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PDBsum entry 2nvz

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Top Page protein dna_rna ligands metals Protein-protein interface(s) links
Transcription,transferase/DNA-RNA hybrid PDB id
2nvz
Jmol
Contents
Protein chains
1398 a.a.
1096 a.a.
266 a.a.
193 a.a.
83 a.a.
133 a.a.
119 a.a.
65 a.a.
114 a.a.
46 a.a.
DNA/RNA
Ligands
UTP
Metals
_ZN ×8
_MG ×2
HEADER    TRANSCRIPTION,TRANSFERASE/DNA-RNA HYBRID14-NOV-06   2NVZ
TITLE     RNA POLYMERASE II ELONGATION COMPLEX WITH UTP, UPDATED
TITLE    2 11/2006
COMPND    MOL_ID: 1;
COMPND   2 MOLECULE: 5'-R(*AP*UP*CP*GP*AP*GP*AP*GP*GP*A)-3';
COMPND   3 CHAIN: R;
COMPND   4 ENGINEERED: YES;
COMPND   5 MOL_ID: 2;
COMPND   6 MOLECULE: 28-MER DNA TEMPLATE STRAND;
COMPND   7 CHAIN: T;
COMPND   8 ENGINEERED: YES;
COMPND   9 MOL_ID: 3;
COMPND  10 MOLECULE: 5'-D(*CP*TP*GP*CP*TP*TP*AP*TP*CP*GP*GP*TP*AP*G)-
COMPND  11 3';
COMPND  12 CHAIN: N;
COMPND  13 ENGINEERED: YES;
COMPND  14 MOL_ID: 4;
COMPND  15 MOLECULE: DNA-DIRECTED RNA POLYMERASE II LARGEST SUBUNIT;
COMPND  16 CHAIN: A;
COMPND  17 SYNONYM: RNA POLYMERASE II SUBUNIT 1, B220;
COMPND  18 EC: 2.7.7.6;
COMPND  19 MOL_ID: 5;
COMPND  20 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 140 KDA
COMPND  21 POLYPEPTIDE;
COMPND  22 CHAIN: B;
COMPND  23 SYNONYM: B150, RNA POLYMERASE II SUBUNIT 2;
COMPND  24 EC: 2.7.7.6;
COMPND  25 MOL_ID: 6;
COMPND  26 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 45 KDA
COMPND  27 POLYPEPTIDE;
COMPND  28 CHAIN: C;
COMPND  29 SYNONYM: B44.5;
COMPND  30 EC: 2.7.7.6;
COMPND  31 MOL_ID: 7;
COMPND  32 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 27
COMPND  33 KDA POLYPEPTIDE;
COMPND  34 CHAIN: E;
COMPND  35 SYNONYM: ABC27;
COMPND  36 EC: 2.7.7.6;
COMPND  37 MOL_ID: 8;
COMPND  38 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 23
COMPND  39 KDA POLYPEPTIDE;
COMPND  40 CHAIN: F;
COMPND  41 SYNONYM: ABC23;
COMPND  42 EC: 2.7.7.6;
COMPND  43 MOL_ID: 9;
COMPND  44 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 14.5
COMPND  45 KDA POLYPEPTIDE;
COMPND  46 CHAIN: H;
COMPND  47 SYNONYM: ABC14.4;
COMPND  48 EC: 2.7.7.6;
COMPND  49 MOL_ID: 10;
COMPND  50 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT 9;
COMPND  51 CHAIN: I;
COMPND  52 SYNONYM: DNA-DIRECTED RNA POLYMERASE II 14.2 KDA
COMPND  53 POLYPEPTIDE, B12.6;
COMPND  54 EC: 2.7.7.6;
COMPND  55 MOL_ID: 11;
COMPND  56 MOLECULE: DNA-DIRECTED RNA POLYMERASES I/II/III SUBUNIT 10;
COMPND  57 CHAIN: J;
COMPND  58 SYNONYM: DNA- DIRECTED RNA POLYMERASES I, II, AND III 8.3
COMPND  59 KDA POLYPEPTIDE, ABC10- BETA, ABC8;
COMPND  60 EC: 2.7.7.6;
COMPND  61 MOL_ID: 12;
COMPND  62 MOLECULE: DNA-DIRECTED RNA POLYMERASE II 13.6 KDA
COMPND  63 POLYPEPTIDE;
COMPND  64 CHAIN: K;
COMPND  65 SYNONYM: B13.6;
COMPND  66 EC: 2.7.7.6;
COMPND  67 MOL_ID: 13;
COMPND  68 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III 7.7
COMPND  69 KDA POLYPEPTIDE;
COMPND  70 CHAIN: L;
COMPND  71 SYNONYM: ABC10-ALPHA;
COMPND  72 EC: 2.7.7.6
SOURCE    MOL_ID: 1;
SOURCE   2 SYNTHETIC: YES;
SOURCE   3 MOL_ID: 2;
SOURCE   4 SYNTHETIC: YES;
SOURCE   5 MOL_ID: 3;
SOURCE   6 SYNTHETIC: YES;
SOURCE   7 MOL_ID: 4;
SOURCE   8 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE   9 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  10 ORGANISM_TAXID: 4932;
SOURCE  11 STRAIN: DELTA-RPB4;
SOURCE  12 MOL_ID: 5;
SOURCE  13 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  14 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  15 ORGANISM_TAXID: 4932;
SOURCE  16 STRAIN: DELTA-RPB4;
SOURCE  17 MOL_ID: 6;
SOURCE  18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  19 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  20 ORGANISM_TAXID: 4932;
SOURCE  21 STRAIN: DELTA-RPB4;
SOURCE  22 MOL_ID: 7;
SOURCE  23 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  24 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  25 ORGANISM_TAXID: 4932;
SOURCE  26 STRAIN: DELTA-RPB4;
SOURCE  27 MOL_ID: 8;
SOURCE  28 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  29 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  30 ORGANISM_TAXID: 4932;
SOURCE  31 STRAIN: DELTA-RPB4;
SOURCE  32 MOL_ID: 9;
SOURCE  33 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  34 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  35 ORGANISM_TAXID: 4932;
SOURCE  36 STRAIN: DELTA-RPB4;
SOURCE  37 MOL_ID: 10;
SOURCE  38 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  39 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  40 ORGANISM_TAXID: 4932;
SOURCE  41 STRAIN: DELTA-RPB4;
SOURCE  42 MOL_ID: 11;
SOURCE  43 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  44 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  45 ORGANISM_TAXID: 4932;
SOURCE  46 STRAIN: DELTA-RPB4;
SOURCE  47 MOL_ID: 12;
SOURCE  48 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  49 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  50 ORGANISM_TAXID: 4932;
SOURCE  51 STRAIN: DELTA-RPB4;
SOURCE  52 MOL_ID: 13;
SOURCE  53 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE  54 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE  55 ORGANISM_TAXID: 4932;
SOURCE  56 STRAIN: DELTA-RPB4
KEYWDS    TRANSCRIPTION, MRNA, MULTIPROTEIN COMPLEX, MOLECULAR
KEYWDS   2 MACHINE, DNA, TRANSCRIPTION,TRANSFERASE/DNA-RNA HYBRID
KEYWDS   3 COMPLEX
EXPDTA    X-RAY DIFFRACTION
AUTHOR    D.WANG,D.A.BUSHNELL,K.D.WESTOVER,C.D.KAPLAN,R.D.KORNBERG
REVDAT   2   24-FEB-09 2NVZ    1       VERSN
REVDAT   1   19-DEC-06 2NVZ    0
JRNL        AUTH   D.WANG,D.A.BUSHNELL,K.D.WESTOVER,C.D.KAPLAN,
JRNL        AUTH 2 R.D.KORNBERG
JRNL        TITL   STRUCTURAL BASIS OF TRANSCRIPTION: ROLE OF THE
JRNL        TITL 2 TRIGGER LOOP IN SUBSTRATE SPECIFICITY AND CATALYSIS
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 127   941 2006
JRNL        REFN                   ISSN 0092-8674
JRNL        PMID   17129781
JRNL        DOI    10.1016/J.CELL.2006.11.023
REMARK   1
REMARK   2
REMARK   2 RESOLUTION.    4.30 ANGSTROMS.
REMARK   3
REMARK   3 REFINEMENT.
REMARK   3   PROGRAM     : REFMAC 5.2.0019
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON
REMARK   3
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK   3
REMARK   3  DATA USED IN REFINEMENT.
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.30
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL
REMARK   3   NUMBER OF REFLECTIONS             : 37247
REMARK   3
REMARK   3  FIT TO DATA USED IN REFINEMENT.
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.276
REMARK   3   R VALUE            (WORKING SET) : 0.270
REMARK   3   FREE R VALUE                     : 0.332
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100
REMARK   3   FREE R VALUE TEST SET COUNT      : 4179
REMARK   3
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.
REMARK   3   TOTAL NUMBER OF BINS USED           : 20
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 4.30
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 4.41
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2666
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 84.14
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3640
REMARK   3   BIN FREE R VALUE SET COUNT          : 311
REMARK   3   BIN FREE R VALUE                    : 0.4180
REMARK   3
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK   3   PROTEIN ATOMS            : 27897
REMARK   3   NUCLEIC ACID ATOMS       : 1066
REMARK   3   HETEROGEN ATOMS          : 39
REMARK   3   SOLVENT ATOMS            : 0
REMARK   3
REMARK   3  B VALUES.
REMARK   3   FROM WILSON PLOT           (A**2) : NULL
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 126.99
REMARK   3   OVERALL ANISOTROPIC B VALUE.
REMARK   3    B11 (A**2) : 0.00000
REMARK   3    B22 (A**2) : 0.00000
REMARK   3    B33 (A**2) : 0.00000
REMARK   3    B12 (A**2) : 0.00000
REMARK   3    B13 (A**2) : 0.00000
REMARK   3    B23 (A**2) : 0.00000
REMARK   3
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.
REMARK   3   ESU BASED ON R VALUE                            (A): NULL
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 1.369
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 1.171
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 208.996
REMARK   3
REMARK   3 CORRELATION COEFFICIENTS.
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.873
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.817
REMARK   3
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 29660 ; 0.009 ; 0.022
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 40270 ; 1.364 ; 2.017
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  3483 ; 7.070 ; 5.000
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1322 ;39.073 ;24.009
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  5187 ;21.606 ;15.000
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   221 ;17.847 ;15.000
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  4534 ; 0.098 ; 0.200
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 21796 ; 0.003 ; 0.020
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 14419 ; 0.245 ; 0.200
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 19321 ; 0.307 ; 0.200
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   948 ; 0.177 ; 0.200
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    40 ; 0.223 ; 0.200
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     1 ; 0.299 ; 0.200
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2): 18024 ; 0.340 ; 1.500
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 28315 ; 0.615 ; 2.000
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 13443 ; 0.494 ; 3.000
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11955 ; 0.973 ; 4.500
REMARK   3
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL
REMARK   3
REMARK   3  NCS RESTRAINTS STATISTICS
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK   3
REMARK   3  TLS DETAILS
REMARK   3   NUMBER OF TLS GROUPS  : NULL
REMARK   3
REMARK   3  BULK SOLVENT MODELLING.
REMARK   3   METHOD USED : MASK
REMARK   3   PARAMETERS FOR MASK CALCULATION
REMARK   3   VDW PROBE RADIUS   : 1.40
REMARK   3   ION PROBE RADIUS   : 0.80
REMARK   3   SHRINKAGE RADIUS   : 0.80
REMARK   3
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK   3  RIDING POSITIONS
REMARK   4
REMARK   4 2NVZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-DEC-06.
REMARK 100 THE RCSB ID CODE IS RCSB040369.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-03
REMARK 200  TEMPERATURE           (KELVIN) : 100
REMARK 200  PH                             : 6.5
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) : 0.98
REMARK 200  MONOCHROMATOR                  : NULL
REMARK 200  OPTICS                         : NULL
REMARK 200
REMARK 200  DETECTOR TYPE                  : CCD
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200  DATA SCALING SOFTWARE          : NULL
REMARK 200
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50043
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.200
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8
REMARK 200  DATA REDUNDANCY                : 2.500
REMARK 200  R MERGE                    (I) : NULL
REMARK 200  R SYM                      (I) : 0.15700
REMARK 200   FOR THE DATA SET  : 11.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.20
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.30
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.2
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL
REMARK 200  R MERGE FOR SHELL          (I) : NULL
REMARK 200  R SYM FOR SHELL            (I) : 0.36100
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: 1SFO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS   (%): 67.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 390MM (NH4)2HPO4/NAH2PO4, PH 6.5,
REMARK 280  50MM DIOXANE, 10MM DTT, 9-12% PEG6000, VAPOR DIFFUSION,
REMARK 280  HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290       4555   -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290     WHERE NNN -> OPERATOR NUMBER
REMARK 290           MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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       84.82350
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      111.16900
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.82350
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000      111.16900
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIDECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R, T, N, A, B, C, E, F, H,
REMARK 350                    AND CHAINS: 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 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     ASP A   156
REMARK 465     ASP A   157
REMARK 465     PRO A   158
REMARK 465     THR A   159
REMARK 465     GLN A   160
REMARK 465     LYS A   186
REMARK 465     LYS A   187
REMARK 465     ASP A   188
REMARK 465     ARG A   189
REMARK 465     ALA A   190
REMARK 465     THR A   191
REMARK 465     GLY A   192
REMARK 465     ASP A   193
REMARK 465     ALA A   194
REMARK 465     ASP A   195
REMARK 465     GLU A   196
REMARK 465     PRO A   197
REMARK 465     GLU A   198
REMARK 465     LEU A   315
REMARK 465     GLN A   316
REMARK 465     LYS A   317
REMARK 465     SER A   318
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     ASN A  1232
REMARK 465     ASP A  1233
REMARK 465     GLU A  1234
REMARK 465     LYS A  1235
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     ASP A  1446
REMARK 465     GLU A  1447
REMARK 465     GLU A  1448
REMARK 465     SER A  1449
REMARK 465     LEU A  1450
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     PHE B    18
REMARK 465     GLU B    19
REMARK 465     LEU B    71
REMARK 465     GLU B    72
REMARK 465     GLN B    73
REMARK 465     LEU B    74
REMARK 465     ALA B    75
REMARK 465     GLN B    76
REMARK 465     HIS B    77
REMARK 465     THR B    78
REMARK 465     THR B    79
REMARK 465     GLU B    80
REMARK 465     SER B    81
REMARK 465     ASP B    82
REMARK 465     ASN B    83
REMARK 465     ILE B    84
REMARK 465     SER B    85
REMARK 465     ARG B    86
REMARK 465     LYS B    87
REMARK 465     TYR B    88
REMARK 465     GLU B    89
REMARK 465     LYS B   133
REMARK 465     LYS B   134
REMARK 465     ARG B   135
REMARK 465     THR B   136
REMARK 465     TYR B   137
REMARK 465     GLU B   138
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     ARG B   249
REMARK 465     PHE B   250
REMARK 465     ARG B   336
REMARK 465     ARG B   337
REMARK 465     GLY B   338
REMARK 465     THR B   339
REMARK 465     ALA B   340
REMARK 465     LEU B   341
REMARK 465     GLY B   342
REMARK 465     ILE B   343
REMARK 465     LYS B   344
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     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   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     HIS B   733
REMARK 465     HIS B   734
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     SER B   933
REMARK 465     LYS B   934
REMARK 465     PHE B  1224
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 E     1
REMARK 465     ASP E     2
REMARK 465     SER E    49
REMARK 465     MET E    50
REMARK 465     GLY E    51
REMARK 465     CYS E    83
REMARK 465     ASP E    84
REMARK 465     GLU E    85
REMARK 465     PRO E    86
REMARK 465     SER E    87
REMARK 465     VAL E    88
REMARK 465     GLY E    89
REMARK 465     VAL E    90
REMARK 465     LYS E    91
REMARK 465     THR E    92
REMARK 465     MET E    93
REMARK 465     LYS E    94
REMARK 465     TYR E   112
REMARK 465     GLN E   113
REMARK 465     ASN E   114
REMARK 465     ASN E   115
REMARK 465     ILE E   116
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     MET I     1
REMARK 465     PHE I   121
REMARK 465     SER I   122
REMARK 465     LEU J    66
REMARK 465     GLU J    67
REMARK 465     LYS J    68
REMARK 465     ARG J    69
REMARK 465     ASP J    70
REMARK 465     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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470   M RES CSSEQI  ATOMS
REMARK 470       A R  10    O3'
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   SG   CYS A    77    ZN    ZN  A  1735              1.03
REMARK 500   O    THR A  1080     N    ASN A  1082              1.86
REMARK 500   ND2  ASN C   184     O    THR C   189              2.13
REMARK 500   O    THR B   487     OG   SER B   490              2.14
REMARK 500   O    GLY A  1073     OG1  THR A  1077              2.15
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    PRO A1158   CG    PRO A1158   CD      0.186
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     DT T   2   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES
REMARK 500     DC T   4   O4' -  C1' -  N1  ANGL. DEV. =   3.6 DEGREES
REMARK 500     DC T   5   O4' -  C1' -  N1  ANGL. DEV. =   3.3 DEGREES
REMARK 500     DG T   6   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES
REMARK 500     DT T   8   O4' -  C1' -  N1  ANGL. DEV. =   3.1 DEGREES
REMARK 500     DA T  10   O4' -  C1' -  N9  ANGL. DEV. =   2.3 DEGREES
REMARK 500     DG T  11   O4' -  C1' -  N9  ANGL. DEV. =   5.9 DEGREES
REMARK 500     DC T  16   O4' -  C4' -  C3' ANGL. DEV. =  -2.4 DEGREES
REMARK 500     DC T  16   O4' -  C1' -  N1  ANGL. DEV. =   6.2 DEGREES
REMARK 500     DA T  15   C3' -  O3' -  P   ANGL. DEV. =   9.3 DEGREES
REMARK 500     DT T  19   C4  -  C5  -  C7  ANGL. DEV. =   4.9 DEGREES
REMARK 500     DT T  19   C6  -  C5  -  C7  ANGL. DEV. =  -4.4 DEGREES
REMARK 500     DC T  20   O4' -  C4' -  C3' ANGL. DEV. =  -3.4 DEGREES
REMARK 500     DC T  20   C4' -  C3' -  C2' ANGL. DEV. =  -4.7 DEGREES
REMARK 500     DC T  23   O4' -  C4' -  C3' ANGL. DEV. =  -4.1 DEGREES
REMARK 500     DC T  23   C4' -  C3' -  C2' ANGL. DEV. =  -4.5 DEGREES
REMARK 500     DC T  23   O4' -  C1' -  N1  ANGL. DEV. =   5.5 DEGREES
REMARK 500     DT T  24   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES
REMARK 500     DC T  25   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES
REMARK 500     DA T  27   O4' -  C4' -  C3' ANGL. DEV. =  -2.9 DEGREES
REMARK 500     DC N   1   O4' -  C1' -  N1  ANGL. DEV. =   3.9 DEGREES
REMARK 500     DT N   5   O4' -  C1' -  N1  ANGL. DEV. =   2.2 DEGREES
REMARK 500     DT N   6   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES
REMARK 500     DC N   9   O4' -  C1' -  N1  ANGL. DEV. =   2.5 DEGREES
REMARK 500     DT N  12   O4' -  C1' -  N1  ANGL. DEV. =   3.0 DEGREES
REMARK 500    LEU B 883   CA  -  CB  -  CG  ANGL. DEV. =  14.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500  M RES CSSEQI        PSI       PHI
REMARK 500    SER A   8       82.37    -65.99
REMARK 500    ILE A  35       76.52     48.21
REMARK 500    GLU A  39      -80.01    -97.25
REMARK 500    THR A  40      -60.85   -147.37
REMARK 500    MET A  41      -85.29   -104.21
REMARK 500    THR A  44       80.12     61.61
REMARK 500    THR A  46      103.15    -55.33
REMARK 500    ALA A  48     -110.01   -160.38
REMARK 500    ASN A  54       63.85     22.70
REMARK 500    ASP A  55      -53.11   -164.42
REMARK 500    LEU A  58     -172.18    -63.15
REMARK 500    ARG A  63       51.06     18.00
REMARK 500    THR A  69       19.79     49.44
REMARK 500    GLN A  71     -116.95    -77.24
REMARK 500    GLU A  72      -73.88     57.19
REMARK 500    MET A 108     -175.68     66.67
REMARK 500    ASP A 130      162.83     74.60
REMARK 500    PRO A 153      150.80    -44.74
REMARK 500    LEU A 179      -36.57   -137.24
REMARK 500    HIS A 213     -114.49    -86.42
REMARK 500    ILE A 214      122.44     64.75
REMARK 500    ARG A 247       84.49   -150.11
REMARK 500    PRO A 248     -155.96    -76.04
REMARK 500    SER A 249     -106.51   -141.32
REMARK 500    ILE A 250      124.98     51.08
REMARK 500    ASN A 253      -62.94   -129.73
REMARK 500    GLU A 254      117.23     71.60
REMARK 500    ARG A 257      -19.76   -168.28
REMARK 500    LEU A 279      -18.40    124.35
REMARK 500    ASN A 282      -78.07   -102.28
REMARK 500    ALA A 284       -2.65   -170.85
REMARK 500    HIS A 287      -64.83   -166.46
REMARK 500    ALA A 288       58.28   -179.21
REMARK 500    ILE A 289        5.14     52.33
REMARK 500    GLU A 290       36.66   -149.23
REMARK 500    ASN A 306       60.51   -169.90
REMARK 500    PRO A 312      -77.17    -70.55
REMARK 500    GLN A 313     -150.96    161.02
REMARK 500    PRO A 321     -128.46    -91.71
REMARK 500    LYS A 323      -84.58   -115.51
REMARK 500    ILE A 325      -48.73     63.23
REMARK 500    LYS A 332      120.27     72.73
REMARK 500    GLU A 333       -2.86     56.49
REMARK 500    ASN A 339       14.97   -140.72
REMARK 500    LEU A 340      -34.12   -138.29
REMARK 500    PRO A 396       23.06    -66.54
REMARK 500    ASN A 397      -62.45   -123.44
REMARK 500    TYR A 404      135.05     55.60
REMARK 500    TYR A 417     -154.72    -90.08
REMARK 500    SER A 418      157.64     63.04
REMARK 500    ASP A 423      -95.65   -172.55
REMARK 500    ILE A 424      127.01     57.39
REMARK 500    HIS A 435      178.40    -56.83
REMARK 500    ASN A 439       71.85     57.34
REMARK 500    HIS A 451     -154.96   -151.15
REMARK 500    TYR A 465      157.16     59.06
REMARK 500    ASN A 479       66.19     87.34
REMARK 500    ASP A 483        8.78    -67.44
REMARK 500    LEU A 504      -56.24   -138.14
REMARK 500    PRO A 514       47.50    -80.29
REMARK 500    GLN A 515      -46.16   -152.80
REMARK 500    ASN A 517       25.12     35.58
REMARK 500    GLN A 525     -115.41     91.02
REMARK 500    LEU A 543      -76.58    -14.03
REMARK 500    LYS A 567     -174.91    -69.67
REMARK 500    PRO A 568      -34.35    -20.15
REMARK 500    GLN A 576      -82.12    -31.63
REMARK 500    ARG A 590      -75.80   -123.93
REMARK 500    PHE A 591      106.90     64.34
REMARK 500    LEU A 597       -9.60     66.93
REMARK 500    MET A 605      104.47   -171.43
REMARK 500    THR A 621      -63.44   -106.71
REMARK 500    SER A 624       30.34    -64.04
REMARK 500    LYS A 637      107.36     -2.27
REMARK 500    GLN A 650      -74.41    -42.84
REMARK 500    LYS A 651      -37.96    -32.97
REMARK 500    PHE A 662      142.23    176.59
REMARK 500    SER A 663     -155.77   -146.46
REMARK 500    PRO A 674       49.37    -65.80
REMARK 500    THR A 675      -33.26   -144.88
REMARK 500    LEU A 702      -81.89    142.96
REMARK 500    MET A 708      -10.22     58.04
REMARK 500    LEU A 710      102.34    115.42
REMARK 500    GLU A 712      -39.82   -132.34
REMARK 500    SER A 713      -87.56   -174.44
REMARK 500    LEU A 737       82.73    -69.13
REMARK 500    ASN A 741      100.98    -45.75
REMARK 500    SER A 754     -157.83   -154.74
REMARK 500    ALA A 763      -82.58   -106.33
REMARK 500    ILE A 775      120.60    -28.52
REMARK 500    ASP A 790       78.57     65.58
REMARK 500    VAL A 829      -65.41   -102.78
REMARK 500    ARG A 839      -18.83    -47.18
REMARK 500    GLU A 846     -109.22     48.58
REMARK 500    ASP A 847       27.64    -74.62
REMARK 500    TYR A 852       23.95    -75.21
REMARK 500    ASP A 853       31.60   -143.11
REMARK 500    ASN A 854        9.74     53.85
REMARK 500    TYR A 868      139.11    -36.36
REMARK 500    GLU A 870       22.00     44.13
REMARK 500    ASP A 871       10.35   -152.81
REMARK 500    LYS A 880       76.30    -69.54
REMARK 500    LEU A 883       93.91    -62.10
REMARK 500    ASP A 884       39.92    -90.88
REMARK 500    ILE A 886      -75.91    -64.31
REMARK 500    LYS A 895       31.21    -74.79
REMARK 500    ARG A 896      -23.78   -142.04
REMARK 500    TYR A 897      -31.57   -136.59
REMARK 500    LEU A 902       97.62    -59.40
REMARK 500    ASN A 903       89.37    151.26
REMARK 500    PRO A 910        4.85    -55.09
REMARK 500    LEU A 920      109.12    -29.39
REMARK 500    ASP A 922      150.11     64.16
REMARK 500    LEU A 923      -60.30   -101.35
REMARK 500    VAL A 958      105.46     61.68
REMARK 500    ARG A 961      -39.22    -36.85
REMARK 500    GLN A 968       49.46    -82.29
REMARK 500    GLN A 969      -16.62   -162.88
REMARK 500    HIS A 972       99.61    -25.53
REMARK 500    HIS A 975     -126.66    -83.86
REMARK 500    LEU A 998      125.71     57.21
REMARK 500    LYS A1003      -18.34   -164.05
REMARK 500    ASP A1013       36.61    -70.34
REMARK 500    ALA A1014      -37.45   -148.73
REMARK 500    THR A1016      -62.30     -6.36
REMARK 500    LEU A1026       57.62    -99.60
REMARK 500    GLN A1033      -61.15   -144.71
REMARK 500    LEU A1054        4.49    -64.11
REMARK 500    GLU A1062      120.68    -26.15
REMARK 500    ALA A1069     -134.68    -73.68
REMARK 500    GLN A1070       45.63    -90.72
REMARK 500    ILE A1072     -111.35     80.12
REMARK 500    GLU A1074      -72.84    -72.17
REMARK 500    THR A1080     -119.76    -96.55
REMARK 500    LEU A1081      -17.10     18.95
REMARK 500    PHE A1084      164.56     50.22
REMARK 500    HIS A1085      138.03    -19.20
REMARK 500    PHE A1086      -54.13   -157.22
REMARK 500    ALA A1087      -73.62   -135.96
REMARK 500    LYS A1092     -132.70     47.18
REMARK 500    LYS A1093      -51.87   -140.79
REMARK 500    VAL A1094      -58.41     96.00
REMARK 500    VAL A1107       77.11     69.44
REMARK 500    LYS A1112      -73.22    -71.31
REMARK 500    ALA A1126       18.57   -155.27
REMARK 500    ASP A1127       98.09    -43.11
REMARK 500    GLN A1128       53.59     31.31
REMARK 500    TYR A1153      116.16    108.42
REMARK 500    TYR A1154     -141.95    -73.38
REMARK 500    PRO A1156     -120.07      9.43
REMARK 500    ASP A1157      175.65     72.68
REMARK 500    PRO A1158       46.02     13.27
REMARK 500    SER A1160       87.05     23.42
REMARK 500    ILE A1163      111.44     33.62
REMARK 500    PRO A1164      139.08    -31.34
REMARK 500    GLU A1165       95.46     14.05
REMARK 500    GLU A1167     -106.38    -72.94
REMARK 500    GLN A1171      -84.28    -76.87
REMARK 500    LEU A1172       29.20     29.45
REMARK 500    HIS A1173       69.42   -102.81
REMARK 500    PHE A1174       42.79    -75.79
REMARK 500    SER A1175       41.74   -105.65
REMARK 500    TRP A1191      131.11     58.26
REMARK 500    LEU A1192      125.92    102.06
REMARK 500    ARG A1194      -72.86    -91.19
REMARK 500    LEU A1195      150.74     77.75
REMARK 500    ASP A1198       76.76     72.06
REMARK 500    ALA A1200       87.73   -167.63
REMARK 500    ALA A1201     -119.77     47.16
REMARK 500    ASP A1204      -83.88    -88.53
REMARK 500    ASP A1206      100.40    -47.02
REMARK 500    GLU A1214      -72.24   -111.63
REMARK 500    PHE A1220      -53.34   -144.30
REMARK 500    LYS A1221      -28.72     71.04
REMARK 500    ASP A1223       72.46   -155.87
REMARK 500    LEU A1224      101.71    172.42
REMARK 500    TRP A1228       82.13     70.94
REMARK 500    SER A1229     -167.62   -113.41
REMARK 500    GLU A1230       69.49   -110.42
REMARK 500    ILE A1237      161.11    177.18
REMARK 500    GLU A1255       78.77     54.67
REMARK 500    LYS A1262       28.42    -68.34
REMARK 500    GLU A1269       60.33   -109.45
REMARK 500    ASN A1270      -44.93   -164.26
REMARK 500    ASN A1278      -22.13     81.93
REMARK 500    GLU A1280     -102.30   -112.81
REMARK 500    PRO A1292      108.15    -59.92
REMARK 500    ASN A1312       49.15   -147.88
REMARK 500    SER A1314      -61.25    -26.17
REMARK 500    ALA A1357       39.80    -86.25
REMARK 500    SER A1358      -78.24    -85.60
REMARK 500    ASP A1359       59.48    -91.67
REMARK 500    TYR A1365      -69.33     -0.30
REMARK 500    ARG A1366      -49.22    -26.99
REMARK 500    ARG A1391      -38.20   -174.07
REMARK 500    SER A1392       67.76    -48.97
REMARK 500    ASN A1393        9.06     36.60
REMARK 500    SER A1401       31.55    -90.60
REMARK 500    PHE A1402     -103.75   -118.49
REMARK 500    THR A1405      -71.03   -127.93
REMARK 500    SER A1415        8.02    -68.02
REMARK 500    CYS A1421       38.45     72.79
REMARK 500    MET A1433       96.95    -66.96
REMARK 500    PRO A1435       80.32    -54.78
REMARK 500    ILE A1436      -89.50   -111.16
REMARK 500    MET A1444     -157.17   -125.17
REMARK 500    THR B  26     -164.68   -119.98
REMARK 500    PHE B  38      -55.17     76.13
REMARK 500    LYS B  41      -75.37    -77.99
REMARK 500    TYR B  57      -57.61   -120.04
REMARK 500    CYS B  64      -76.14    -58.08
REMARK 500    ASP B  66       -5.41    124.86
REMARK 500    THR B  68      129.59    -36.73
REMARK 500    LEU B  69     -136.41   -137.76
REMARK 500    PRO B 100      135.81    -28.77
REMARK 500    TYR B 124       53.23    -65.78
REMARK 500    ALA B 184       53.97     96.30
REMARK 500    LYS B 193      -14.23     81.48
REMARK 500    ASP B 198      109.91    -44.90
REMARK 500    ASN B 206       16.27     53.30
REMARK 500    LYS B 228       76.48     89.16
REMARK 500    PRO B 231       60.89   -114.53
REMARK 500    SER B 232      133.37     71.40
REMARK 500    SER B 235      -13.55   -158.44
REMARK 500    ALA B 266      101.46    100.16
REMARK 500    ARG B 267       42.46    -91.92
REMARK 500    PRO B 274       91.12    -23.14
REMARK 500    TYR B 275      168.91     58.01
REMARK 500    ILE B 276      125.70     60.40
REMARK 500    LYS B 277      170.95     65.98
REMARK 500    ASP B 294       68.34     76.65
REMARK 500    ILE B 301      -93.10    -75.68
REMARK 500    TYR B 303      -65.27   -102.76
REMARK 500    PHE B 322       -8.37    -59.92
REMARK 500    ASP B 326     -127.78     67.53
REMARK 500    ARG B 327      -77.17    -78.20
REMARK 500    GLU B 328       79.90     55.57
REMARK 500    THR B 329       59.83   -110.48
REMARK 500    ILE B 349       65.11   -105.70
REMARK 500    ALA B 352      -69.13   -141.79
REMARK 500    LEU B 361       70.83     43.36
REMARK 500    ILE B 364      -61.24     83.46
REMARK 500    THR B 365      171.90    173.18
REMARK 500    GLU B 371      -61.13   -105.86
REMARK 500    ASP B 391       92.32     45.47
REMARK 500    ARG B 392     -109.75     69.10
REMARK 500    ALA B 409      -57.46    -26.44
REMARK 500    VAL B 436       28.88     32.48
REMARK 500    ALA B 447      -54.67     76.46
REMARK 500    LYS B 458      -75.15    -51.04
REMARK 500    GLU B 468      -72.60   -160.92
REMARK 500    SER B 474      -82.95     52.38
REMARK 500    ARG B 476      -58.31    -23.66
REMARK 500    ALA B 477      101.17    -30.54
REMARK 500    VAL B 482       31.35    -75.50
REMARK 500    LEU B 483     -144.87     55.56
REMARK 500    ASN B 484      102.71   -172.89
REMARK 500    ARG B 485       63.22   -114.53
REMARK 500    LEU B 521      -54.28   -147.90
REMARK 500    GLN B 531      -87.43     52.64
REMARK 500    LEU B 558      -71.78    -83.99
REMARK 500    PRO B 571      -70.37    -31.31
REMARK 500    HIS B 572      -26.29   -166.27
REMARK 500    GLN B 573      178.70     59.40
REMARK 500    SER B 574      103.84    -55.96
REMARK 500    ASN B 592       91.23     63.88
REMARK 500    LYS B 606      -22.30   -147.17
REMARK 500    THR B 628       38.80   -141.52
REMARK 500    ARG B 635     -158.08   -149.72
REMARK 500    PRO B 636     -140.03    -33.90
REMARK 500    ASP B 642       41.18    -80.18
REMARK 500    HIS B 648      -69.64   -127.76
REMARK 500    LYS B 649      112.57   -165.32
REMARK 500    LYS B 652       14.17    -66.45
REMARK 500    THR B 680     -152.08   -126.03
REMARK 500    SER B 700       40.93    -99.20
REMARK 500    MET B 705      -85.27    -58.48
REMARK 500    GLN B 706       77.02     60.53
REMARK 500    PRO B 707       53.71    -93.97
REMARK 500    GLU B 708      -11.84   -177.32
REMARK 500    LEU B 710       10.65     93.57
REMARK 500    GLU B 711      -26.01   -174.32
REMARK 500    PRO B 712     -153.75    -85.05
REMARK 500    VAL B 731      -78.38    -72.49
REMARK 500    THR B 737       47.28   -151.46
REMARK 500    SER B 746      -28.50    -39.75
REMARK 500    VAL B 751      -74.74    -73.08
REMARK 500    ASN B 786       16.29    -68.26
REMARK 500    VAL B 787      -10.39   -147.69
REMARK 500    MET B 792      139.82     64.24
REMARK 500    LYS B 813       71.26     28.88
REMARK 500    ARG B 815        4.68    -65.90
REMARK 500    TYR B 830     -101.26   -148.87
REMARK 500    ASN B 834       14.94    -69.15
REMARK 500    GLU B 836       73.28     36.40
REMARK 500    PHE B 855      110.71   -160.24
REMARK 500    LYS B 864     -179.11     47.81
REMARK 500    LYS B 865     -129.42   -157.09
REMARK 500    SER B 869      151.10     79.06
REMARK 500    ILE B 870       94.46     55.69
REMARK 500    GLN B 878       51.34     98.45
REMARK 500    THR B 880       -4.73     86.91
REMARK 500    THR B 882      -79.61    103.23
REMARK 500    ARG B 884       42.84     39.11
REMARK 500    LYS B 886       45.66    -73.26
REMARK 500    HIS B 887      -34.28     57.11
REMARK 500    TYR B 890       31.63    -95.68
REMARK 500    ASP B 894     -163.96    -69.37
REMARK 500    GLU B 908       48.27    -97.91
REMARK 500    ALA B 937       31.70   -151.81
REMARK 500    ASN B 946      158.97    178.86
REMARK 500    PRO B 974       81.55    -57.09
REMARK 500    GLN B 975     -172.76    -68.38
REMARK 500    ARG B 983       24.42    -79.91
REMARK 500    HIS B 984       23.10   -142.06
REMARK 500    ARG B 996      -25.85    -37.93
REMARK 500    ASP B 998        2.72    -66.25
REMARK 500    ILE B1017      -51.10   -126.08
REMARK 500    ARG B1020      -25.95    116.50
REMARK 500    MET B1021      123.57    -15.55
REMARK 500    THR B1022       67.82   -163.38
REMARK 500    PRO B1046      -74.14    -55.09
REMARK 500    PHE B1047       67.94   -101.15
REMARK 500    ARG B1096     -170.05    -67.68
REMARK 500    HIS B1097       84.70     75.49
REMARK 500    ILE B1103      117.27    -31.63
REMARK 500    ARG B1108      174.83     77.65
REMARK 500    GLN B1112     -167.79    -64.94
REMARK 500    ARG B1124       49.42   -108.80
REMARK 500    ASP B1125       62.97     25.47
REMARK 500    PHE B1130       70.40   -100.14
REMARK 500    ALA B1143       95.11    -63.39
REMARK 500    ARG B1150        9.49    -66.29
REMARK 500    LEU B1151       25.12   -146.25
REMARK 500    MET B1152      -70.70   -143.73
REMARK 500    SER B1155      -86.87   -151.19
REMARK 500    ILE B1165      -76.93   -108.14
REMARK 500    THR B1170      -31.09   -140.08
REMARK 500    HIS B1177      160.99    102.65
REMARK 500    ASN B1178       23.85    112.81
REMARK 500    PHE B1180      -87.09   -132.44
REMARK 500    GLU B1181      105.46     68.19
REMARK 500    MET B1210        3.29    -62.32
REMARK 500    ASN B1211       49.63     76.28
REMARK 500    PRO C   6      123.05    -35.75
REMARK 500    SER C  14     -155.18   -146.80
REMARK 500    ILE C  21     -156.32    -79.89
REMARK 500    LEU C  22       68.65    176.71
REMARK 500    ILE C  38      -76.12    -61.79
REMARK 500    ALA C  39      -70.25    -83.10
REMARK 500    ASP C  47       -6.41   -148.31
REMARK 500    ASP C  76       23.50    -76.73
REMARK 500    GLN C  79       35.69    -85.64
REMARK 500    CYS C  88     -150.54    -71.87
REMARK 500    ASP C  90      -82.93     58.86
REMARK 500    THR C 110      106.10     47.67
REMARK 500    MET C 125        1.51     58.61
REMARK 500    VAL C 142      126.87     60.00
REMARK 500    ARG C 148     -118.58   -106.94
REMARK 500    HIS C 167      124.30    158.56
REMARK 500    ALA C 168        1.94    -58.43
REMARK 500    PRO C 172       24.94    -78.72
REMARK 500    ALA C 173      -97.24    -65.77
REMARK 500    ALA C 174     -111.91    101.04
REMARK 500    ASP C 181       80.68     60.03
REMARK 500    GLN C 195      -38.46   -131.80
REMARK 500    TYR C 209       44.26     71.63
REMARK 500    GLU C 210      114.55   -164.25
REMARK 500    ASN C 214      153.61     70.83
REMARK 500    THR C 227       97.94     68.39
REMARK 500    ASP C 266       16.84    -63.37
REMARK 500    PHE E  29     -171.44    -63.69
REMARK 500    ILE E  30      118.54     93.66
REMARK 500    VAL E  35      -71.70    -92.07
REMARK 500    GLU E  36       30.00    -61.92
REMARK 500    LYS E  56      -48.47    -28.63
REMARK 500    MET E  57       57.32   -100.80
REMARK 500    PHE E  60      158.61    177.22
REMARK 500    GLU E  66       33.00    -70.98
REMARK 500    ASP E  74      -45.95   -135.36
REMARK 500    PHE E  96      -16.42   -162.62
REMARK 500    ASN E 104       64.17     61.31
REMARK 500    PRO E 125       70.00   -102.59
REMARK 500    ALA E 130       90.47    -44.36
REMARK 500    ALA E 139     -109.37     66.76
REMARK 500    VAL E 141      -88.35     71.50
REMARK 500    HIS E 146       37.18    -83.78
REMARK 500    LEU E 165       40.54    -75.56
REMARK 500    LYS E 166      -33.99   -163.46
REMARK 500    GLN E 174        6.40    -55.25
REMARK 500    PRO F  75     -173.78    -65.98
REMARK 500    ASP F  77     -156.51    -92.81
REMARK 500    THR F  81     -175.99    -66.68
REMARK 500    ASN F 104       75.42    -28.23
REMARK 500    PRO F 106      133.06    -33.12
REMARK 500    ASP F 110       94.75    -63.40
REMARK 500    LEU F 111       97.81    -61.74
REMARK 500    GLU F 112       40.02    -72.32
REMARK 500    PRO F 117       -9.45    -54.96
REMARK 500    LYS F 128       77.37    -51.41
REMARK 500    PRO F 139      -54.35    -29.52
REMARK 500    ASP F 145     -113.09    -77.51
REMARK 500    TRP F 146      121.39     88.34
REMARK 500    PHE H   6      -89.88   -134.52
REMARK 500    ASP H   7      131.64     74.71
REMARK 500    VAL H  23      100.31     62.55
REMARK 500    THR H  32      -57.16     77.07
REMARK 500    CYS H  36      135.84    178.16
REMARK 500    LEU H  55     -168.03   -121.66
REMARK 500    ILE H  59      -74.80   -101.38
REMARK 500    ALA H  60     -175.28     65.84
REMARK 500    SER H  61       22.59   -155.00
REMARK 500    SER H  62      -65.26   -152.46
REMARK 500    ARG H  77       99.05     31.19
REMARK 500    PRO H  81     -165.54    -71.92
REMARK 500    PRO H  82      -85.44    -66.20
REMARK 500    GLN H  83       -3.16     88.50
REMARK 500    ALA H  84       97.48      9.93
REMARK 500    ASP H  86       27.59     84.64
REMARK 500    ARG H  87       40.12    -77.45
REMARK 500    SER H  88      178.66     59.59
REMARK 500    LEU H  89      -39.68    126.86
REMARK 500    ALA H  90     -114.84   -126.26
REMARK 500    ASP H  91      -56.94     54.83
REMARK 500    ASP H  94      -62.25    -93.00
REMARK 500    TYR H 102     -116.19   -140.71
REMARK 500    GLU H 105     -156.23    -96.20
REMARK 500    GLU H 106      152.44    174.26
REMARK 500    VAL H 107      -18.01   -167.34
REMARK 500    SER H 108      -66.65   -126.59
REMARK 500    LYS H 109      -63.45   -145.25
REMARK 500    ASP H 110       79.24     46.12
REMARK 500    ILE H 112      122.63    101.03
REMARK 500    ARG H 130     -123.58     49.86
REMARK 500    ASN H 131      -65.66   -172.99
REMARK 500    LEU H 132      -19.59     75.95
REMARK 500    ALA H 140      111.56    172.80
REMARK 500    THR I   3      105.02     74.10
REMARK 500    PHE I   4      -10.60    102.96
REMARK 500    PHE I   6     -169.81   -110.68
REMARK 500    CYS I  10      -45.15   -139.84
REMARK 500    ASN I  11       98.31     84.92
REMARK 500    ASN I  12     -158.97   -164.09
REMARK 500    GLU I  18      145.61     89.58
REMARK 500    ASP I  19       70.70     60.38
REMARK 500    LYS I  20       91.38     53.68
REMARK 500    GLU I  21      106.06     40.57
REMARK 500    ASN I  22      -24.51     93.07
REMARK 500    ASN I  23       88.19     67.44
REMARK 500    ARG I  24     -176.32   -171.29
REMARK 500    LEU I  25      118.72   -165.32
REMARK 500    LEU I  26       46.78    112.00
REMARK 500    CYS I  29     -153.38    -95.63
REMARK 500    THR I  31      -20.66   -140.74
REMARK 500    CYS I  32       31.40    -79.71
REMARK 500    TYR I  34      100.65     75.90
REMARK 500    PRO I  41      127.11    -36.20
REMARK 500    LEU I  42      163.46     61.63
REMARK 500    HIS I  46      -78.45    163.76
REMARK 500    GLU I  47      135.94     56.42
REMARK 500    VAL I  59     -158.93    -91.98
REMARK 500    SER I  71     -144.65   -124.10
REMARK 500    ASP I  72       -4.61   -147.21
REMARK 500    SER I  80       93.91     68.87
REMARK 500    PHE I  86     -156.95   -158.29
REMARK 500    GLN I  90       56.84    -92.01
REMARK 500    ARG I  92     -121.29   -139.22
REMARK 500    LYS I  93      -78.94   -100.82
REMARK 500    CYS I 106      -32.08   -138.51
REMARK 500    ASP I 113       99.09    -57.28
REMARK 500    LYS I 117     -166.10     54.54
REMARK 500    ARG I 118      117.32     84.24
REMARK 500    THR I 119       35.16    -79.88
REMARK 500    ILE J   2      113.64     72.06
REMARK 500    ARG J   6     -175.72     59.19
REMARK 500    SER J   9      -75.76    -71.03
REMARK 500    CYS J  10      -80.19    -63.41
REMARK 500    TYR J  21      -71.23    -59.26
REMARK 500    GLU J  29      101.72     62.68
REMARK 500    GLU K   8       37.35    -73.43
REMARK 500    PHE K  10      -29.52   -153.27
REMARK 500    HIS K  40       41.48    -73.75
REMARK 500    ALA K  59      118.25   -161.50
REMARK 500    HIS K  65      114.03   -167.42
REMARK 500    PRO K  66      -17.05    -37.60
REMARK 500    ALA K  69       77.94    -69.78
REMARK 500    THR L  26       66.03      9.50
REMARK 500    LYS L  28      -54.35   -131.35
REMARK 500    ALA L  32      -72.19    -61.98
REMARK 500    SER L  35      105.00    -45.30
REMARK 500    SER L  41      -90.33   -114.20
REMARK 500    ARG L  42      -88.14    -93.13
REMARK 500    ASP L  44        8.04   -161.86
REMARK 500    ALA L  45     -143.32     55.39
REMARK 500    ILE L  55      -71.27    -44.72
REMARK 500    LEU L  56      103.94     60.57
REMARK 500    ALA L  59      -95.96     50.56
REMARK 500    ALA L  69       47.84    -89.69
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 HIS A  451     LYS A  452                  144.84
REMARK 500 ASP A  974     HIS A  975                 -146.45
REMARK 500 ALA A 1068     ALA A 1069                  149.80
REMARK 500 ALA A 1069     GLN A 1070                  -44.40
REMARK 500 GLN A 1070     SER A 1071                 -146.97
REMARK 500 MET A 1079     THR A 1080                  140.16
REMARK 500 PHE A 1084     HIS A 1085                  -36.22
REMARK 500 ASP A 1155     PRO A 1156                 -143.66
REMARK 500 ASP A 1157     PRO A 1158                 -132.42
REMARK 500 ASN B 1176     HIS B 1177                 -142.93
REMARK 500 ASN H  128     TYR H  129                  148.62
REMARK 500 ARG H  130     ASN H  131                  146.20
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 A1735  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A  67   SG
REMARK 620 2 CYS A  70   SG  105.1
REMARK 620 3 HIS A  80   NE2 115.5  85.0
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN A1734  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 MET A 108   SD
REMARK 620 2 CYS A 110   SG   99.4
REMARK 620 3 CYS A 167   SG   90.4 134.1
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A2002  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 481   OD1
REMARK 620 2 ASP A 483   OD1 108.6
REMARK 620 3 ASP B 837   OD1  89.3 130.9
REMARK 620 4 UTP B3000   O3G 125.7  91.1 115.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              MG A2001  MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 483   OD1
REMARK 620 2 ASP A 485   OD1  99.9
REMARK 620 N                    1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN B1307  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1166   SG
REMARK 620 2 CYS B1182   SG  163.3
REMARK 620 3 CYS B1185   SG   49.1 133.8
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN C 319  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C  86   SG
REMARK 620 2 CYS C  88   SG  117.3
REMARK 620 3 CYS C  92   SG   84.4 103.4
REMARK 620 4 CYS C  95   SG  110.6 131.8  75.0
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN I 203  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I  10   SG
REMARK 620 2 CYS I  29   SG   92.1
REMARK 620 3 CYS I  32   SG  127.4 133.5
REMARK 620 N                    1     2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN I 204  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS I  75   SG
REMARK 620 2 CYS I  78   SG   98.2
REMARK 620 3 CYS I 103   SG  108.2 115.5
REMARK 620 4 CYS I 106   SG  135.8  51.3  69.9
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN J 101  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS J   7   SG
REMARK 620 2 CYS J  10   SG  113.4
REMARK 620 3 CYS J  45   SG  145.8  92.7
REMARK 620 4 CYS J  46   SG  121.7  51.3  58.3
REMARK 620 N                    1     2     3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL
REMARK 620                              ZN L 105  ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS L  34   SG
REMARK 620 2 CYS L  48   SG  135.9
REMARK 620 3 CYS L  51   SG   83.4  56.1
REMARK 620 N                    1     2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1734
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1735
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1307
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 319
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 203
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 204
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 101
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 105
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2001
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2002
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UTP B 3000
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R9S   RELATED DB: PDB
REMARK 900 RELATED ID: 1R9T   RELATED DB: PDB
REMARK 900 RELATED ID: 1SFO   RELATED DB: PDB
REMARK 900 RELATED ID: 2E2H   RELATED DB: PDB
REMARK 900 RELATED ID: 2E2I   RELATED DB: PDB
REMARK 900 RELATED ID: 2E2J   RELATED DB: PDB
REMARK 900 RELATED ID: 2NVQ   RELATED DB: PDB
REMARK 900 RELATED ID: 2NVS   RELATED DB: PDB
REMARK 900 RELATED ID: 2NVT   RELATED DB: PDB
REMARK 900 RELATED ID: 2NVX   RELATED DB: PDB
REMARK 900 RELATED ID: 2NVY   RELATED DB: PDB
DBREF  2NVZ A    1  1733  UNP    P04050   RPB1_YEAST       1   1733
DBREF  2NVZ B    1  1224  UNP    P08518   RPB2_YEAST       1   1224
DBREF  2NVZ C    1   318  UNP    P16370   RPB3_YEAST       1    318
DBREF  2NVZ E    1   215  UNP    P20434   RPB5_YEAST       1    215
DBREF  2NVZ F    1   155  UNP    P20435   RPB6_YEAST       1    155
DBREF  2NVZ H    1   146  UNP    P20436   RPB8_YEAST       1    146
DBREF  2NVZ I    1   122  UNP    P27999   RPB9_YEAST       1    122
DBREF  2NVZ J    1    70  UNP    P22139   RPAB5_YEAST      1     70
DBREF  2NVZ K    1   120  UNP    P38902   RPB11_YEAST      1    120
DBREF  2NVZ L    1    70  UNP    P40422   RPAB4_YEAST      1     70
DBREF  2NVZ R    1    10  PDB    2NVZ     2NVZ             1     10
DBREF  2NVZ T    1    28  PDB    2NVZ     2NVZ             1     28
DBREF  2NVZ N    1    14  PDB    2NVZ     2NVZ             1     14
SEQRES   1 R   10    A   U   C   G   A   G   A   G   G   A
SEQRES   1 T   28   DC  DT  DA  DC  DC  DG  DA  DT  DA  DA  DG  DC  DA
SEQRES   2 T   28   DG  DA  DC  DG  DA  DT  DC  DC  DT  DC  DT  DC  DG
SEQRES   3 T   28   DA  DT
SEQRES   1 N   14   DC  DT  DG  DC  DT  DT  DA  DT  DC  DG  DG  DT  DA
SEQRES   2 N   14   DG
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     ZN  A1734       1
HET     ZN  A1735       1
HET     ZN  B1307       1
HET     ZN  C 319       1
HET     ZN  I 203       1
HET     ZN  I 204       1
HET     ZN  J 101       1
HET     ZN  L 105       1
HET     MG  A2001       1
HET     MG  A2002       1
HET    UTP  B3000      29
HETNAM      ZN ZINC ION
HETNAM      MG MAGNESIUM ION
HETNAM     UTP URIDINE 5'-TRIPHOSPHATE
FORMUL  14   ZN    8(ZN 2+)
FORMUL  22   MG    2(MG 2+)
FORMUL  24  UTP    C9 H15 N2 O15 P3
HELIX    1   1 SER A   23  SER A   31  1                                   9
HELIX    2   2 HIS A   92  GLY A   94  5                                   3
HELIX    3   3 PHE A   95  GLU A  104  1                                  10
HELIX    4   4 ARG A  134  TRP A  139  1                                   6
HELIX    5   5 THR A  140  CYS A  142  5                                   3
HELIX    6   6 SER A  203  HIS A  213  1                                  11
HELIX    7   7 VAL A  216  LEU A  222  1                                   7
HELIX    8   8 PRO A  243  ARG A  247  5                                   5
HELIX    9   9 LEU A  262  SER A  275  1                                  14
HELIX   10  10 ALA A  292  TYR A  303  1                                  12
HELIX   11  11 ILE A  325  LYS A  330  1                                   6
HELIX   12  12 GLY A  334  LEU A  340  1                                   7
HELIX   13  13 PRO A  367  LYS A  372  1                                   6
HELIX   14  14 ASN A  384  GLY A  395  1                                  12
HELIX   15  15 SER A  494  GLN A  503  1                                  10
HELIX   16  16 ALA A  506  ILE A  511  5                                   6
HELIX   17  17 GLN A  525  LEU A  536  1                                  12
HELIX   18  18 LEU A  543  TYR A  551  1                                   9
HELIX   19  19 GLY A  574  SER A  579  1                                   6
HELIX   20  20 GLY A  628  GLU A  636  1                                   9
HELIX   21  21 GLY A  638  GLY A  661  1                                  24
HELIX   22  22 GLY A  665  THR A  669  5                                   5
HELIX   23  23 ASP A  672  THR A  675  5                                   4
HELIX   24  24 MET A  676  LYS A  689  1                                  14
HELIX   25  25 LYS A  689  GLN A  698  1                                  10
HELIX   26  26 ASP A  716  ALA A  733  1                                  18
HELIX   27  27 ASN A  741  ALA A  749  1                                   9
HELIX   28  28 SER A  754  ALA A  763  1                                  10
HELIX   29  29 SER A  793  GLY A  798  1                                   6
HELIX   30  30 THR A  809  THR A  827  1                                  19
HELIX   31  31 VAL A  829  GLU A  846  1                                  18
HELIX   32  32 ILE A  867  ASP A  871  5                                   5
HELIX   33  33 ASP A  874  ALA A  876  5                                   3
HELIX   34  34 SER A  889  ARG A  898  1                                  10
HELIX   35  35 SER A  915  LEU A  920  1                                   6
HELIX   36  36 LEU A  928  PHE A  947  1                                  20
HELIX   37  37 ASN A  959  PHE A  971  1                                  13
HELIX   38  38 THR A  982  GLN A  994  1                                  13
HELIX   39  39 ASN A 1004  LEU A 1026  1                                  23
HELIX   40  40 ALA A 1027  LEU A 1032  1                                   6
HELIX   41  41 THR A 1038  LEU A 1054  1                                  17
HELIX   42  42 MET A 1063  ALA A 1069  1                                   7
HELIX   43  43 ILE A 1072  THR A 1080  1                                   9
HELIX   44  44 GLY A 1097  VAL A 1107  1                                  11
HELIX   45  45 GLN A 1130  SER A 1136  1                                   7
HELIX   46  46 LEU A 1143  THR A 1147  5                                   5
HELIX   47  47 ASP A 1198  ASN A 1203  1                                   6
HELIX   48  48 THR A 1208  ILE A 1216  1                                   9
HELIX   49  49 LYS A 1217  PHE A 1220  5                                   4
HELIX   50  50 GLU A 1256  GLU A 1269  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  ALA A 1357  1                                  18
HELIX   54  54 TYR A 1365  THR A 1377  1                                  13
HELIX   55  55 GLY A 1395  SER A 1401  1                                   7
HELIX   56  56 THR A 1405  SER A 1415  1                                  11
HELIX   57  57 GLY A 1423  LEU A 1430  1                                   8
HELIX   58  58 ASP B   29  GLU B   40  1                                  12
HELIX   59  59 GLN B   46  ASP B   56  1                                  11
HELIX   60  60 TYR B   57  GLU B   65  1                                   9
HELIX   61  61 TYR B  113  ASN B  121  1                                   9
HELIX   62  62 CYS B  179  GLU B  183  5                                   5
HELIX   63  63 THR B  185  LEU B  192  1                                   8
HELIX   64  64 PRO B  281  ALA B  288  1                                   8
HELIX   65  65 ASP B  307  LEU B  314  1                                   8
HELIX   66  66 LEU B  314  PHE B  322  1                                   9
HELIX   67  67 ALA B  352  GLN B  357  1                                   6
HELIX   68  68 GLU B  371  ASP B  391  1                                  21
HELIX   69  69 HIS B  400  GLY B  402  5                                   3
HELIX   70  70 LEU B  408  VAL B  436  1                                  29
HELIX   71  71 ALA B  450  GLY B  464  1                                  15
HELIX   72  72 THR B  487  ARG B  496  1                                  10
HELIX   73  73 HIS B  515  TRP B  519  5                                   5
HELIX   74  74 PRO B  551  SER B  559  1                                   9
HELIX   75  75 PRO B  593  ARG B  605  1                                  13
HELIX   76  76 ARG B  654  GLN B  667  1                                  14
HELIX   77  77 THR B  680  GLU B  687  1                                   8
HELIX   78  78 ASP B  694  GLU B  699  1                                   6
HELIX   79  79 HIS B  744  LEU B  749  5                                   6
HELIX   80  80 GLY B  750  ILE B  755  1                                   6
HELIX   81  81 PHE B  758  ASN B  762  5                                   5
HELIX   82  82 GLN B  763  LYS B  775  1                                  13
HELIX   83  83 LEU B  782  ARG B  788  5                                   7
HELIX   84  84 THR B  806  TYR B  811  5                                   6
HELIX   85  85 ASN B  842  GLY B  849  1                                   8
HELIX   86  86 THR B 1022  GLY B 1039  1                                  18
HELIX   87  87 THR B 1051  ARG B 1060  1                                  10
HELIX   88  88 MET B 1098  ILE B 1103  1                                   6
HELIX   89  89 GLY B 1121  ASP B 1125  5                                   5
HELIX   90  90 GLY B 1131  HIS B 1141  1                                  11
HELIX   91  91 SER B 1145  ARG B 1150  1                                   6
HELIX   92  92 PRO B 1197  ASN B 1211  1                                  15
HELIX   93  93 ASP C   26  ILE C   38  1                                  13
HELIX   94  94 ALA C   59  ILE C   70  1                                  12
HELIX   95  95 SER C   74  LEU C   80  5                                   7
HELIX   96  96 HIS C  167  GLY C  171  5                                   5
HELIX   97  97 PRO C  239  THR C  263  1                                  25
HELIX   98  98 GLN C  264  ASP C  268  5                                   5
HELIX   99  99 GLU E    6  ARG E   11  1                                   6
HELIX  100 100 TRP E   13  ARG E   26  1                                  14
HELIX  101 101 PRO E   38  ALA E   44  1                                   7
HELIX  102 102 ARG E   55  SER E   59  5                                   5
HELIX  103 103 GLU E   67  LYS E   71  5                                   5
HELIX  104 104 PHE E   96  LYS E  103  1                                   8
HELIX  105 105 SER E  157  TYR E  168  1                                  12
HELIX  106 106 ASP E  182  LEU E  188  1                                   7
HELIX  107 107 THR F   86  MET F  103  1                                  18
HELIX  108 108 LEU F  118  GLU F  127  1                                  10
HELIX  109 109 GLN I   60  SER I   64  5                                   5
HELIX  110 110 ASP J   16  GLU J   27  1                                  12
HELIX  111 111 ASP J   31  LEU J   39  1                                   9
HELIX  112 112 ARG J   43  THR J   52  1                                  10
HELIX  113 113 LEU J   56  ARG J   62  1                                   7
HELIX  114 114 THR K   41  ILE K   46  1                                   6
HELIX  115 115 ASP K   82  ASN K  110  1                                  29
SHEET    1   A 3 LEU A1418  ASP A1419  0
SHEET    2   A 3 GLU A  16  GLN A  18 -1  N  VAL A  17   O  ASP A1419
SHEET    3   A 3 ARG B1215  TYR B1217 -1  O  ARG B1215   N  GLN A  18
SHEET    1   B 2 GLY A  82  VAL A  90  0
SHEET    2   B 2 LEU A 236  VAL A 241 -1  O  VAL A 241   N  GLY A  82
SHEET    1   C 3 THR A 173  LYS A 176  0
SHEET    2   C 3 LEU A 181  SER A 184 -1  O  VAL A 182   N  ARG A 175
SHEET    3   C 3 VAL A 201  LEU A 202 -1  O  LEU A 202   N  LEU A 181
SHEET    1   D 2 LYS A 343  VAL A 345  0
SHEET    2   D 2 LEU B1128  PHE B1130 -1  O  PHE B1130   N  LYS A 343
SHEET    1   E 6 GLN A 363  VAL A 364  0
SHEET    2   E 6 MET A 455  VAL A 460  1  O  ARG A 459   N  VAL A 364
SHEET    3   E 6 PRO A 441  ASN A 445 -1  N  PHE A 444   O  MET A 456
SHEET    4   E 6 GLU A 486  HIS A 490 -1  O  ASN A 488   N  ASN A 445
SHEET    5   E 6 SER A 348  GLY A 355 -1  N  THR A 351   O  MET A 487
SHEET    6   E 6 PHE A 468  LEU A 470  1  O  PHE A 468   N  VAL A 352
SHEET    1   F 6 GLN A 363  VAL A 364  0
SHEET    2   F 6 MET A 455  VAL A 460  1  O  ARG A 459   N  VAL A 364
SHEET    3   F 6 PRO A 441  ASN A 445 -1  N  PHE A 444   O  MET A 456
SHEET    4   F 6 GLU A 486  HIS A 490 -1  O  ASN A 488   N  ASN A 445
SHEET    5   F 6 SER A 348  GLY A 355 -1  N  THR A 351   O  MET A 487
SHEET    6   F 6 HIS B1104  ARG B1106 -1  O  ARG B1106   N  SER A 348
SHEET    1   G 2 VAL A 405  ILE A 406  0
SHEET    2   G 2 ARG A 412  ILE A 413 -1  O  ILE A 413   N  VAL A 405
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 2 MET A 605  ILE A 608  0
SHEET    2   I 2 GLN A 611  GLY A 615 -1  O  GLN A 611   N  ILE A 608
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 2 SER A 769  VAL A 770  0
SHEET    2   K 2 LYS A 773  ARG A 774 -1  O  LYS A 773   N  VAL A 770
SHEET    1   L 3 MET A 849  VAL A 850  0
SHEET    2   L 3 THR A 856  ARG A 857 -1  O  ARG A 857   N  MET A 849
SHEET    3   L 3 VAL A 863  GLN A 865 -1  O  ILE A 864   N  THR A 856
SHEET    1   M 2 ILE A 878  SER A 882  0
SHEET    2   M 2 ASN A 953  PRO A 957 -1  O  LEU A 956   N  GLU A 879
SHEET    1   N 4 VAL A1282  PRO A1292  0
SHEET    2   N 4 TYR A1298  ASP A1309 -1  O  VAL A1305   N  MET A1285
SHEET    3   N 4 SER A1115  TYR A1119 -1  N  LEU A1116   O  THR A1308
SHEET    4   N 4 TYR A1328  THR A1329 -1  O  TYR A1328   N  THR A1117
SHEET    1   O 2 ILE A1227  TRP A1228  0
SHEET    2   O 2 ILE A1238  ARG A1239 -1  O  ARG A1239   N  ILE A1227
SHEET    1   P 3 ASP A1442  MET A1444  0
SHEET    2   P 3 VAL F 133  LEU F 138 -1  O  ARG F 135   N  ASP A1442
SHEET    3   P 3 GLY F 141  GLU F 144 -1  O  GLY F 141   N  LEU F 138
SHEET    1   Q 3 ILE B  95  VAL B  97  0
SHEET    2   Q 3 SER B 125  VAL B 130 -1  O  PHE B 129   N  TYR B  96
SHEET    3   Q 3 VAL B 165  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  SER B 208   N  ILE B 205
SHEET    3   R 3 SER B 480  GLN B 481 -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  ARG B 497   N  ALA B 214
SHEET    4   S 4 LYS B 537  ASN B 538 -1  O  LYS B 537   N  THR B 498
SHEET    1   T 4 VAL B 223  PHE B 226  0
SHEET    2   T 4 ILE B 234  SER B 242 -1  O  VAL B 237   N  PHE B 226
SHEET    3   T 4 SER B 252  TYR B 259 -1  O  VAL B 256   N  ALA B 238
SHEET    4   T 4 ILE B 269  THR B 272 -1  O  THR B 272   N  GLN B 255
SHEET    1   U 2 CYS B 544  ILE B 545  0
SHEET    2   U 2 VAL B 633  TYR B 634 -1  O  TYR B 634   N  CYS B 544
SHEET    1   V 4 TRP B 586  HIS B 590  0
SHEET    2   V 4 THR B 578  VAL B 582 -1  N  VAL B 580   O  GLY B 588
SHEET    3   V 4 GLU B 623  PHE B 627  1  O  LEU B 624   N  PHE B 581
SHEET    4   V 4 SER B 614  ASP B 618 -1  N  ILE B 616   O  LYS B 625
SHEET    1   W 2 VAL B 640  GLU B 641  0
SHEET    2   W 2 GLU B 650  LEU B 651 -1  O  GLU B 650   N  GLU B 641
SHEET    1   X 2 ILE B 703  ALA B 704  0
SHEET    2   X 2 HIS B 740  CYS B 741  1  O  HIS B 740   N  ALA B 704
SHEET    1   Y 5 ASN B 794  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  VAL B 968   N  ARG B 857
SHEET    4   Y 5 ASN B 946  THR B 956 -1  N  ILE B 948   O  ARG B 969
SHEET    5   Y 5 ARG B 904  SER B 906 -1  N  VAL B 905   O  GLY B 947
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 3 GLY B 820  GLN B 821  0
SHEET    2  AA 3 TYR B1092  ARG B1094 -1  O  TYR B1092   N  GLN B 821
SHEET    3  AA 3 PHE B 980  SER B 982 -1  N  ALA B 981   O  GLN B1093
SHEET    1  AB 6 THR B 989  THR B 993  0
SHEET    2  AB 6 SER B 838  MET B 841  1  N  MET B 839   O  THR B 989
SHEET    3  AB 6 LEU B1010  ILE B1012 -1  O  ILE B1011   N  ILE B 840
SHEET    4  AB 6 ILE B 824  ILE B 827  1  N  ALA B 826   O  LEU B1010
SHEET    5  AB 6 ILE B1085  PRO B1089 -1  O  GLY B1088   N  VAL B 825
SHEET    6  AB 6 PHE B1069  GLU B1070 -1  N  GLU B1070   O  ILE B1085
SHEET    1  AC 2 THR B 873  PHE B 874  0
SHEET    2  AC 2 LYS B 914  THR B 915 -1  O  THR B 915   N  THR B 873
SHEET    1  AD 2 PHE B1001  THR B1002  0
SHEET    2  AD 2 MET B1072  TYR B1073 -1  O  TYR B1073   N  PHE B1001
SHEET    1  AE 2 ARG B1159  CYS B1163  0
SHEET    2  AE 2 ILE B1191  HIS B1195 -1  O  TYR B1192   N  ILE B1162
SHEET    1  AF 4 ILE C  10  ALA C  13  0
SHEET    2  AF 4 ASN C  17  PHE C  20 -1  O  ASP C  19   N  GLU C  12
SHEET    3  AF 4 MET C 230  GLU C 233 -1  O  MET C 230   N  PHE C  20
SHEET    4  AF 4 ILE C 176  GLU C 177 -1  N  GLU C 177   O  ASN C 231
SHEET    1  AG 4 THR C  53  ASN C  54  0
SHEET    2  AG 4 GLU C 152  LYS C 154 -1  O  LYS C 154   N  THR C  53
SHEET    3  AG 4 VAL C  97  PHE C 104 -1  N  ALA C 103   O  LEU C 153
SHEET    4  AG 4 LEU C 118  ILE C 120 -1  O  VAL C 119   N  THR C 100
SHEET    1  AH 6 THR C  53  ASN C  54  0
SHEET    2  AH 6 GLU C 152  LYS C 154 -1  O  LYS C 154   N  THR C  53
SHEET    3  AH 6 VAL C  97  PHE C 104 -1  N  ALA C 103   O  LEU C 153
SHEET    4  AH 6 CYS C 157  ILE C 163 -1  O  CYS C 157   N  LEU C  99
SHEET    5  AH 6 PRO C  42  VAL C  51 -1  N  ASP C  47   O  VAL C 158
SHEET    6  AH 6 VAL L  65  GLU L  68 -1  O  PHE L  67   N  VAL C  49
SHEET    1  AI 2 THR C 111  TYR C 114  0
SHEET    2  AI 2 LEU C 143  LEU C 147 -1  O  LEU C 147   N  THR C 111
SHEET    1  AJ 4 PHE E  60  ALA E  62  0
SHEET    2  AJ 4 LEU E  78  VAL E  80 -1  O  LEU E  78   N  ALA E  62
SHEET    3  AJ 4 THR E 107  ILE E 109  1  O  ILE E 109   N  TRP E  79
SHEET    4  AJ 4 THR E 131  GLU E 133  1  O  GLU E 133   N  GLY E 108
SHEET    1  AK 4 HIS E 153  ARG E 155  0
SHEET    2  AK 4 VAL E 196  ARG E 200 -1  O  LYS E 197   N  ILE E 154
SHEET    3  AK 4 TYR E 208  CYS E 214 -1  O  ARG E 212   N  VAL E 196
SHEET    4  AK 4 ARG E 177  ILE E 178  1  N  ILE E 178   O  ILE E 213
SHEET    1  AL 9 TYR H  95  VAL H  96  0
SHEET    2  AL 9 LEU H 143  ILE H 144 -1  O  ILE H 144   N  TYR H  95
SHEET    3  AL 9 SER H  54  THR H  58 -1  N  THR H  58   O  LEU H 143
SHEET    4  AL 9 ILE H   9  VAL H  15 -1  N  PHE H  10   O  LEU H  55
SHEET    5  AL 9 ILE H  26  SER H  30 -1  O  GLU H  27   N  SER H  13
SHEET    6  AL 9 LYS H  37  LEU H  40 -1  O  LEU H  38   N  ALA H  28
SHEET    7  AL 9 LEU H 121  GLU H 126 -1  O  ARG H 124   N  THR H  39
SHEET    8  AL 9 ALA H 113  PHE H 118 -1  N  PHE H 118   O  LEU H 121
SHEET    9  AL 9 THR H 100  ALA H 101 -1  N  THR H 100   O  SER H 117
SHEET    1  AM 3 TYR I  15  PRO I  16  0
SHEET    2  AM 3 LEU I  26  GLU I  28 -1  O  GLU I  28   N  TYR I  15
SHEET    3  AM 3 VAL I  35  GLU I  37 -1  O  GLU I  36   N  PHE I  27
SHEET    1  AN 3 ASN I  83  GLN I  87  0
SHEET    2  AN 3 LEU I  99  CYS I 103 -1  O  VAL I 102   N  VAL I  84
SHEET    3  AN 3 ILE I 109  PHE I 110 -1  O  PHE I 110   N  PHE I 101
SHEET    1  AO 4 LEU K  19  PRO K  23  0
SHEET    2  AO 4 ALA K  30  PHE K  35 -1  O  VAL K  32   N  ASP K  22
SHEET    3  AO 4 PHE K  71  THR K  77 -1  O  LEU K  73   N  ILE K  33
SHEET    4  AO 4 VAL K  56  VAL K  63 -1  N  ALA K  60   O  ARG K  74
SHEET    1  AP 2 TYR L  29  ILE L  30  0
SHEET    2  AP 2 LYS L  37  LEU L  38 -1  O  LEU L  38   N  TYR L  29
SSBOND   1 CYS A   70    CYS A   77                          1555   1555  2.04
SSBOND   2 CYS B 1166    CYS B 1185                          1555   1555  2.02
SSBOND   3 CYS C   92    CYS C   95                          1555   1555  2.85
SSBOND   4 CYS I   78    CYS I  106                          1555   1555  2.02
SSBOND   5 CYS I  103    CYS I  106                          1555   1555  2.67
SSBOND   6 CYS J   10    CYS J   46                          1555   1555  2.02
SSBOND   7 CYS J   45    CYS J   46                          1555   1555  2.29
SSBOND   8 CYS L   48    CYS L   51                          1555   1555  2.04
LINK         SG  CYS A  67                ZN    ZN A1735     1555   1555  2.35
LINK         SG  CYS A  70                ZN    ZN A1735     1555   1555  2.34
LINK         NE2 HIS A  80                ZN    ZN A1735     1555   1555  2.37
LINK         SD  MET A 108                ZN    ZN A1734     1555   1555  2.96
LINK         SG  CYS A 110                ZN    ZN A1734     1555   1555  2.35
LINK         SG  CYS A 167                ZN    ZN A1734     1555   1555  2.34
LINK         OD1 ASP A 481                MG    MG A2002     1555   1555  2.21
LINK         OD1 ASP A 483                MG    MG A2001     1555   1555  2.20
LINK         OD1 ASP A 483                MG    MG A2002     1555   1555  2.21
LINK         OD1 ASP A 485                MG    MG A2001     1555   1555  2.18
LINK         OD1 ASP B 837                MG    MG A2002     1555   1555  2.21
LINK         SG  CYS B1166                ZN    ZN B1307     1555   1555  2.33
LINK         SG  CYS B1182                ZN    ZN B1307     1555   1555  2.35
LINK         SG  CYS B1185                ZN    ZN B1307     1555   1555  2.52
LINK         SG  CYS C  86                ZN    ZN C 319     1555   1555  2.35
LINK         SG  CYS C  88                ZN    ZN C 319     1555   1555  2.34
LINK         SG  CYS C  92                ZN    ZN C 319     1555   1555  2.34
LINK         SG  CYS C  95                ZN    ZN C 319     1555   1555  2.34
LINK         SG  CYS I  10                ZN    ZN I 203     1555   1555  2.33
LINK         SG  CYS I  29                ZN    ZN I 203     1555   1555  2.33
LINK         SG  CYS I  32                ZN    ZN I 203     1555   1555  2.34
LINK         SG  CYS I  75                ZN    ZN I 204     1555   1555  2.34
LINK         SG  CYS I  78                ZN    ZN I 204     1555   1555  2.33
LINK         SG  CYS I 103                ZN    ZN I 204     1555   1555  2.32
LINK         SG  CYS I 106                ZN    ZN I 204     1555   1555  2.34
LINK         SG  CYS J   7                ZN    ZN J 101     1555   1555  2.15
LINK         SG  CYS J  10                ZN    ZN J 101     1555   1555  2.32
LINK         SG  CYS J  45                ZN    ZN J 101     1555   1555  2.35
LINK         SG  CYS J  46                ZN    ZN J 101     1555   1555  2.35
LINK         SG  CYS L  34                ZN    ZN L 105     1555   1555  2.35
LINK         SG  CYS L  48                ZN    ZN L 105     1555   1555  1.91
LINK         SG  CYS L  51                ZN    ZN L 105     1555   1555  2.34
LINK        MG    MG A2002                 O3G UTP B3000     1555   1555  2.00
CISPEP   1 GLY A    3    GLN A    4          0         2.82
CISPEP   2 PRO A   38    GLU A   39          0         5.46
CISPEP   3 THR A   44    GLN A   45          0        -0.35
CISPEP   4 PRO A   56    ARG A   57          0         5.34
CISPEP   5 GLU A  254    SER A  255          0        10.11
CISPEP   6 GLN A  256    ARG A  257          0        -6.57
CISPEP   7 ASN A  282    GLY A  283          0        -1.61
CISPEP   8 ALA A  288    ILE A  289          0        -4.12
CISPEP   9 ARG A  320    PRO A  321          0         4.17
CISPEP  10 GLN A  447    PRO A  448          0         2.46
CISPEP  11 LYS A  637    GLY A  638          0         0.89
CISPEP  12 ALA A  699    ASN A  700          0        -4.44
CISPEP  13 LEU A  701    LEU A  702          0        -6.84
CISPEP  14 GLY A  707    MET A  708          0       -18.02
CISPEP  15 THR A  709    LEU A  710          0        10.95
CISPEP  16 LEU A  710    ARG A  711          0         0.47
CISPEP  17 GLU A  712    SER A  713          0        -2.61
CISPEP  18 ILE A  973    ASP A  974          0        -1.66
CISPEP  19 HIS A  975    THR A  976          0        11.77
CISPEP  20 SER A 1071    ILE A 1072          0         8.50
CISPEP  21 ASN A 1082    THR A 1083          0         6.45
CISPEP  22 THR A 1083    PHE A 1084          0        17.00
CISPEP  23 HIS A 1085    PHE A 1086          0         7.43
CISPEP  24 GLY A 1088    VAL A 1089          0         4.78
CISPEP  25 VAL A 1089    ALA A 1090          0        -2.80
CISPEP  26 SER A 1091    LYS A 1092          0        10.30
CISPEP  27 LYS A 1092    LYS A 1093          0       -28.07
CISPEP  28 LYS A 1093    VAL A 1094          0         3.87
CISPEP  29 SER A 1096    GLY A 1097          0         2.68
CISPEP  30 ILE A 1152    TYR A 1153          0       -21.27
CISPEP  31 ARG A 1159    SER A 1160          0        -1.71
CISPEP  32 VAL A 1162    ILE A 1163          0         0.14
CISPEP  33 GLU A 1167    GLU A 1168          0        -8.47
CISPEP  34 ILE A 1170    GLN A 1171          0         2.03
CISPEP  35 TRP A 1191    LEU A 1192          0         7.58
CISPEP  36 LEU A 1197    ASP A 1198          0         6.92
CISPEP  37 ALA A 1200    ALA A 1201          0        -9.12
CISPEP  38 ILE A 1227    TRP A 1228          0        12.15
CISPEP  39 LEU A 1236    ILE A 1237          0        -0.58
CISPEP  40 GLU B  183    ALA B  184          0       -20.28
CISPEP  41 LYS B  227    LYS B  228          0        13.03
CISPEP  42 PRO B  231    SER B  232          0        -6.40
CISPEP  43 PRO B  293    ASP B  294          0        12.87
CISPEP  44 ARG B  327    GLU B  328          0        21.70
CISPEP  45 GLU B  328    THR B  329          0         5.40
CISPEP  46 GLN B  350    TYR B  351          0         9.83
CISPEP  47 ASP B  391    ARG B  392          0         6.42
CISPEP  48 PRO B  571    HIS B  572          0        -6.30
CISPEP  49 HIS B  572    GLN B  573          0        17.19
CISPEP  50 PRO B  636    LEU B  637          0        -2.73
CISPEP  51 MET B  705    GLN B  706          0        23.83
CISPEP  52 ASP B  709    LEU B  710          0        -2.21
CISPEP  53 GLY B  867    MET B  868          0         7.84
CISPEP  54 MET B  868    SER B  869          0         4.96
CISPEP  55 PRO B  877    GLN B  878          0        12.59
CISPEP  56 THR B  882    LEU B  883          0       -11.59
CISPEP  57 SER B 1019    ARG B 1020          0         1.31
CISPEP  58 LEU B 1175    ASN B 1176          0         0.52
CISPEP  59 HIS B 1177    ASN B 1178          0        -1.16
CISPEP  60 PRO E  128    PRO E  129          0         2.81
CISPEP  61 ALA E  138    ALA E  139          0        -3.90
CISPEP  62 LEU E  140    VAL E  141          0         3.23
CISPEP  63 ALA H   84    GLY H   85          0         4.30
CISPEP  64 GLY H   85    ASP H   86          0        19.68
CISPEP  65 LYS H  109    ASP H  110          0        -3.15
CISPEP  66 ASP H  110    LEU H  111          0         3.39
CISPEP  67 LEU H  111    ILE H  112          0         2.31
CISPEP  68 THR I    3    PHE I    4          0         4.40
CISPEP  69 ARG I   17    GLU I   18          0       -11.54
CISPEP  70 ASP I   19    LYS I   20          0       -10.70
CISPEP  71 LYS I   20    GLU I   21          0        -2.53
CISPEP  72 LEU I   25    LEU I   26          0        -4.95
CISPEP  73 SER I   33    TYR I   34          0         0.91
CISPEP  74 VAL I   43    TYR I   44          0        13.97
CISPEP  75 ARG I   45    HIS I   46          0       -16.99
CISPEP  76 HIS I   79    SER I   80          0        -4.69
CISPEP  77 GLN I  114    LYS I  115          0        -1.34
CISPEP  78 ARG L   42    THR L   43          0         0.60
SITE     1 AC1  3 MET A 108  CYS A 110  CYS A 167
SITE     1 AC2  4 CYS A  67  CYS A  70  CYS A  77  HIS A  80
SITE     1 AC3  4 CYS B1163  CYS B1166  CYS B1182  CYS B1185
SITE     1 AC4  4 CYS C  86  CYS C  88  CYS C  92  CYS C  95
SITE     1 AC5  4 CYS I  10  CYS I  29  ARG I  30  CYS I  32
SITE     1 AC6  5 CYS I  75  CYS I  78  SER I  80  CYS I 103
SITE     2 AC6  5 CYS I 106
SITE     1 AC7  5 CYS J   7  SER J   9  CYS J  10  CYS J  45
SITE     2 AC7  5 CYS J  46
SITE     1 AC8  4 CYS L  31  CYS L  34  CYS L  48  CYS L  51
SITE     1 AC9  5 ASP A 483  ASP A 485   MG A2002  UTP B3000
SITE     2 AC9  5   A R  10
SITE     1 BC1  6 ASP A 481  ASP A 483   MG A2001  ASP B 837
SITE     2 BC1  6 ARG B1020  UTP B3000
SITE     1 BC2 13 ARG A 446  ASP A 481  ASP A 483  ASN A1082
SITE     2 BC2 13 HIS A1085   MG A2001   MG A2002  ARG B 766
SITE     3 BC2 13 ASP B 837  LYS B 987  ARG B1020    A R  10
SITE     4 BC2 13  DA T  18
CRYST1  169.647  222.338  194.316  90.00 101.67  90.00 C 1 2 1       4
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      0.005895  0.000000  0.001217        0.00000
SCALE2      0.000000  0.004498  0.000000        0.00000
SCALE3      0.000000  0.000000  0.005255        0.00000
      
PROCHECK
Go to PROCHECK summary
 References