;
COMPND  54 MOL_ID: 10;
COMPND  55 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 7.7
COMPND  56 KDA POLYPEPTIDE;
COMPND  57 CHAIN: L;
COMPND  58 SYNONYM: ABC10-ALPHA;
COMPND  59 EC: 2.7.7.6
SOURCE    MOL_ID: 1;
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE   4 ORGANISM_TAXID: 4932;
SOURCE   5 STRAIN: DELTA-RPB4;
SOURCE   6 MOL_ID: 2;
SOURCE   7 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE   8 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE   9 ORGANISM_TAXID: 4932;
SOURCE  10 STRAIN: DELTA-RPB4;
SOURCE  11 MOL_ID: 3;
SOURCE  12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  14 ORGANISM_TAXID: 4932;
SOURCE  15 STRAIN: DELTA-RPB4;
SOURCE  16 MOL_ID: 4;
SOURCE  17 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  18 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  19 ORGANISM_TAXID: 4932;
SOURCE  20 STRAIN: DELTA-RPB4;
SOURCE  21 MOL_ID: 5;
SOURCE  22 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  23 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  24 ORGANISM_TAXID: 4932;
SOURCE  25 STRAIN: DELTA-RPB4;
SOURCE  26 MOL_ID: 6;
SOURCE  27 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  28 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  29 ORGANISM_TAXID: 4932;
SOURCE  30 STRAIN: DELTA-RPB4;
SOURCE  31 MOL_ID: 7;
SOURCE  32 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  33 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  34 ORGANISM_TAXID: 4932;
SOURCE  35 STRAIN: DELTA-RPB4;
SOURCE  36 MOL_ID: 8;
SOURCE  37 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  38 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  39 ORGANISM_TAXID: 4932;
SOURCE  40 STRAIN: DELTA-RPB4;
SOURCE  41 MOL_ID: 9;
SOURCE  42 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  43 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  44 ORGANISM_TAXID: 4932;
SOURCE  45 STRAIN: DELTA-RPB4;
SOURCE  46 MOL_ID: 10;
SOURCE  47 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  48 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  49 ORGANISM_TAXID: 4932;
SOURCE  50 STRAIN: DELTA-RPB4
KEYWDS    TRANSCRIPTION, MRNA, MULTIPROTEIN COMPLEX, MOLECULAR
KEYWDS   2 MACHINE, ZINC MOTIFS
EXPDTA    X-RAY DIFFRACTION
AUTHOR    K.D.WESTOVER,D.A.BUSHNELL,R.D.KORNBERG
REVDAT   3   24-FEB-09 1TWG    1       VERSN
REVDAT   2   14-DEC-04 1TWG    1       JRNL
REVDAT   1   16-NOV-04 1TWG    0
JRNL        AUTH   K.D.WESTOVER,D.A.BUSHNELL,R.D.KORNBERG
JRNL        TITL   STRUCTURAL BASIS OF TRANSCRIPTION: NUCLEOTIDE
JRNL        TITL 2 SELECTION BY ROTATION IN THE RNA POLYMERASE II
JRNL        TITL 3 ACTIVE CENTER.
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 119   481 2004
JRNL        REFN                   ISSN 0092-8674
JRNL        PMID   15537538
JRNL        DOI    10.1016/J.CELL.2004.10.016
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : CNS
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) : 3.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 77786
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : NULL
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL
REMARK   3   R VALUE            (WORKING SET) : 0.263
REMARK   3   FREE R VALUE                     : 0.281
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            : 27687
REMARK   3   NUCLEIC ACID ATOMS       : 0
REMARK   3   HETEROGEN ATOMS          : 39
REMARK   3   SOLVENT ATOMS            : 5
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : NULL
REMARK   3    B22 (A**2) : NULL
REMARK   3    B33 (A**2) : NULL
REMARK   3    B12 (A**2) : NULL
REMARK   3    B13 (A**2) : NULL
REMARK   3    B23 (A**2) : NULL
REMARK   3
REMARK   3  ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL
REMARK   3   ESD FROM SIGMAA              (A) : NULL
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL
REMARK   3
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.
REMARK   3   BOND LENGTHS                 (A) : NULL
REMARK   3   BOND ANGLES            (DEGREES) : NULL
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL MODEL : NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL
REMARK   3
REMARK   3  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 1TWG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-04.
REMARK 100 THE RCSB ID CODE IS RCSB022969.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-01
REMARK 200  TEMPERATURE           (KELVIN) : 100.0
REMARK 200  PH                             : 6.00
REMARK 200  NUMBER OF CRYSTALS USED        : 1
REMARK 200
REMARK 200  SYNCHROTRON              (Y/N) : Y
REMARK 200  RADIATION SOURCE               : SSRL
REMARK 200  BEAMLINE                       : BL11-1
REMARK 200  X-RAY GENERATOR MODEL          : NULL
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : NULL
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 77786
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL
REMARK 200  DATA REDUNDANCY                : NULL
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : NULL
REMARK 200   FOR THE DATA SET  : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : NULL
REMARK 200   FOR SHELL         : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1I50
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 54.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, AMMONIUM HYDROGEN
REMARK 280  PHOSPHATE, SODIUM DIHYDROGEN PHOSPHATE, DIOXANE, DTT, PH 6.00,
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290      SYMOP   SYMMETRY
REMARK 290     NNNMMM   OPERATOR
REMARK 290       1555   X,Y,Z
REMARK 290       2555   -X,-Y,Z
REMARK 290       3555   -X,Y,-Z
REMARK 290       4555   X,-Y,-Z
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2
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+1/2
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        0.00000
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        0.00000
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       61.50000
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      111.50000
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      187.00000
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       61.50000
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      111.50000
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      187.00000
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       61.50000
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      111.50000
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      187.00000
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       61.50000
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      111.50000
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      187.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3
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: DECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 55370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 144430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -271.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, F, H, I, J, K, L
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 40-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 238570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 560620 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1145.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, E, F, J, I, C, K, L
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      123.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000      123.00000
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000        0.00000
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: EICOSAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 116550 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 283040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -570.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, E, F, J, I, C, K, L
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      123.00000
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000
REMARK 350   BIOMT3   2  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     VAL A     2
REMARK 465     SER A   249
REMARK 465     ILE A   250
REMARK 465     SER A   251
REMARK 465     PHE A   252
REMARK 465     ASN A   253
REMARK 465     GLU A   254
REMARK 465     SER A   255
REMARK 465     GLN A   256
REMARK 465     ARG A   257
REMARK 465     GLY A   258
REMARK 465     GLU A   259
REMARK 465     ASP A   260
REMARK 465     ASN A   306
REMARK 465     ASP A   307
REMARK 465     ILE A   308
REMARK 465     ALA A   309
REMARK 465     GLY A   310
REMARK 465     GLN A   311
REMARK 465     PRO A   312
REMARK 465     GLN A   313
REMARK 465     ALA A   314
REMARK 465     LEU A   315
REMARK 465     GLN A   316
REMARK 465     LYS A   317
REMARK 465     SER A   318
REMARK 465     GLY A   319
REMARK 465     ARG A   320
REMARK 465     PRO A   321
REMARK 465     VAL A   322
REMARK 465     LYS A   323
REMARK 465     ARG A   328
REMARK 465     LEU A   329
REMARK 465     LYS A   330
REMARK 465     GLY A   331
REMARK 465     LYS A   332
REMARK 465     GLU A   333
REMARK 465     GLY A   334
REMARK 465     ARG A   335
REMARK 465     ILE A   336
REMARK 465     ARG A   337
REMARK 465     GLY A   338
REMARK 465     ASN A   339
REMARK 465     LEU A   340
REMARK 465     MET A   341
REMARK 465     GLY A   342
REMARK 465     LYS A   343
REMARK 465     ARG A   344
REMARK 465     VAL A   345
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     PHE A  1174
REMARK 465     SER A  1175
REMARK 465     LEU A  1177
REMARK 465     ASP A  1178
REMARK 465     GLU A  1179
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     ARG A  1244
REMARK 465     PRO A  1245
REMARK 465     LYS A  1246
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     ARG A  1386
REMARK 465     HIS A  1387
REMARK 465     GLY A  1388
REMARK 465     PHE A  1389
REMARK 465     ASN A  1390
REMARK 465     ARG A  1391
REMARK 465     SER A  1392
REMARK 465     ASN A  1393
REMARK 465     THR A  1394
REMARK 465     GLY A  1395
REMARK 465     ALA A  1396
REMARK 465     LEU A  1397
REMARK 465     MET A  1398
REMARK 465     ARG A  1399
REMARK 465     CYS A  1400
REMARK 465     SER A  1401
REMARK 465     PHE A  1402
REMARK 465     GLU A  1403
REMARK 465     GLU A  1404
REMARK 465     VAL A  1451
REMARK 465     LYS A  1452
REMARK 465     TYR A  1453
REMARK 465     MET A  1454
REMARK 465     PRO A  1455
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     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     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     GLU B   468
REMARK 465     GLN B   469
REMARK 465     LYS B   470
REMARK 465     LYS B   471
REMARK 465     ALA B   472
REMARK 465     MET B   473
REMARK 465     SER B   474
REMARK 465     SER B   475
REMARK 465     ARG B   476
REMARK 465     GLY B   503
REMARK 465     ARG B   504
REMARK 465     ASP B   505
REMARK 465     GLY B   506
REMARK 465     LYS B   507
REMARK 465     LEU B   508
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     ALA B   713
REMARK 465     GLU B   714
REMARK 465     ALA B   715
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   917
REMARK 465     ILE B   918
REMARK 465     SER B   919
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     MET B  1111
REMARK 465     GLN B  1112
REMARK 465     VAL B  1113
REMARK 465     LEU B  1114
REMARK 465     THR B  1115
REMARK 465     ARG B  1116
REMARK 465     GLN B  1117
REMARK 465     PRO B  1118
REMARK 465     VAL B  1119
REMARK 465     GLU B  1120
REMARK 465     GLY B  1121
REMARK 465     ARG B  1122
REMARK 465     SER B  1123
REMARK 465     ARG B  1124
REMARK 465     ASP B  1125
REMARK 465     GLY B  1126
REMARK 465     MET C     1
REMARK 465     SER C     2
REMARK 465     LYS C   269
REMARK 465     VAL C   270
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     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     THR F    68
REMARK 465     LEU F    69
REMARK 465     LYS F    70
REMARK 465     GLU F    71
REMARK 465     LEU F   155
REMARK 465     MET H     1
REMARK 465     ASN H    64
REMARK 465     LEU H    65
REMARK 465     GLU H    66
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     SER I   122
REMARK 465     PRO J    65
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     ALA K   115
REMARK 465     ALA K   116
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     THR L    24
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   NZ   LYS A   567     CE1  TYR H    95              1.45
REMARK 500   O    PHE H   104     N    GLU H   106              1.50
REMARK 500   OG   SER A   369     ND2  ASN K     2              1.60
REMARK 500   C2'  CTP B  3008     O    HOH B  3010              1.65
REMARK 500   C3'  CTP B  3008     O    HOH B  3010              1.74
REMARK 500   O    ASN H   128     ND2  ASN H   131              1.82
REMARK 500   OD2  ASP A    42     N    ARG A    47              1.84
REMARK 500   OD1  ASP A   555     NZ   LYS K    26              1.89
REMARK 500   NZ   LYS A   567     CZ   TYR H    95              1.93
REMARK 500   SG   CYS A    70     NE2  HIS A    80              1.94
REMARK 500   OD2  ASP K    53     OH   TYR K    81              1.97
REMARK 500   O    ASP A    55     N    ARG A    57              1.99
REMARK 500   O    ASN K   110     N    GLN K   112              2.01
REMARK 500   O    CYS B  1166     N    LEU B  1168              2.01
REMARK 500   O    LEU H    89     N    ASP H    91              2.02
REMARK 500   N    THR B   916     O    ARG B   935              2.03
REMARK 500   OH   TYR B   890     OD1  ASP B   936              2.06
REMARK 500   O    CYS E    83     NE2  GLN E   113              2.07
REMARK 500   O    PRO F    75     O    ASP F    77              2.10
REMARK 500   NZ   LYS E    71     OE2  GLU E   160              2.10
REMARK 500   O    LEU H     5     ND2  ASN H   133              2.11
REMARK 500   O    GLU H   138     N    ALA H   140              2.11
REMARK 500   OE2  GLU E     6     NZ   LYS E    43              2.11
REMARK 500   O    GLY A    73     N    ASN A    75              2.12
REMARK 500   O    ARG B   261     N    SER B   264              2.12
REMARK 500   OD1  ASP K    24     NH1  ARG K    74              2.13
REMARK 500   OE1  GLU B   104     NE   ARG L    54              2.13
REMARK 500   O    PHE H   104     CA   GLU H   106              2.14
REMARK 500   OE2  GLU E    85     OG1  THR E    92              2.15
REMARK 500   CE   LYS A   752     OG   SER B  1019              2.15
REMARK 500   NZ   LYS H   103     OE2  GLU H   105              2.16
REMARK 500   OG1  THR B    98     O    GLY B   127              2.17
REMARK 500   O3A  CTP B  3008     O    HOH B  3010              2.17
REMARK 500   CG   MET A  1079     OD2  ASP A  1359              2.18
REMARK 500   C1'  CTP B  3008     O    HOH B  3010              2.18
REMARK 500   O    ASP A   156     CD   PRO A   158              2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE
REMARK 500   O    ARG B   434     ND2  ASN B   465     2655     2.11
REMARK 500   OD1  ASP B  1223     CE   MET E     1     8455     2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION
REMARK 500    GLY A   3   N     GLY A   3   CA      0.148
REMARK 500    GLN A   4   CB    GLN A   4   CG      0.283
REMARK 500    GLN A   4   CA    GLN A   4   C       0.161
REMARK 500    GLN A   5   CA    GLN A   5   CB      0.140
REMARK 500    GLN A   5   CB    GLN A   5   CG      0.371
REMARK 500    GLN A   5   C     GLN A   5   O      -0.130
REMARK 500    TYR A   6   CG    TYR A   6   CD1     0.113
REMARK 500    TYR A   6   CE1   TYR A   6   CZ      0.090
REMARK 500    TYR A   6   C     TYR A   6   O       0.131
REMARK 500    SER A   7   N     SER A   7   CA      0.184
REMARK 500    SER A   7   CB    SER A   7   OG     -0.085
REMARK 500    SER A   8   CA    SER A   8   CB      0.091
REMARK 500    ALA A   9   CA    ALA A   9   CB      0.285
REMARK 500    PRO A  10   CG    PRO A  10   CD      0.195
REMARK 500    ARG A  12   CZ    ARG A  12   NH1     0.113
REMARK 500    ARG A  12   C     ARG A  12   O      -0.170
REMARK 500    LYS A  15   CB    LYS A  15   CG      0.273
REMARK 500    LYS A  15   CD    LYS A  15   CE      0.160
REMARK 500    LYS A  15   CE    LYS A  15   NZ      0.156
REMARK 500    GLU A  16   CG    GLU A  16   CD      0.160
REMARK 500    GLU A  16   CD    GLU A  16   OE1     0.168
REMARK 500    GLU A  16   CD    GLU A  16   OE2     0.245
REMARK 500    GLU A  16   C     GLU A  16   O       0.177
REMARK 500    PHE A  19   CD1   PHE A  19   CE1    -0.211
REMARK 500    PHE A  19   CZ    PHE A  19   CE2    -0.115
REMARK 500    PHE A  22   CB    PHE A  22   CG     -0.105
REMARK 500    PHE A  22   CE1   PHE A  22   CZ      0.125
REMARK 500    PRO A  24   CB    PRO A  24   CG      0.358
REMARK 500    PRO A  24   CG    PRO A  24   CD     -0.243
REMARK 500    PRO A  24   CA    PRO A  24   C       0.219
REMARK 500    GLU A  26   CD    GLU A  26   OE2    -0.096
REMARK 500    VAL A  27   CA    VAL A  27   CB     -0.156
REMARK 500    VAL A  27   CB    VAL A  27   CG1     0.160
REMARK 500    VAL A  27   C     VAL A  27   O       0.127
REMARK 500    ARG A  28   NE    ARG A  28   CZ      0.102
REMARK 500    ARG A  28   C     ARG A  28   O       0.140
REMARK 500    SER A  31   CA    SER A  31   C       0.220
REMARK 500    SER A  31   C     SER A  31   O       0.149
REMARK 500    ALA A  33   CA    ALA A  33   CB      0.156
REMARK 500    LYS A  34   CB    LYS A  34   CG      0.241
REMARK 500    LYS A  34   C     LYS A  34   O      -0.123
REMARK 500    ILE A  35   CA    ILE A  35   C       0.174
REMARK 500    ARG A  36   NE    ARG A  36   CZ      0.115
REMARK 500    PHE A  37   CB    PHE A  37   CG      0.156
REMARK 500    PHE A  37   CG    PHE A  37   CD2     0.208
REMARK 500    PHE A  37   CD1   PHE A  37   CE1     0.245
REMARK 500    PHE A  37   CE1   PHE A  37   CZ      0.210
REMARK 500    PHE A  37   CE2   PHE A  37   CD2     0.176
REMARK 500    PHE A  37   C     PHE A  37   O      -0.122
REMARK 500    GLU A  39   CD    GLU A  39   OE2    -0.086
REMARK 500
REMARK 500 THIS ENTRY HAS    4676 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3
REMARK 500    GLN A   4   CB  -  CA  -  C   ANGL. DEV. =  13.2 DEGREES
REMARK 500    GLN A   5   N   -  CA  -  CB  ANGL. DEV. =  11.4 DEGREES
REMARK 500    LEU A  11   CB  -  CG  -  CD2 ANGL. DEV. =  13.9 DEGREES
REMARK 500    ARG A  12   CG  -  CD  -  NE  ANGL. DEV. = -17.4 DEGREES
REMARK 500    ARG A  12   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES
REMARK 500    ARG A  12   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.4 DEGREES
REMARK 500    VAL A  17   CG1 -  CB  -  CG2 ANGL. DEV. = -13.3 DEGREES
REMARK 500    PHE A  22   CB  -  CG  -  CD1 ANGL. DEV. =  -6.6 DEGREES
REMARK 500    PHE A  22   N   -  CA  -  C   ANGL. DEV. = -17.4 DEGREES
REMARK 500    PRO A  24   N   -  CD  -  CG  ANGL. DEV. =  10.5 DEGREES
REMARK 500    GLU A  25   CG  -  CD  -  OE2 ANGL. DEV. = -13.0 DEGREES
REMARK 500    ILE A  30   CG1 -  CB  -  CG2 ANGL. DEV. =  20.3 DEGREES
REMARK 500    VAL A  32   CG1 -  CB  -  CG2 ANGL. DEV. = -19.8 DEGREES
REMARK 500    ILE A  35   CG1 -  CB  -  CG2 ANGL. DEV. = -15.0 DEGREES
REMARK 500    MET A  41   CG  -  SD  -  CE  ANGL. DEV. =  14.6 DEGREES
REMARK 500    ASP A  42   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES
REMARK 500    ASP A  42   CB  -  CG  -  OD2 ANGL. DEV. =  13.5 DEGREES
REMARK 500    ARG A  47   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES
REMARK 500    LYS A  49   CB  -  CG  -  CD  ANGL. DEV. =  18.6 DEGREES
REMARK 500    ILE A  50   CB  -  CA  -  C   ANGL. DEV. = -18.4 DEGREES
REMARK 500    LEU A  53   CA  -  CB  -  CG  ANGL. DEV. =  24.0 DEGREES
REMARK 500    LEU A  53   CB  -  CG  -  CD1 ANGL. DEV. =  13.9 DEGREES
REMARK 500    ASN A  54   CA  -  C   -  N   ANGL. DEV. =  15.0 DEGREES
REMARK 500    PRO A  56   O   -  C   -  N   ANGL. DEV. =  10.5 DEGREES
REMARK 500    GLY A  59   N   -  CA  -  C   ANGL. DEV. =  20.4 DEGREES
REMARK 500    ILE A  61   N   -  CA  -  C   ANGL. DEV. = -24.8 DEGREES
REMARK 500    ARG A  63   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES
REMARK 500    LEU A  65   CA  -  CB  -  CG  ANGL. DEV. =  15.7 DEGREES
REMARK 500    LEU A  65   CB  -  CG  -  CD2 ANGL. DEV. =  17.5 DEGREES
REMARK 500    CYS A  67   CB  -  CA  -  C   ANGL. DEV. =   7.5 DEGREES
REMARK 500    CYS A  70   CA  -  CB  -  SG  ANGL. DEV. =  21.6 DEGREES
REMARK 500    GLU A  72   OE1 -  CD  -  OE2 ANGL. DEV. =  -8.3 DEGREES
REMARK 500    MET A  74   CG  -  SD  -  CE  ANGL. DEV. =  23.0 DEGREES
REMARK 500    CYS A  77   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES
REMARK 500    GLY A  79   N   -  CA  -  C   ANGL. DEV. = -16.5 DEGREES
REMARK 500    PHE A  81   CB  -  CG  -  CD2 ANGL. DEV. =   4.4 DEGREES
REMARK 500    PHE A  81   CD1 -  CG  -  CD2 ANGL. DEV. =  -8.7 DEGREES
REMARK 500    ASP A  85   CB  -  CG  -  OD1 ANGL. DEV. =  -9.6 DEGREES
REMARK 500    LEU A  86   CB  -  CG  -  CD2 ANGL. DEV. =  17.3 DEGREES
REMARK 500    VAL A  90   N   -  CA  -  CB  ANGL. DEV. = -15.0 DEGREES
REMARK 500    VAL A  93   CB  -  CA  -  C   ANGL. DEV. = -19.7 DEGREES
REMARK 500    PHE A  95   N   -  CA  -  CB  ANGL. DEV. = -12.2 DEGREES
REMARK 500    ILE A  96   CG1 -  CB  -  CG2 ANGL. DEV. = -24.2 DEGREES
REMARK 500    LYS A  98   CG  -  CD  -  CE  ANGL. DEV. = -18.8 DEGREES
REMARK 500    ILE A  99   CG1 -  CB  -  CG2 ANGL. DEV. = -14.1 DEGREES
REMARK 500    CYS A 107   CA  -  CB  -  SG  ANGL. DEV. =  20.8 DEGREES
REMARK 500    CYS A 107   N   -  CA  -  C   ANGL. DEV. = -18.4 DEGREES
REMARK 500    CYS A 110   CA  -  CB  -  SG  ANGL. DEV. =  10.7 DEGREES
REMARK 500    LYS A 112   CD  -  CE  -  NZ  ANGL. DEV. = -17.5 DEGREES
REMARK 500    LEU A 113   CB  -  CG  -  CD1 ANGL. DEV. = -15.0 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS    1999 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A  23      153.96    -47.66
REMARK 500    VAL A  32      -97.45    -80.01
REMARK 500    ILE A  35      108.16     19.58
REMARK 500    ARG A  36      -58.08   -143.96
REMARK 500    MET A  41      169.72     67.95
REMARK 500    ASP A  42       75.74     62.37
REMARK 500    GLU A  43       87.07    -52.27
REMARK 500    THR A  44      -43.67     76.20
REMARK 500    GLN A  45       29.97    149.01
REMARK 500    ARG A  47       77.26    -54.32
REMARK 500    ALA A  48      -86.24   -131.77
REMARK 500    ASN A  54      -73.68     69.61
REMARK 500    PRO A  56       13.94    -38.51
REMARK 500    ARG A  57      -20.30    118.45
REMARK 500    LEU A  58     -160.38    -79.13
REMARK 500    SER A  60      119.44    165.14
REMARK 500    ASP A  62       -4.41    136.55
REMARK 500    ARG A  63      -42.98     70.18
REMARK 500    ASN A  64      101.81    -49.14
REMARK 500    LEU A  65       57.67    -44.20
REMARK 500    CYS A  67     -104.67   -135.43
REMARK 500    THR A  69       20.30     41.37
REMARK 500    GLN A  71      -94.21     59.97
REMARK 500    GLU A  72      166.75     -6.13
REMARK 500    MET A  74       42.22    -62.10
REMARK 500    ASN A  75      -43.52   -166.32
REMARK 500    GLU A 104       -3.62    -51.18
REMARK 500    HIS A 109      -64.14    -96.85
REMARK 500    ASP A 116     -153.17   -155.91
REMARK 500    GLU A 120      -69.32    107.07
REMARK 500    ALA A 136      -71.68    -49.56
REMARK 500    ASP A 151      140.65   -175.06
REMARK 500    GLU A 155      -98.39    -51.28
REMARK 500    ASP A 156     -158.85     21.91
REMARK 500    PRO A 158       19.69    -63.49
REMARK 500    CYS A 167      -64.90     86.20
REMARK 500    SER A 184       99.17   -162.37
REMARK 500    LYS A 186     -156.10   -129.86
REMARK 500    ASP A 188     -159.56   -179.45
REMARK 500    ALA A 190       57.58    108.19
REMARK 500    THR A 191     -123.23   -108.71
REMARK 500    ASP A 193      -57.26    101.51
REMARK 500    ALA A 194       99.16   -165.93
REMARK 500    GLU A 196      123.08     70.99
REMARK 500    ARG A 200      129.34   -177.97
REMARK 500    THR A 237      -29.43   -157.41
REMARK 500    LEU A 279      -45.49   -165.47
REMARK 500    ALA A 284      146.54    174.44
REMARK 500    HIS A 286      -79.28    -24.30
REMARK 500    ARG A 326       52.33    -44.27
REMARK 500    PHE A 347       36.81     72.11
REMARK 500    PRO A 400       94.08     -9.90
REMARK 500    ASP A 408      -67.66     -9.28
REMARK 500    LEU A 415        4.40    -63.80
REMARK 500    TYR A 417      -84.05   -106.39
REMARK 500    SER A 418       98.33     21.27
REMARK 500    ASN A 439       -2.89     80.60
REMARK 500    PRO A 464     -107.77    -75.14
REMARK 500    TYR A 465     -144.25    -68.72
REMARK 500    GLN A 525     -113.21     49.71
REMARK 500    LYS A 567     -101.94    -52.49
REMARK 500    ASP A 592     -156.06    -96.64
REMARK 500    SER A 599       92.91    -14.75
REMARK 500    ASP A 602       47.19     75.31
REMARK 500    ASP A 609       47.43     33.10
REMARK 500    GLU A 618     -159.19   -148.88
REMARK 500    SER A 624       52.10    -97.14
REMARK 500    HIS A 706      124.57     80.40
REMARK 500    THR A 709      159.55    -46.51
REMARK 500    ASN A 736       -9.58    -58.01
REMARK 500    LYS A 752      141.76   -174.20
REMARK 500    ASP A 853        7.73    -67.46
REMARK 500    ASP A 871      -14.82   -160.23
REMARK 500    THR A 885      -31.72    -35.26
REMARK 500    ASP A 909      150.74    -47.65
REMARK 500    SER A 915       14.00    -51.77
REMARK 500    PHE A 947       73.73   -118.18
REMARK 500    VAL A 958       98.88     55.09
REMARK 500    HIS A 972       72.75     50.80
REMARK 500    MET A1063       79.00   -101.01
REMARK 500    GLN A1078       34.52    -91.95
REMARK 500    THR A1080       52.98    -33.75
REMARK 500    THR A1113       66.45   -107.50
REMARK 500    GLN A1128      -31.71    -35.98
REMARK 500    LEU A1172       37.83    -75.58
REMARK 500    SER A1189      133.10    -29.16
REMARK 500    ALA A1200      -76.72    -30.61
REMARK 500    ASP A1204      -10.94    -42.48
REMARK 500    LYS A1221     -120.69    109.16
REMARK 500    ASP A1223       -3.14    -53.44
REMARK 500    GLU A1234      -40.83     83.31
REMARK 500    GLU A1255       27.61     82.87
REMARK 500    GLU A1256       41.62    -75.05
REMARK 500    ASN A1278       -7.25     80.91
REMARK 500    GLU A1280     -100.16    -81.89
REMARK 500    ILE A1327      138.78    -35.86
REMARK 500    ASP A1359       -9.95    -51.08
REMARK 500    GLU A1448       -5.17    -31.10
REMARK 500    GLU B  19      121.04     75.63
REMARK 500    ASP B  56      -18.38    -46.82
REMARK 500    TYR B  57      -46.46   -148.67
REMARK 500    ASP B  66       55.14      5.98
REMARK 500    LEU B  69     -153.20   -116.25
REMARK 500    ILE B  90      110.48     67.65
REMARK 500    SER B 105       87.78    -64.13
REMARK 500    ASP B 106       99.00     69.05
REMARK 500    VAL B 108      137.69     58.55
REMARK 500    THR B 109      109.10     33.23
REMARK 500    ALA B 111      130.75    -37.92
REMARK 500    TYR B 124       83.76    -62.43
REMARK 500    VAL B 130     -167.87    -76.83
REMARK 500    TYR B 137      124.79    173.85
REMARK 500    VAL B 165       97.13    102.84
REMARK 500    ARG B 175        4.84     56.04
REMARK 500    ASN B 178        5.37    -65.17
REMARK 500    ASN B 221       10.36     82.64
REMARK 500    ALA B 230      -63.84     22.18
REMARK 500    ALA B 243      173.13    178.11
REMARK 500    SER B 248     -146.90   -128.65
REMARK 500    ILE B 251       79.84   -118.62
REMARK 500    GLU B 262      100.33    -48.70
REMARK 500    ALA B 266       92.42     29.07
REMARK 500    TYR B 303       38.33    -86.16
REMARK 500    ASP B 304      104.35   -161.62
REMARK 500    ASP B 307       68.77    -66.47
REMARK 500    LEU B 361       64.46     30.55
REMARK 500    ILE B 364      -74.93    -79.71
REMARK 500    ASP B 391       43.08     79.65
REMARK 500    ARG B 398       -4.63    -59.68
REMARK 500    LEU B 408     -163.54   -106.88
REMARK 500    THR B 419      -39.19    -38.49
REMARK 500    LYS B 423      -71.88    -62.51
REMARK 500    LEU B 424      -31.37    -34.40
REMARK 500    TYR B 431       35.48    -95.54
REMARK 500    MET B 432      -35.28   -179.29
REMARK 500    ARG B 434       44.86   -109.24
REMARK 500    VAL B 436       -1.56    -50.37
REMARK 500    ALA B 447       40.43     76.09
REMARK 500    ALA B 450      -64.69   -100.99
REMARK 500    LYS B 451      -52.98    -18.40
REMARK 500    THR B 452      -33.55    -35.81
REMARK 500    TRP B 466      -71.27   -161.16
REMARK 500    TRP B 519      119.01    -37.04
REMARK 500    CYS B 533      108.46    -40.77
REMARK 500    ASN B 583       45.45     39.86
REMARK 500    ASN B 592       62.52   -113.38
REMARK 500    ASP B 643      -67.79   -158.51
REMARK 500    GLU B 644      113.55     76.62
REMARK 500    SER B 645      -87.41     24.43
REMARK 500    LEU B 646       30.23    -52.84
REMARK 500    GLU B 708       12.74    -67.15
REMARK 500    GLU B 711      145.72    -25.77
REMARK 500    ASP B 724       96.17    -45.37
REMARK 500    PRO B 725      -10.46    -49.85
REMARK 500    HIS B 733       70.22     -4.58
REMARK 500    HIS B 734       35.34    -87.29
REMARK 500    ASN B 784       38.09    -89.51
REMARK 500    ALA B 819       61.15   -154.36
REMARK 500    TYR B 830       86.41   -159.19
REMARK 500    SER B 831      -23.80    107.41
REMARK 500    ASN B 834       41.17   -105.18
REMARK 500    GLU B 863     -147.62   -105.56
REMARK 500    LYS B 864      171.86    -32.82
REMARK 500    LYS B 865     -130.91   -150.50
REMARK 500    MET B 868       75.80    -69.46
REMARK 500    SER B 869       42.76     35.15
REMARK 500    LYS B 876      104.25    -58.35
REMARK 500    GLN B 878      -28.47   -149.65
REMARK 500    ARG B 879       69.70    121.49
REMARK 500    MET B 885     -158.25   -105.67
REMARK 500    HIS B 887        2.34    -34.80
REMARK 500    ASP B 891        1.17    -54.40
REMARK 500    ASP B 894     -168.08    -66.98
REMARK 500    SER B 906     -170.05   -170.15
REMARK 500    ASP B 909      128.15    -38.71
REMARK 500    ILE B 911      -32.44   -132.23
REMARK 500    SER B 943      -51.37    -28.67
REMARK 500    THR B 955     -167.87   -167.09
REMARK 500    ASN B 957     -167.68    -45.48
REMARK 500    ARG B 983       32.99    -89.28
REMARK 500    GLU B1004       12.46    -69.47
REMARK 500    THR B1022       69.91   -108.18
REMARK 500    HIS B1097       76.09     93.10
REMARK 500    VAL B1099       -8.36    -54.09
REMARK 500    ASP B1101      -16.70    -47.30
REMARK 500    LYS B1102      -55.52   -132.71
REMARK 500    ALA B1105       59.64   -175.89
REMARK 500    ARG B1108      160.54     20.59
REMARK 500    LEU B1128       44.84    106.34
REMARK 500    PHE B1130       68.24   -153.30
REMARK 500    SER B1155      101.95    -30.18
REMARK 500    ALA B1157       76.31    -67.73
REMARK 500    PHE B1158      130.12    -26.90
REMARK 500    LYS B1183      113.21    -34.13
REMARK 500    ILE B1189      -81.56    -68.82
REMARK 500    ASN B1211       15.31     55.69
REMARK 500    ARG B1220      -82.26    -70.36
REMARK 500    SER B1221       35.14    -65.31
REMARK 500    ARG B1222     -172.62     74.19
REMARK 500    ASP B1223       -4.27    -48.10
REMARK 500    GLU C   4      128.23     25.11
REMARK 500    LYS C   9       45.01    174.77
REMARK 500    ILE C  10      133.54    -20.26
REMARK 500    THR C  56      170.61    -54.82
REMARK 500    ASP C  76       45.45    -91.45
REMARK 500    ASP C  90      -98.70     59.15
REMARK 500    CYS C  92     -168.79   -171.32
REMARK 500    SER C  96      136.14   -170.11
REMARK 500    GLU C 106      -60.68    -96.11
REMARK 500    SER C 107      156.97    -48.65
REMARK 500    ASP C 117        9.06    -67.86
REMARK 500    VAL C 121       23.07   -146.73
REMARK 500    LEU C 124       -7.98    -57.82
REMARK 500    MET C 125       41.68     31.55
REMARK 500    ALA C 174     -120.13   -105.41
REMARK 500    PHE C 178      125.43   -172.10
REMARK 500    PRO C 182      -19.04    -49.11
REMARK 500    ASN C 184       68.92   -114.56
REMARK 500    GLU C 194      -63.25   -101.31
REMARK 500    ASN C 206        5.57    -45.01
REMARK 500    GLU C 208      -57.86    -24.24
REMARK 500    TYR C 209       16.06    -60.98
REMARK 500    PRO C 212      150.14    -41.16
REMARK 500    ASP C 217      108.87    -13.46
REMARK 500    ASN C 231       95.67    168.25
REMARK 500    ASP C 266     -160.38    -72.45
REMARK 500    GLN C 267     -133.79     77.95
REMARK 500    ASP E   2       40.85   -166.33
REMARK 500    ASN E   8      -39.03    -34.32
REMARK 500    ARG E  11      -65.32    -24.10
REMARK 500    LEU E  37      103.20    -25.84
REMARK 500    ALA E  44      -81.79    -69.14
REMARK 500    ASP E  48      175.54    -51.26
REMARK 500    MET E  50      -35.58   -170.16
REMARK 500    LYS E  56      -68.84    -11.60
REMARK 500    SER E  59      161.37    -36.57
REMARK 500    PRO E  64     -169.91    -48.45
REMARK 500    GLU E  81      136.85   -174.14
REMARK 500    ASN E 104       45.76     70.48
REMARK 500    ASN E 114      -22.39   -150.21
REMARK 500    PRO E 118      -20.40    -35.40
REMARK 500    LEU E 123        5.18    -55.12
REMARK 500    VAL E 124      -66.07    -90.05
REMARK 500    SER E 126      -21.65   -177.51
REMARK 500    ILE E 127       31.98   -147.71
REMARK 500    ARG E 169       49.20     33.43
REMARK 500    ALA F  73      135.76     56.02
REMARK 500    GLN F  78       -8.69     63.78
REMARK 500    MET F 103       38.75    -90.44
REMARK 500    LEU F 111       80.28    -62.09
REMARK 500    LEU H   5      -13.19   -169.69
REMARK 500    ASP H   7      128.60    173.46
REMARK 500    ASP H   8     -173.10   -172.56
REMARK 500    GLU H  14      131.98   -170.62
REMARK 500    ARG H  19      -45.66     95.98
REMARK 500    THR H  32     -104.55    123.09
REMARK 500    PHE H  47       80.55    177.43
REMARK 500    GLN H  52       -2.31     36.94
REMARK 500    ASP H  53      172.84    -38.19
REMARK 500    SER H  61      -14.11   -141.64
REMARK 500    SER H  62     -108.99   -146.69
REMARK 500    ARG H  77      147.51     58.81
REMARK 500    SER H  78     -158.04    -48.42
REMARK 500    PRO H  81     -122.30    -71.79
REMARK 500    PRO H  82     -131.43    -93.59
REMARK 500    GLN H  83      -71.76     68.63
REMARK 500    ASP H  86      -23.74   -173.08
REMARK 500    SER H  88       26.37    -72.71
REMARK 500    LEU H  89       74.21    -65.16
REMARK 500    ALA H  90       16.78    -57.84
REMARK 500    LYS H 103      -69.83     82.47
REMARK 500    PHE H 104       73.73      1.49
REMARK 500    GLU H 105       69.42    -18.98
REMARK 500    VAL H 107       80.70     34.91
REMARK 500    LYS H 109     -115.93     47.49
REMARK 500    TYR H 116      127.14     45.53
REMARK 500    ASN H 128      -15.59   -174.78
REMARK 500    LEU H 132       56.13    -67.80
REMARK 500    ASN H 133      -57.34   -148.42
REMARK 500    LEU H 135      104.61    -15.35
REMARK 500    LYS H 136       -3.58    -26.64
REMARK 500    GLU H 138      -91.57    -90.17
REMARK 500    ASN H 139       82.15     -2.48
REMARK 500    PHE I   4      106.65     18.66
REMARK 500    HIS I  79        3.16     50.36
REMARK 500    ASP I 113       98.95    -58.14
REMARK 500    LYS I 115       50.40    -98.15
REMARK 500    GLN I 120      -71.99   -108.60
REMARK 500    ASN K  29       50.06     72.62
REMARK 500    ASP K  39     -153.69   -141.95
REMARK 500    ALA K 100      -75.86    -44.55
REMARK 500    THR K 103      -70.33    -77.41
REMARK 500    LEU K 111       22.38    -46.85
REMARK 500    THR L  26     -169.94     61.72
REMARK 500    LEU L  27      -40.43   -152.90
REMARK 500    LYS L  28      -58.09     -0.13
REMARK 500    GLU L  33      -72.72    -63.15
REMARK 500    LEU L  38     -159.64   -102.59
REMARK 500    SER L  39      100.73    155.39
REMARK 500    SER L  41     -103.55   -143.56
REMARK 500    ALA L  45     -149.94    109.52
REMARK 500    VAL L  46       35.05   -159.28
REMARK 500    ARG L  47     -135.84   -118.32
REMARK 500    LYS L  49       70.59   -162.83
REMARK 500    ASP L  50       -2.08    131.14
REMARK 500    LYS L  58      -30.18    -33.44
REMARK 500    ALA L  59      128.62     80.85
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500                                 MODEL     OMEGA
REMARK 500 THR A   44     GLN A   45                 -125.28
REMARK 500 GLY A   52     LEU A   53                  144.37
REMARK 500 SER A   60     ILE A   61                  148.87
REMARK 500 LEU A   65     LYS A   66                 -148.99
REMARK 500 MET A   74     ASN A   75                 -142.46
REMARK 500 GLU A  120     LEU A  121                  146.20
REMARK 500 ILE A  128     LYS A  129                 -143.56
REMARK 500 THR A  150     ASP A  151                 -147.98
REMARK 500 PRO A  158     THR A  159                  133.57
REMARK 500 THR A  159     GLN A  160                 -148.04
REMARK 500 GLY A  165     GLY A  166                  141.44
REMARK 500 THR A  191     GLY A  192                  131.42
REMARK 500 ALA A  194     ASP A  195                  147.04
REMARK 500 ASP A  261     LEU A  262                  146.66
REMARK 500 ILE A  325     ARG A  326                  146.90
REMARK 500 HIS A  399     PRO A  400                  -52.66
REMARK 500 PRO A  464     TYR A  465                 -123.06
REMARK 500 ASP A  555     TRP A  556                  136.74
REMARK 500 TRP A  556     ASP A  557                  143.21
REMARK 500 LYS A  705     HIS A  706                  145.37
REMARK 500 HIS A  706     GLY A  707                 -137.50
REMARK 500 LYS A 1093     VAL A 1094                  139.27
REMARK 500 GLY A 1123     HIS A 1124                 -142.22
REMARK 500 SER A 1160     THR A 1161                 -147.66
REMARK 500 PHE A 1220     LYS A 1221                  149.41
REMARK 500 ASN A 1232     ASP A 1233                 -139.57
REMARK 500 TYR A 1365     ARG A 1366                 -149.97
REMARK 500 VAL A 1384     THR A 1385                  140.31
REMARK 500 CYS B   64     GLU B   65                  146.72
REMARK 500 GLU B  104     SER B  105                  144.82
REMARK 500 GLY B  107     VAL B  108                  146.99
REMARK 500 THR B  109     HIS B  110                 -145.49
REMARK 500 LYS B  133     LYS B  134                  145.92
REMARK 500 TYR B  180     LEU B  181                 -143.43
REMARK 500 SER B  248     ARG B  249                  142.71
REMARK 500 GLY B  369     PHE B  370                 -138.93
REMARK 500 TYR B  431     MET B  432                 -149.65
REMARK 500 PRO B  501     ILE B  502                  145.54
REMARK 500 ASP B  642     ASP B  643                   31.07
REMARK 500 ASP B  643     GLU B  644                 -119.37
REMARK 500 GLU B  644     SER B  645                   98.59
REMARK 500 SER B  732     HIS B  733                  122.43
REMARK 500 MET B  860     ASP B  861                  145.85
REMARK 500 THR B  882     LEU B  883                  137.10
REMARK 500 THR B  915     THR B  916                  146.45
REMARK 500 ASP B 1101     LYS B 1102                 -129.73
REMARK 500 ARG B 1108     GLY B 1109                  141.65
REMARK 500 GLY B 1109     PRO B 1110                  143.89
REMARK 500 MET B 1152     GLU B 1153                  143.88
REMARK 500 GLU B 1153     ALA B 1154                  144.42
REMARK 500 ALA B 1157     PHE B 1158                  137.54
REMARK 500 GLU B 1181     CYS B 1182                  149.27
REMARK 500 SER B 1221     ARG B 1222                  136.04
REMARK 500 ARG B 1222     ASP B 1223                  136.28
REMARK 500 GLU C    4     GLY C    5                 -134.26
REMARK 500 SER C   96     VAL C   97                  145.86
REMARK 500 ASN C  140     GLY C  141                 -145.34
REMARK 500 ASN C  184     LYS C  185                 -129.46
REMARK 500 ASP C  190     TYR C  191                 -146.81
REMARK 500 ASN C  214     GLU C  215                 -141.62
REMARK 500 ALA C  261     LEU C  262                  136.26
REMARK 500 GLN C  267     ASP C  268                  125.44
REMARK 500 LYS E   56     MET E   57                 -146.66
REMARK 500 SER E   77     LEU E   78                 -145.34
REMARK 500 SER E  119     ALA E  120                  149.96
REMARK 500 PRO E  125     SER E  126                 -146.34
REMARK 500 LEU E  170     LYS E  171                  147.42
REMARK 500 ASN H    3     THR H    4                  148.70
REMARK 500 PRO H   17     GLY H   18                 -145.96
REMARK 500 ALA H   29     SER H   30                  149.78
REMARK 500 SER H   54     LEU H   55                 -147.03
REMARK 500 SER H   61     SER H   62                  137.17
REMARK 500 SER H   62     LEU H   63                 -131.26
REMARK 500 ASP H   86     ARG H   87                  147.02
REMARK 500 ARG H   87     SER H   88                 -136.41
REMARK 500 SER H   88     LEU H   89                 -149.99
REMARK 500 TYR H  102     LYS H  103                  135.16
REMARK 500 LYS H  103     PHE H  104                 -130.57
REMARK 500 GLY H  127     ASN H  128                  145.48
REMARK 500 ASN H  131     LEU H  132                  145.94
REMARK 500 LEU H  135     LYS H  136                  145.82
REMARK 500 LYS H  136     GLN H  137                 -141.08
REMARK 500 THR I    3     PHE I    4                  127.71
REMARK 500 THR I  111     SER I  112                  148.67
REMARK 500 LEU K  111     GLN K  112                 -147.25
REMARK 500 LEU L   27     LYS L   28                 -146.10
REMARK 500 SER L   35     SER L   36                 -139.65
REMARK 500 LYS L   49     ASP L   50                  146.61
REMARK 500 ALA L   59     ARG L   60                 -143.60
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    ARG A 434         0.10    SIDE_CHAIN
REMARK 500    TYR A 478         0.06    SIDE_CHAIN
REMARK 500    GLN A 650         0.07    SIDE_CHAIN
REMARK 500    HIS A 659         0.14    SIDE_CHAIN
REMARK 500    TYR A 852         0.06    SIDE_CHAIN
REMARK 500    TYR A 897         0.08    SIDE_CHAIN
REMARK 500    TYR A1035         0.07    SIDE_CHAIN
REMARK 500    TYR A1119         0.09    SIDE_CHAIN
REMARK 500    ASN A1278         0.08    SIDE_CHAIN
REMARK 500    TYR A1298         0.07    SIDE_CHAIN
REMARK 500    TYR A1328         0.09    SIDE_CHAIN
REMARK 500    ARG A1366         0.09    SIDE_CHAIN
REMARK 500    TYR B 124         0.08    SIDE_CHAIN
REMARK 500    TYR B 202         0.07    SIDE_CHAIN
REMARK 500    PHE B 203         0.08    SIDE_CHAIN
REMARK 500    TYR B 259         0.07    SIDE_CHAIN
REMARK 500    TYR B 351         0.08    SIDE_CHAIN
REMARK 500    HIS B 518         0.13    SIDE_CHAIN
REMARK 500    PHE B 627         0.08    SIDE_CHAIN
REMARK 500    HIS B 648         0.07    SIDE_CHAIN
REMARK 500    TYR B 692         0.09    SIDE_CHAIN
REMARK 500    TYR B 769         0.10    SIDE_CHAIN
REMARK 500    PHE B 851         0.09    SIDE_CHAIN
REMARK 500    HIS B 984         0.12    SIDE_CHAIN
REMARK 500    ARG B1020         0.06    SIDE_CHAIN
REMARK 500    HIS B1025         0.14    SIDE_CHAIN
REMARK 500    HIS B1062         0.11    SIDE_CHAIN
REMARK 500    HIS B1097         0.14    SIDE_CHAIN
REMARK 500    HIS B1141         0.09    SIDE_CHAIN
REMARK 500    TYR B1198         0.07    SIDE_CHAIN
REMARK 500    TYR B1217         0.08    SIDE_CHAIN
REMARK 500    PHE C  20         0.08    SIDE_CHAIN
REMARK 500    ARG C  34         0.07    SIDE_CHAIN
REMARK 500    PHE C  62         0.07    SIDE_CHAIN
REMARK 500    GLU C 200         0.08    SIDE_CHAIN
REMARK 500    PHE E 135         0.10    SIDE_CHAIN
REMARK 500    HIS E 147         0.10    SIDE_CHAIN
REMARK 500    ARG E 212         0.16    SIDE_CHAIN
REMARK 500    TYR I  15         0.11    SIDE_CHAIN
REMARK 500    ARG I  45         0.10    SIDE_CHAIN
REMARK 500    PHE K  58         0.08    SIDE_CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500  M RES CSSEQI        ANGLE
REMARK 500    PRO A  78        -10.58
REMARK 500    PRO A 158        -11.45
REMARK 500    THR A 159         12.13
REMARK 500    PRO A 377        -12.97
REMARK 500    HIS A 399        -12.59
REMARK 500    PRO A 441        -10.68
REMARK 500    PRO A 464         15.53
REMARK 500    GLY A 484         11.63
REMARK 500    LEU A 504         10.54
REMARK 500    ARG A 537        -12.55
REMARK 500    GLN A 545        -10.79
REMARK 500    ASN A 741         13.46
REMARK 500    GLU A 870        -11.55
REMARK 500    ASP A 884        -11.10
REMARK 500    ASP A 900         11.05
REMARK 500    THR A 907        -10.65
REMARK 500    LEU A 936        -11.76
REMARK 500    ALA A 952         11.57
REMARK 500    ASN A 966         10.11
REMARK 500    ASP A 992         11.61
REMARK 500    LEU A 998        -11.87
REMARK 500    LEU A1046         12.70
REMARK 500    MET A1111        -11.92
REMARK 500    THR A1117         10.87
REMARK 500    THR A1208        -11.02
REMARK 500    GLU A1301        -14.46
REMARK 500    LEU A1306        -10.51
REMARK 500    SER A1361         11.23
REMARK 500    MET A1375        -10.91
REMARK 500    ALA B  23        -11.96
REMARK 500    ALA B 238        -14.37
REMARK 500    LEU B 408        -10.82
REMARK 500    SER B 546        -12.38
REMARK 500    ILE B 616        -10.71
REMARK 500    ARG B 620         10.36
REMARK 500    ALA B 808        -11.64
REMARK 500    GLY B 849         11.11
REMARK 500    ARG B 967        -10.20
REMARK 500    GLN B 975        -16.05
REMARK 500    ILE B 990        -10.60
REMARK 500    HIS B1062        -10.03
REMARK 500    PHE B1086         10.25
REMARK 500    CYS B1166         11.30
REMARK 500    ARG C 127         10.10
REMARK 500    THR C 156        -11.24
REMARK 500    ILE C 163         10.73
REMARK 500    GLY C 171         10.89
REMARK 500    LEU C 186         10.35
REMARK 500    THR C 227        -11.40
REMARK 500    VAL C 240         12.57
REMARK 500    GLN E  61        -10.89
REMARK 500    SER I  33        -10.55
REMARK 500    GLY I  39        -12.73
REMARK 500    VAL I  43         10.14
REMARK 500    VAL I  84         11.71
REMARK 500    PHE I 100         10.03
REMARK 500    SER J   9         10.46
REMARK 500    MET J  49        -11.40
REMARK 500    HIS K  40         11.17
REMARK 500    ARG K  70         12.55
REMARK 500    PHE K  71         10.11
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 A3006  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 167   SG
REMARK 620 2 CYS A 110   SG   92.5
REMARK 620 3 CYS A 107   SG  101.7  84.2
REMARK 620 4 CYS A 148   SG  100.4 132.2 135.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A3008  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A  80   NE2
REMARK 620 2 CYS A  70   SG   82.3
REMARK 620 3 CYS A  77   SG  112.9 164.4
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B3007  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1185   SG
REMARK 620 2 CYS B1163   SG   99.0
REMARK 620 3 CYS B1166   SG  105.5  98.1
REMARK 620 4 CYS B1182   SG  153.4 104.4  83.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN C3002  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C  86   SG
REMARK 620 2 CYS C  88   SG  127.5
REMARK 620 3 CYS C  92   SG  117.3 106.9
REMARK 620 4 CYS C  95   SG  103.4  94.2 101.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN I3003  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I  32   SG
REMARK 620 2 CYS I  29   SG  129.3
REMARK 620 3 CYS I   7   SG   97.3 126.8
REMARK 620 4 CYS I  10   SG   95.5 107.7  88.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN I3004  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I  75   SG
REMARK 620 2 CYS I 106   SG  165.5
REMARK 620 3 CYS I  78   SG   95.3  74.1
REMARK 620 4 CYS I 103   SG   91.3  74.4  52.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN L3005  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L  48   SG
REMARK 620 2 CYS L  31   SG   85.0
REMARK 620 3 CYS L  51   SG  107.3  94.2
REMARK 620 4 CYS L  34   SG  141.0  90.2 111.6
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN J3001  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J  45   SG
REMARK 620 2 CYS J   7   SG  125.2
REMARK 620 3 CYS J  10   SG  118.4 102.7
REMARK 620 4 CYS J  46   SG  116.2  98.6  88.2
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A3009  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 483   OD2
REMARK 620 2 ASP A 485   OD2  77.9
REMARK 620 3 CTP B3008   O2G 107.2 109.4
REMARK 620 4 ASP A 481   OD1  70.5  72.4 176.9
REMARK 620 5 CTP B3008   O1B  90.7 167.6  78.4  99.4
REMARK 620 N                    1     2     3     4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MN A3010  MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CTP B3008   O1B
REMARK 620 2 ASP A 481   OD2  92.7
REMARK 620 3 ASP B 837   OD2 176.7  84.0
REMARK 620 4 ASP A 483   OD1  72.4  91.0 107.0
REMARK 620 N                    1     2     3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 3009
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 3010
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 3001
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 3002
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 3003
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 3004
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 3005
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3006
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 3007
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 3008
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CTP B 3008
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TWA   RELATED DB: PDB
REMARK 900 RELATED ID: 1TWC   RELATED DB: PDB
REMARK 900 RELATED ID: 1TWF   RELATED DB: PDB
REMARK 900 RELATED ID: 1TWH   RELATED DB: PDB
DBREF  1TWG A    1  1733  UNP    P04050   RPB1_YEAST       1   1733
DBREF  1TWG B    1  1224  UNP    P08518   RPB2_YEAST       1   1224
DBREF  1TWG C    1   318  UNP    P16370   RPB3_YEAST       1    318
DBREF  1TWG E    1   215  UNP    P20434   RPB5_YEAST       1    215
DBREF  1TWG F    1   155  UNP    P20435   RPB6_YEAST       1    155
DBREF  1TWG H    1   146  UNP    P20436   RPB8_YEAST       1    146
DBREF  1TWG I    1   122  UNP    P27999   RPB9_YEAST       1    122
DBREF  1TWG J    1    70  UNP    P22139   RPB10_YEAST      1     70
DBREF  1TWG K    1   120  UNP    P38902   RPB11_YEAST      1    120
DBREF  1TWG L    1    70  UNP    P40422   RPC10_YEAST      1     70
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  318  MET SER GLU GLU GLY PRO GLN VAL LYS ILE ARG GLU ALA
SEQRES   2 C  318  SER LYS ASP ASN VAL ASP PHE ILE LEU SER ASN VAL ASP
SEQRES   3 C  318  LEU ALA MET ALA ASN SER LEU ARG ARG VAL MET ILE ALA
SEQRES   4 C  318  GLU ILE PRO THR LEU ALA ILE ASP SER VAL GLU VAL GLU
SEQRES   5 C  318  THR ASN THR THR VAL LEU ALA ASP GLU PHE ILE ALA HIS
SEQRES   6 C  318  ARG LEU GLY LEU ILE PRO LEU GLN SER MET ASP ILE GLU
SEQRES   7 C  318  GLN LEU GLU TYR SER ARG ASP CYS PHE CYS GLU ASP HIS
SEQRES   8 C  318  CYS ASP LYS CYS SER VAL VAL LEU THR LEU GLN ALA PHE
SEQRES   9 C  318  GLY GLU SER GLU SER THR THR ASN VAL TYR SER LYS ASP
SEQRES  10 C  318  LEU VAL ILE VAL SER ASN LEU MET GLY ARG ASN ILE GLY
SEQRES  11 C  318  HIS PRO ILE ILE GLN ASP LYS GLU GLY ASN GLY VAL LEU
SEQRES  12 C  318  ILE CYS LYS LEU ARG LYS GLY GLN GLU LEU LYS LEU THR
SEQRES  13 C  318  CYS VAL ALA LYS LYS GLY ILE ALA LYS GLU HIS ALA LYS
SEQRES  14 C  318  TRP GLY PRO ALA ALA ALA ILE GLU PHE GLU TYR ASP PRO
SEQRES  15 C  318  TRP ASN LYS LEU LYS HIS THR ASP TYR TRP TYR GLU GLN
SEQRES  16 C  318  ASP SER ALA LYS GLU TRP PRO GLN SER LYS ASN CYS GLU
SEQRES  17 C  318  TYR GLU ASP PRO PRO ASN GLU GLY ASP PRO PHE ASP TYR
SEQRES  18 C  318  LYS ALA GLN ALA ASP THR PHE TYR MET ASN VAL GLU SER
SEQRES  19 C  318  VAL GLY SER ILE PRO VAL ASP GLN VAL VAL VAL ARG GLY
SEQRES  20 C  318  ILE ASP THR LEU GLN LYS LYS VAL ALA SER ILE LEU LEU
SEQRES  21 C  318  ALA LEU THR GLN MET ASP GLN ASP LYS VAL ASN PHE ALA
SEQRES  22 C  318  SER GLY ASP ASN ASN THR ALA SER ASN MET LEU GLY SER
SEQRES  23 C  318  ASN GLU ASP VAL MET MET THR GLY ALA GLU GLN ASP PRO
SEQRES  24 C  318  TYR SER ASN ALA SER GLN MET GLY ASN THR GLY SER GLY
SEQRES  25 C  318  GLY TYR ASP ASN ALA TRP
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 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
HET     MN  A3009       1
HET     MN  A3010       1
HET     ZN  J3001       1
HET     ZN  C3002       1
HET     ZN  I3003       1
HET     ZN  I3004       1
HET     ZN  L3005       1
HET     ZN  A3006       1
HET     ZN  B3007       1
HET     ZN  A3008       1
HET    CTP  B3008      29
HETNAM      MN MANGANESE (II) ION
HETNAM      ZN ZINC ION
HETNAM     CTP CYTIDINE-5'-TRIPHOSPHATE
FORMUL  11   MN    2(MN 2+)
FORMUL  13   ZN    8(ZN 2+)
FORMUL  21  CTP    C9 H16 N3 O14 P3
FORMUL  22  HOH   *5(H2 O)
HELIX    1   1 SER A   23  ILE A   30  1                                   8
HELIX    2   2 PHE A   95  GLU A  104  1                                  10
HELIX    3   3 GLU A  120  ALA A  127  1                                   8
HELIX    4   4 ASP A  130  LYS A  143  1                                  14
HELIX    5   5 SER A  203  HIS A  213  1                                  11
HELIX    6   6 SER A  215  SER A  221  1                                   7
HELIX    7   7 ARG A  230  TRP A  233  5                                   4
HELIX    8   8 LEU A  262  HIS A  281  1                                  20
HELIX    9   9 PRO A  285  ASP A  305  1                                  21
HELIX   10  10 SER A  324  ARG A  326  1                                   3
HELIX   11  11 LYS A  368  LYS A  372  1                                   5
HELIX   12  12 ASN A  384  GLY A  395  1                                  12
HELIX   13  13 HIS A  451  MET A  453  5                                   3
HELIX   14  14 VAL A  474  ASN A  479  1                                   6
HELIX   15  15 SER A  494  CYS A  505  1                                  12
HELIX   16  16 ALA A  506  GLN A  510  5                                   5
HELIX   17  17 VAL A  524  THR A  535  1                                  12
HELIX   18  18 LEU A  543  VAL A  553  1                                  11
HELIX   19  19 GLY A  574  SER A  579  1                                   6
HELIX   20  20 GLU A  618  GLY A  623  1                                   6
HELIX   21  21 GLY A  628  GLY A  638  1                                  11
HELIX   22  22 GLY A  638  GLY A  661  1                                  24
HELIX   23  23 GLY A  665  ILE A  670  5                                   6
HELIX   24  24 ASP A  672  ASN A  700  1                                  29
HELIX   25  25 THR A  709  ASN A  736  1                                  28
HELIX   26  26 ASN A  741  GLY A  750  1                                  10
HELIX   27  27 SER A  754  ALA A  763  1                                  10
HELIX   28  28 THR A  809  GLU A  846  1                                  38
HELIX   29  29 ILE A  867  ASP A  871  5                                   5
HELIX   30  30 ASP A  874  ILE A  878  5                                   5
HELIX   31  31 ASP A  884  GLY A  887  5                                   4
HELIX   32  32 SER A  889  ARG A  898  1                                  10
HELIX   33  33 LEU A  913  SER A  917  5                                   5
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 THR A  982  GLU A  995  1                                  14
HELIX   37  37 ASN A 1004  VAL A 1015  1                                  12
HELIX   38  38 VAL A 1015  LEU A 1026  1                                  12
HELIX   39  39 ALA A 1027  GLU A 1034  1                                   8
HELIX   40  40 THR A 1038  SER A 1056  1                                  19
HELIX   41  41 MET A 1063  GLN A 1078  1                                  16
HELIX   42  42 SER A 1096  VAL A 1107  1                                  12
HELIX   43  43 ASP A 1127  GLU A 1139  1                                  13
HELIX   44  44 THR A 1142  VAL A 1146  1                                   5
HELIX   45  45 ILE A 1163  GLU A 1165  5                                   3
HELIX   46  46 ASP A 1166  LEU A 1172  1                                   7
HELIX   47  47 ASP A 1198  ASP A 1204  1                                   7
HELIX   48  48 THR A 1208  LYS A 1221  1                                  14
HELIX   49  49 GLU A 1230  GLU A 1234  5                                   5
HELIX   50  50 ASP A 1257  ASN A 1270  1                                  14
HELIX   51  51 ASN A 1312  MET A 1317  1                                   6
HELIX   52  52 SER A 1331  GLY A 1340  1                                  10
HELIX   53  53 GLY A 1340  ASP A 1359  1                                  20
HELIX   54  54 ASN A 1364  THR A 1377  1                                  14
HELIX   55  55 THR A 1405  ALA A 1416  1                                  12
HELIX   56  56 GLY A 1423  LEU A 1430  1                                   8
HELIX   57  57 ILE A 1436  ALA A 1440  5                                   5
HELIX   58  58 THR B   26  GLU B   28  5                                   3
HELIX   59  59 ASP B   29  GLY B   42  1                                  14
HELIX   60  60 VAL B   44  TYR B   57  1                                  14
HELIX   61  61 TYR B   57  GLU B   65  1                                   9
HELIX   62  62 TYR B  113  ARG B  120  1                                   8
HELIX   63  63 THR B  185  LEU B  192  1                                   8
HELIX   64  64 ILE B  282  LEU B  289  1                                   8
HELIX   65  65 PRO B  293  CYS B  302  1                                  10
HELIX   66  66 ASP B  307  GLY B  321  1                                  15
HELIX   67  67 ASP B  326  ARG B  336  1                                  11
HELIX   68  68 LYS B  344  GLU B  359  1                                  16
HELIX   69  69 PHE B  370  LEU B  390  1                                  21
HELIX   70  70 HIS B  400  GLY B  402  5                                   3
HELIX   71  71 LEU B  408  THR B  425  1                                  18
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 HIS B  515  TRP B  519  5                                   5
HELIX   75  75 PRO B  551  TRP B  561  1                                  11
HELIX   76  76 GLU B  567  TYR B  569  5                                   3
HELIX   77  77 VAL B  570  SER B  574  5                                   5
HELIX   78  78 ASN B  592  LYS B  606  1                                  15
HELIX   79  79 ARG B  654  GLN B  667  1                                  14
HELIX   80  80 THR B  680  GLU B  687  1                                   8
HELIX   81  81 GLU B  696  ILE B  701  5                                   6
HELIX   82  82 GLN B  706  LEU B  710  5                                   5
HELIX   83  83 HIS B  744  LEU B  749  5                                   6
HELIX   84  84 ALA B  752  ILE B  756  5                                   5
HELIX   85  85 PHE B  758  ASN B  762  5                                   5
HELIX   86  86 GLN B  763  GLY B  774  1                                  12
HELIX   87  87 LYS B  775  ALA B  777  5                                   3
HELIX   88  88 ASN B  784  ARG B  788  5                                   5
HELIX   89  89 ALA B  808  LYS B  813  1                                   6
HELIX   90  90 GLN B  843  ARG B  848  1                                   6
HELIX   91  91 THR B  889  LEU B  893  5                                   5
HELIX   92  92 ARG B  995  MET B  999  5                                   5
HELIX   93  93 ASN B 1013  ILE B 1017  5                                   5
HELIX   94  94 THR B 1022  GLY B 1039  1                                  18
HELIX   95  95 THR B 1051  HIS B 1062  1                                  12
HELIX   96  96 MET B 1098  ILE B 1103  1                                   6
HELIX   97  97 GLY B 1131  GLY B 1142  1                                  12
HELIX   98  98 ALA B 1143  LEU B 1151  1                                   9
HELIX   99  99 TYR B 1198  MET B 1210  1                                  13
HELIX  100 100 ASP C   26  GLU C   40  1                                  15
HELIX  101 101 ALA C   59  ILE C   70  1                                  12
HELIX  102 102 ASP C   76  LEU C   80  5                                   5
HELIX  103 103 TYR C  114  LYS C  116  5                                   3
HELIX  104 104 HIS C  167  GLY C  171  5                                   5
HELIX  105 105 ASP C  196  TRP C  201  1                                   6
HELIX  106 106 SER C  204  GLU C  208  5                                   5
HELIX  107 107 VAL C  240  GLN C  264  1                                  25
HELIX  108 108 GLU E    4  GLY E   27  1                                  24
HELIX  109 109 THR E   31  GLU E   36  1                                   6
HELIX  110 110 PRO E   38  TYR E   46  1                                   9
HELIX  111 111 GLN E   54  SER E   59  1                                   6
HELIX  112 112 THR E   65  PHE E   72  1                                   8
HELIX  113 113 GLY E   89  LYS E  103  1                                  15
HELIX  114 114 ALA E  138  VAL E  141  5                                   4
HELIX  115 115 ASN E  143  HIS E  147  5                                   5
HELIX  116 116 SER E  157  TYR E  168  1                                  12
HELIX  117 117 LYS E  171  LEU E  175  5                                   5
HELIX  118 118 ASP E  182  LEU E  188  1                                   7
HELIX  119 119 THR F   86  MET F  103  1                                  18
HELIX  120 120 ASP F  116  LYS F  128  1                                  13
HELIX  121 121 ASP I   61  ASP I   65  5                                   5
HELIX  122 122 LYS J   17  GLU J   27  1                                  11
HELIX  123 123 ASP J   31  LEU J   39  1                                   9
HELIX  124 124 ARG J   43  THR J   52  1                                  10
HELIX  125 125 LEU J   56  LEU J   61  1                                   6
HELIX  126 126 ASP K    5  PHE K   10  5                                   6
HELIX  127 127 ASP K   39  LEU K   51  1                                  13
HELIX  128 128 ASP K   82  TRP K  109  1                                  28
SHEET    1   A 3 LEU A1418  ASP A1419  0
SHEET    2   A 3 GLU A  16  LEU A  21 -1  N  VAL A  17   O  ASP A1419
SHEET    3   A 3 ILE B1212  TYR B1217 -1  O  TYR B1217   N  GLU A  16
SHEET    1   B 2 GLY A  82  PHE A  91  0
SHEET    2   B 2 ILE A 235  VAL A 241 -1  O  VAL A 241   N  GLY A  82
SHEET    1   C 2 ASP A 151  PRO A 153  0
SHEET    2   C 2 LEU A 161  SER A 163 -1  O  VAL A 162   N  VAL A 152
SHEET    1   D 3 THR A 173  LYS A 176  0
SHEET    2   D 3 LEU A 181  TRP A 185 -1  O  VAL A 182   N  ARG A 175
SHEET    3   D 3 GLU A 198  LEU A 202 -1  O  LEU A 202   N  LEU A 181
SHEET    1   E 7 SER A 348  GLY A 355  0
SHEET    2   E 7 PHE A 468  LEU A 470  1  O  LEU A 470   N  SER A 354
SHEET    3   E 7 GLN A 363  PRO A 367 -1  N  GLY A 365   O  ARG A 469
SHEET    4   E 7 MET A 455  ILE A 463  1  O  LYS A 461   N  VAL A 366
SHEET    5   E 7 PRO A 441  ASN A 445 -1  N  VAL A 442   O  HIS A 458
SHEET    6   E 7 GLU A 486  HIS A 490 -1  O  HIS A 490   N  LEU A 443
SHEET    7   E 7 SER A 348  GLY A 355 -1  N  ALA A 349   O  LEU A 489
SHEET    1   F 4 THR A 375  VAL A 379  0
SHEET    2   F 4 LYS A 431  HIS A 435 -1  O  VAL A 432   N  GLU A 378
SHEET    3   F 4 ALA A 402  ILE A 406 -1  N  ILE A 406   O  LYS A 431
SHEET    4   F 4 ARG A 412  ASP A 414 -1  O  ILE A 413   N  VAL A 405
SHEET    1   G 2 VAL A 512  SER A 513  0
SHEET    2   G 2 LYS A 518  PRO A 519 -1  O  LYS A 518   N  SER A 513
SHEET    1   H 2 PHE A 540  GLU A 542  0
SHEET    2   H 2 LEU A 571  SER A 573 -1  O  TRP A 572   N  ILE A 541
SHEET    1   I 3 LEU A 588  ARG A 590  0
SHEET    2   I 3 MET A 605  ILE A 608 -1  O  ILE A 607   N  LEU A 588
SHEET    3   I 3 GLN A 611  PHE A 614 -1  O  PHE A 614   N  LEU A 606
SHEET    1   J 2 GLY A 766  GLN A 767  0
SHEET    2   J 2 PHE A 799  VAL A 800 -1  O  VAL A 800   N  GLY A 766
SHEET    1   K 3 MET A 849  VAL A 850  0
SHEET    2   K 3 THR A 856  ARG A 857 -1  O  ARG A 857   N  MET A 849
SHEET    3   K 3 VAL A 863  GLN A 865 -1  O  GLN A 865   N  THR A 856
SHEET    1   L 2 GLU A 879  SER A 882  0
SHEET    2   L 2 ASN A 953  LEU A 956 -1  O  LEU A 956   N  GLU A 879
SHEET    1   M 4 VAL A1282  TYR A1287  0
SHEET    2   M 4 GLU A1303  THR A1308 -1  O  GLU A1303   N  TYR A1287
SHEET    3   M 4 LEU A1116  TYR A1119 -1  N  VAL A1118   O  LEU A1306
SHEET    4   M 4 TYR A1328  THR A1329 -1  O  TYR A1328   N  THR A1117
SHEET    1   N 5 LEU A1224  TRP A1228  0
SHEET    2   N 5 LEU A1236  VAL A1242 -1  O  ARG A1241   N  PHE A1225
SHEET    3   N 5 TRP A1191  LEU A1197 -1  N  LEU A1193   O  CYS A1240
SHEET    4   N 5 THR A1147  TYR A1154 -1  N  TYR A1153   O  LEU A1192
SHEET    5   N 5 LEU I  42  GLU I  47 -1  O  TYR I  44   N  ILE A1152
SHEET    1   O 2 LYS A1290  PRO A1292  0
SHEET    2   O 2 TYR A1298  LYS A1300 -1  O  VAL A1299   N  VAL A1291
SHEET    1   P 3 ASP A1442  ILE A1445  0
SHEET    2   P 3 LEU F 132  TYR F 137 -1  O  ARG F 135   N  ASP A1442
SHEET    3   P 3 PHE F 143  SER F 147 -1  O  TRP F 146   N  ILE F 134
SHEET    1   Q 4 HIS B 110  ALA B 111  0
SHEET    2   Q 4 TYR B  96  VAL B 102 -1  N  VAL B 102   O  HIS B 110
SHEET    3   Q 4 SER B 125  PHE B 129 -1  O  SER B 125   N  MET B 101
SHEET    4   Q 4 PHE B 166  PRO B 171 -1  O  LEU B 170   N  SER B 126
SHEET    1   R 3 PHE B 203  ILE B 205  0
SHEET    2   R 3 SER B 208  LEU B 212 -1  O  LYS B 210   N  PHE B 203
SHEET    3   R 3 SER B 480  VAL B 482 -1  O  GLN B 481   N  VAL B 211
SHEET    1   S 4 LYS B 404  ASP B 407  0
SHEET    2   S 4 ALA B 214  SER B 218 -1  N  GLN B 215   O  ASP B 407
SHEET    3   S 4 ARG B 497  ASN B 499  1  O  ASN B 499   N  ALA B 214
SHEET    4   S 4 VAL B 536  ASN B 538 -1  O  LYS B 537   N  THR B 498
SHEET    1   T 5 GLN B 224  LYS B 227  0
SHEET    2   T 5 ILE B 234  ARG B 241 -1  O  VAL B 237   N  PHE B 226
SHEET    3   T 5 THR B 253  TYR B 259 -1  O  LEU B 258   N  SER B 235
SHEET    4   T 5 ILE B 269  THR B 272 -1  O  LYS B 270   N  LYS B 257
SHEET    5   T 5 ILE B 280  PRO B 281 -1  O  ILE B 280   N  ALA B 271
SHEET    1   U 3 CYS B 544  ILE B 545  0
SHEET    2   U 3 VAL B 633  GLU B 641 -1  O  TYR B 634   N  CYS B 544
SHEET    3   U 3 VAL B 690  ASP B 694 -1  O  ILE B 693   N  ARG B 635
SHEET    1   V 4 GLU B 650  LEU B 651  0
SHEET    2   V 4 VAL B 633  GLU B 641 -1  N  GLU B 641   O  GLU B 650
SHEET    3   V 4 HIS B 740  CYS B 741 -1  O  CYS B 741   N  PHE B 638
SHEET    4   V 4 ILE B 703  ALA B 704  1  N  ALA B 704   O  HIS B 740
SHEET    1   W 5 GLU B 564  PRO B 565  0
SHEET    2   W 5 VAL B 585  HIS B 590 -1  O  VAL B 589   N  GLU B 564
SHEET    3   W 5 THR B 578  VAL B 582 -1  N  VAL B 580   O  GLY B 588
SHEET    4   W 5 GLU B 623  PHE B 627  1  O  ILE B 626   N  PHE B 581
SHEET    5   W 5 SER B 614  ASP B 618 -1  N  ASP B 618   O  GLU B 623
SHEET    1   X 5 MET B 792  LEU B 796  0
SHEET    2   X 5 SER B 853  ASP B 861 -1  O  LEU B 854   N  ILE B 795
SHEET    3   X 5 LYS B 962  LYS B 972 -1  O  THR B 970   N  PHE B 855
SHEET    4   X 5 GLY B 947  THR B 956 -1  N  LEU B 953   O  LYS B 965
SHEET    5   X 5 ARG B 904  VAL B 905 -1  N  VAL B 905   O  GLY B 947
SHEET    1   Y 5 MET B 792  LEU B 796  0
SHEET    2   Y 5 SER B 853  ASP B 861 -1  O  LEU B 854   N  ILE B 795
SHEET    3   Y 5 LYS B 962  LYS B 972 -1  O  THR B 970   N  PHE B 855
SHEET    4   Y 5 GLY B 947  THR B 956 -1  N  LEU B 953   O  LYS B 965
SHEET    5   Y 5 ILE L  55  LEU L  57 -1  O  LEU L  56   N  VAL B 954
SHEET    1   Z 2 GLY B 804  THR B 805  0
SHEET    2   Z 2 GLY B1042  ASP B1043  1  O  GLY B1042   N  THR B 805
SHEET    1  AA 7 GLN B 821  ILE B 827  0
SHEET    2  AA 7 LEU B1010  ILE B1012  1  O  LEU B1010   N  ALA B 826
SHEET    3  AA 7 SER B 838  ASN B 842 -1  N  ILE B 840   O  ILE B1011
SHEET    4  AA 7 LYS B 987  TYR B 994  1  O  GLY B 991   N  MET B 839
SHEET    5  AA 7 LYS B 979  ALA B 981 -1  N  PHE B 980   O  GLY B 988
SHEET    6  AA 7 PHE B1086  ARG B1094 -1  O  GLN B1093   N  ALA B 981
SHEET    7  AA 7 GLN B 821  ILE B 827 -1  N  VAL B 825   O  GLY B1088
SHEET    1  AB 2 VAL B 910  ILE B 912  0
SHEET    2  AB 2 THR B 939  PRO B 940 -1  O  THR B 939   N  ILE B 911
SHEET    1  AC 2 PHE B1001  THR B1002  0
SHEET    2  AC 2 MET B1072  TYR B1073 -1  O  TYR B1073   N  PHE B1001
SHEET    1  AD 2 ALA B1157  CYS B1163  0
SHEET    2  AD 2 ILE B1191  PRO B1197 -1  O  ILE B1196   N  PHE B1158
SHEET    1  AE 2 ILE B1172  LYS B1174  0
SHEET    2  AE 2 GLN B1179  GLU B1181 -1  O  GLN B1179   N  LYS B1174
SHEET    1  AF 4 GLU C  12  ALA C  13  0
SHEET    2  AF 4 ASN C  17  ASP C  19 -1  O  ASP C  19   N  GLU C  12
SHEET    3  AF 4 ASN C 231  SER C 234 -1  O  VAL C 232   N  VAL C  18
SHEET    4  AF 4 ALA C 173  GLU C 177 -1  N  ALA C 174   O  GLU C 233
SHEET    1  AG 5 LEU C 118  ILE C 120  0
SHEET    2  AG 5 VAL C  98  PHE C 104 -1  N  THR C 100   O  VAL C 119
SHEET    3  AG 5 GLU C 152  GLY C 162 -1  O  CYS C 157   N  LEU C  99
SHEET    4  AG 5 THR C  43  ASN C  54 -1  N  THR C  53   O  LYS C 154
SHEET    5  AG 5 VAL L  65  PHE L  67 -1  O  VAL L  65   N  VAL C  51
SHEET    1  AH 2 THR C 111  VAL C 113  0
SHEET    2  AH 2 CYS C 145  LEU C 147 -1  O  LEU C 147   N  THR C 111
SHEET    1  AI 4 PHE E  60  ALA E  62  0
SHEET    2  AI 4 LEU E  78  PHE E  82 -1  O  VAL E  80   N  PHE E  60
SHEET    3  AI 4 THR E 107  TYR E 112  1  O  VAL E 111   N  GLU E  81
SHEET    4  AI 4 THR E 131  ASN E 136  1  O  GLU E 133   N  PHE E 110
SHEET    1  AJ 2 SER E  87  VAL E  88  0
SHEET    2  AJ 2 ASN E 115  ILE E 116  1  O  ASN E 115   N  VAL E  88
SHEET    1  AK 4 LYS E 152  ARG E 155  0
SHEET    2  AK 4 VAL E 195  SER E 202 -1  O  ILE E 199   N  LYS E 152
SHEET    3  AK 4 GLY E 206  CYS E 214 -1  O  TYR E 208   N  ARG E 200
SHEET    4  AK 4 ARG E 177  ILE E 178  1  N  ILE E 178   O  ILE E 213
SHEET    1  AL 8 TYR H  95  GLY H  99  0
SHEET    2  AL 8 ALA H 140  ARG H 145 -1  O  LEU H 142   N  MET H  97
SHEET    3  AL 8 SER H  54  ALA H  60 -1  N  THR H  56   O  ARG H 145
SHEET    4  AL 8 ILE H   9  ASP H  16 -1  N  PHE H  10   O  LEU H  55
SHEET    5  AL 8 VAL H  23  SER H  30 -1  O  ALA H  29   N  GLN H  11
SHEET    6  AL 8 LYS H  37  ASN H  43 -1  O  LEU H  40   N  ILE H  26
SHEET    7  AL 8 LEU H 121  GLU H 126 -1  O  LEU H 122   N  ASP H  41
SHEET    8  AL 8 ALA H 113  VAL H 114 -1  N  VAL H 114   O  LEU H 125
SHEET    1  AM 8 TYR H  95  GLY H  99  0
SHEET    2  AM 8 ALA H 140  ARG H 145 -1  O  LEU H 142   N  MET H  97
SHEET    3  AM 8 SER H  54  ALA H  60 -1  N  THR H  56   O  ARG H 145
SHEET    4  AM 8 ILE H   9  ASP H  16 -1  N  PHE H  10   O  LEU H  55
SHEET    5  AM 8 VAL H  23  SER H  30 -1  O  ALA H  29   N  GLN H  11
SHEET    6  AM 8 LYS H  37  ASN H  43 -1  O  LEU H  40   N  ILE H  26
SHEET    7  AM 8 LEU H 121  GLU H 126 -1  O  LEU H 122   N  ASP H  41
SHEET    8  AM 8 SER H 117  PHE H 118 -1  N  PHE H 118   O  LEU H 121
SHEET    1  AN 3 LEU I  14  ASP I  19  0
SHEET    2  AN 3 ARG I  24  CYS I  29 -1  O  ARG I  24   N  ASP I  19
SHEET    3  AN 3 VAL I  35  GLU I  37 -1  O  GLU I  36   N  PHE I  27
SHEET    1  AO 4 ARG I  70  SER I  71  0
SHEET    2  AO 4 ASN I  83  GLN I  87 -1  O  ASN I  83   N  SER I  71
SHEET    3  AO 4 LEU I  99  CYS I 103 -1  O  PHE I 100   N  PHE I  86
SHEET    4  AO 4 ILE I 109  THR I 111 -1  O  PHE I 110   N  PHE I 101
SHEET    1  AP 4 ILE K  21  PRO K  23  0
SHEET    2  AP 4 ALA K  30  GLU K  36 -1  O  VAL K  32   N  ASP K  22
SHEET    3  AP 4 ARG K  70  THR K  77 -1  O  ILE K  75   N  VAL K  31
SHEET    4  AP 4 VAL K  56  LYS K  62 -1  N  PHE K  58   O  GLN K  76
SSBOND   1 CYS A  107    CYS A  110                          1555   1555  1.82
SSBOND   2 CYS A  110    CYS A  167                          1555   1555  2.59
SSBOND   3 CYS B 1163    CYS B 1185                          1555   1555  2.48
SSBOND   4 CYS B 1166    CYS B 1185                          1555   1555  2.61
SSBOND   5 CYS B 1182    CYS B 1185                          1555   1555  2.86
SSBOND   6 CYS C   86    CYS C   95                          1555   1555  2.53
SSBOND   7 CYS I    7    CYS I   32                          1555   1555  1.98
SSBOND   8 CYS I   10    CYS I   32                          1555   1555  2.12
SSBOND   9 CYS I   29    CYS I   32                          1555   1555  2.92
SSBOND  10 CYS I   75    CYS I   78                          1555   1555  2.54
SSBOND  11 CYS I   78    CYS I  106                          1555   1555  1.76
SSBOND  12 CYS I  103    CYS I  106                          1555   1555  2.59
SSBOND  13 CYS J    7    CYS J   10                          1555   1555  2.71
SSBOND  14 CYS J   10    CYS J   46                          1555   1555  2.89
SSBOND  15 CYS L   31    CYS L   48                          1555   1555  2.43
LINK        ZN    ZN A3006                 SG  CYS A 167     1555   1555  2.24
LINK        ZN    ZN A3006                 SG  CYS A 110     1555   1555  1.20
LINK        ZN    ZN A3006                 SG  CYS A 107     1555   1555  1.49
LINK        ZN    ZN A3006                 SG  CYS A 148     1555   1555  1.64
LINK        ZN    ZN A3008                 NE2 HIS A  80     1555   1555  1.71
LINK        ZN    ZN A3008                 SG  CYS A  70     1555   1555  1.18
LINK        ZN    ZN A3008                 SG  CYS A  77     1555   1555  2.10
LINK        ZN    ZN B3007                 SG  CYS B1185     1555   1555  0.86
LINK        ZN    ZN B3007                 SG  CYS B1163     1555   1555  2.19
LINK        ZN    ZN B3007                 SG  CYS B1166     1555   1555  2.24
LINK        ZN    ZN B3007                 SG  CYS B1182     1555   1555  2.07
LINK        ZN    ZN C3002                 SG  CYS C  86     1555   1555  1.33
LINK        ZN    ZN C3002                 SG  CYS C  88     1555   1555  2.25
LINK        ZN    ZN C3002                 SG  CYS C  92     1555   1555  2.16
LINK        ZN    ZN C3002                 SG  CYS C  95     1555   1555  1.87
LINK        ZN    ZN I3003                 SG  CYS I  32     1555   1555  1.09
LINK        ZN    ZN I3003                 SG  CYS I  29     1555   1555  2.11
LINK        ZN    ZN I3003                 SG  CYS I   7     1555   1555  1.52
LINK        ZN    ZN I3003                 SG  CYS I  10     1555   1555  1.72
LINK        ZN    ZN I3004                 SG  CYS I  75     1555   1555  1.83
LINK        ZN    ZN I3004                 SG  CYS I 106     1555   1555  1.29
LINK        ZN    ZN I3004                 SG  CYS I  78     1555   1555  1.60
LINK        ZN    ZN L3005                 SG  CYS L  48     1555   1555  1.85
LINK        ZN    ZN L3005                 SG  CYS L  31     1555   1555  1.75
LINK        ZN    ZN L3005                 SG  CYS L  51     1555   1555  2.11
LINK        ZN    ZN L3005                 SG  CYS L  34     1555   1555  1.85
LINK        ZN    ZN J3001                 SG  CYS J  45     1555   1555  1.51
LINK        ZN    ZN J3001                 SG  CYS J   7     1555   1555  1.59
LINK        ZN    ZN J3001                 SG  CYS J  10     1555   1555  1.88
LINK        ZN    ZN J3001                 SG  CYS J  46     1555   1555  2.25
LINK        MN    MN A3009                 OD2 ASP A 483     1555   1555  2.09
LINK        MN    MN A3009                 OD2 ASP A 485     1555   1555  2.19
LINK        MN    MN A3009                 O2G CTP B3008     1555   1555  2.02
LINK        MN    MN A3009                 OD1 ASP A 481     1555   1555  1.97
LINK        MN    MN A3009                 O1B CTP B3008     1555   1555  2.54
LINK        MN    MN A3010                 O1B CTP B3008     1555   1555  2.02
LINK        MN    MN A3010                 OD2 ASP A 481     1555   1555  2.18
LINK        MN    MN A3010                 OD2 ASP B 837     1555   1555  2.45
LINK        MN    MN A3010                 OD1 ASP A 483     1555   1555  2.16
LINK        ZN    ZN I3004                 SG  CYS I 103     1555   1555  2.62
CISPEP   1 GLN A  447    PRO A  448          0        -1.87
CISPEP   2 PRO E  128    PRO E  129          0        28.98
SITE     1 AC1  4 ASP A 481  ASP A 483  ASP A 485  CTP B3008
SITE     1 AC2  4 ASP A 481  ASP A 483  ASP B 837  CTP B3008
SITE     1 AC3  4 CYS J   7  CYS J  10  CYS J  45  CYS J  46
SITE     1 AC4  4 CYS C  86  CYS C  88  CYS C  92  CYS C  95
SITE     1 AC5  4 CYS I   7  CYS I  10  CYS I  29  CYS I  32
SITE     1 AC6  4 CYS I  75  CYS I  78  CYS I 103  CYS I 106
SITE     1 AC7  5 CYS L  31  CYS L  34  SER L  36  CYS L  48
SITE     2 AC7  5 CYS L  51
SITE     1 AC8  4 CYS A 107  CYS A 110  CYS A 148  CYS A 167
SITE     1 AC9  4 CYS B1163  CYS B1166  CYS B1182  CYS B1185
SITE     1 BC1  4 CYS A  67  CYS A  70  CYS A  77  HIS A  80
SITE     1 BC2  9 ASP A 481  ASP A 483  ASP A 485   MN A3009
SITE     2 BC2  9  MN A3010  ARG B 766  GLN B 986  LYS B 987
SITE     3 BC2  9 HOH B3010
CRYST1  123.000  223.000  374.000  90.00  90.00  90.00 I 2 2 2       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      0.008130  0.000000  0.000000        0.00000
SCALE2      0.000000  0.004484  0.000000        0.00000
SCALE3      0.000000  0.000000  0.002674        0.00000
      
PROCHECK
Go to PROCHECK summary
 References