HEADER TRANSFERASE/DNA/RNA 17-JUN-15 5C44
TITLE CRYSTAL STRUCTURE OF A TRANSCRIBING RNA POLYMERASE II COMPLEX REVEALS
TITLE 2 A COMPLETE TRANSCRIPTION BUBBLE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: RNA POLYMERASE II SUBUNIT B1,DNA-DIRECTED RNA POLYMERASE III
COMPND 5 LARGEST SUBUNIT,RNA POLYMERASE II SUBUNIT B220;
COMPND 6 EC: 2.7.7.6;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB2;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: RNA POLYMERASE II SUBUNIT 2,B150,DNA-DIRECTED RNA POLYMERASE
COMPND 11 II 140 KDA POLYPEPTIDE;
COMPND 12 EC: 2.7.7.6;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3;
COMPND 15 CHAIN: C;
COMPND 16 SYNONYM: RNA POLYMERASE II SUBUNIT B3,B44.5,DNA-DIRECTED RNA
COMPND 17 POLYMERASE II 45 KDA POLYPEPTIDE;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB4;
COMPND 20 CHAIN: D;
COMPND 21 SYNONYM: RNA POLYMERASE II SUBUNIT B4,B32,DNA-DIRECTED RNA POLYMERASE
COMPND 22 II 32 KDA POLYPEPTIDE;
COMPND 23 ENGINEERED: YES;
COMPND 24 MOL_ID: 5;
COMPND 25 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC1;
COMPND 26 CHAIN: E;
COMPND 27 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC1,ABC27,DNA-DIRECTED
COMPND 28 RNA POLYMERASES I,AND III 27 KDA POLYPEPTIDE;
COMPND 29 MOL_ID: 6;
COMPND 30 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC2;
COMPND 31 CHAIN: F;
COMPND 32 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC2,ABC23,DNA-DIRECTED
COMPND 33 RNA POLYMERASES I,AND III 23 KDA POLYPEPTIDE;
COMPND 34 MOL_ID: 7;
COMPND 35 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB7;
COMPND 36 CHAIN: G;
COMPND 37 SYNONYM: RNA POLYMERASE II SUBUNIT B7,B16;
COMPND 38 ENGINEERED: YES;
COMPND 39 MOL_ID: 8;
COMPND 40 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC3;
COMPND 41 CHAIN: H;
COMPND 42 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC3,ABC14.4,ABC14.5,
COMPND 43 DNA-DIRECTED RNA POLYMERASES I,AND III 14.5 KDA POLYPEPTIDE;
COMPND 44 MOL_ID: 9;
COMPND 45 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB9;
COMPND 46 CHAIN: I;
COMPND 47 SYNONYM: RNA POLYMERASE II SUBUNIT B9,B12.6,DNA-DIRECTED RNA
COMPND 48 POLYMERASE II 14.2 KDA POLYPEPTIDE,DNA-DIRECTED RNA POLYMERASE II
COMPND 49 SUBUNIT 9;
COMPND 50 MOL_ID: 10;
COMPND 51 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5;
COMPND 52 CHAIN: J;
COMPND 53 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC5,ABC10-BETA,ABC8,
COMPND 54 DNA-DIRECTED RNA POLYMERASES I,AND III 8.3 KDA POLYPEPTIDE;
COMPND 55 MOL_ID: 11;
COMPND 56 MOLECULE: DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11;
COMPND 57 CHAIN: K;
COMPND 58 SYNONYM: RNA POLYMERASE II SUBUNIT B11,B13.6,DNA-DIRECTED RNA
COMPND 59 POLYMERASE II 13.6 KDA POLYPEPTIDE;
COMPND 60 MOL_ID: 12;
COMPND 61 MOLECULE: DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC4;
COMPND 62 CHAIN: L;
COMPND 63 SYNONYM: RNA POLYMERASES I,II,AND III SUBUNIT ABC4,ABC10-ALPHA;
COMPND 64 MOL_ID: 13;
COMPND 65 MOLECULE: SYNTHETIC RNA;
COMPND 66 CHAIN: R;
COMPND 67 ENGINEERED: YES;
COMPND 68 MOL_ID: 14;
COMPND 69 MOLECULE: SYNTHETIC DNA;
COMPND 70 CHAIN: S;
COMPND 71 ENGINEERED: YES;
COMPND 72 MOL_ID: 15;
COMPND 73 MOLECULE: SYNTHETIC DNA;
COMPND 74 CHAIN: U;
COMPND 75 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 ATCC: 204508;
SOURCE 8 OTHER_DETAILS: CELL;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 11 S288C);
SOURCE 12 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 13 ORGANISM_TAXID: 559292;
SOURCE 14 STRAIN: ATCC 204508 / S288C;
SOURCE 15 ATCC: 204508;
SOURCE 16 OTHER_DETAILS: CELL;
SOURCE 17 MOL_ID: 3;
SOURCE 18 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 19 S288C);
SOURCE 20 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 21 ORGANISM_TAXID: 559292;
SOURCE 22 STRAIN: ATCC 204508 / S288C;
SOURCE 23 ATCC: 204508;
SOURCE 24 OTHER_DETAILS: CELL;
SOURCE 25 MOL_ID: 4;
SOURCE 26 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 27 S288C);
SOURCE 28 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 29 ORGANISM_TAXID: 559292;
SOURCE 30 STRAIN: ATCC 204508 / S288C;
SOURCE 31 ATCC: 204508;
SOURCE 32 GENE: RPB4, YJL140W, J0654;
SOURCE 33 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 34 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 35 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 36 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 37 EXPRESSION_SYSTEM_PLASMID: PET-DUET;
SOURCE 38 MOL_ID: 5;
SOURCE 39 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 40 S288C);
SOURCE 41 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 42 ORGANISM_TAXID: 559292;
SOURCE 43 STRAIN: ATCC 204508 / S288C;
SOURCE 44 OTHER_DETAILS: CELL;
SOURCE 45 MOL_ID: 6;
SOURCE 46 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 47 S288C);
SOURCE 48 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 49 ORGANISM_TAXID: 559292;
SOURCE 50 STRAIN: ATCC 204508 / S288C;
SOURCE 51 OTHER_DETAILS: CELL;
SOURCE 52 MOL_ID: 7;
SOURCE 53 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 54 S288C);
SOURCE 55 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 56 ORGANISM_TAXID: 559292;
SOURCE 57 STRAIN: ATCC 204508 / S288C;
SOURCE 58 GENE: RPB7, YDR404C, D9509.22;
SOURCE 59 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 60 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 61 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 62 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 63 EXPRESSION_SYSTEM_PLASMID: PET-DUET;
SOURCE 64 MOL_ID: 8;
SOURCE 65 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 66 S288C);
SOURCE 67 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 68 ORGANISM_TAXID: 559292;
SOURCE 69 STRAIN: ATCC 204508 / S288C;
SOURCE 70 OTHER_DETAILS: CELL;
SOURCE 71 MOL_ID: 9;
SOURCE 72 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 73 S288C);
SOURCE 74 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 75 ORGANISM_TAXID: 559292;
SOURCE 76 STRAIN: ATCC 204508 / S288C;
SOURCE 77 OTHER_DETAILS: CELL;
SOURCE 78 MOL_ID: 10;
SOURCE 79 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 80 S288C);
SOURCE 81 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 82 ORGANISM_TAXID: 559292;
SOURCE 83 STRAIN: ATCC 204508 / S288C;
SOURCE 84 OTHER_DETAILS: CELL;
SOURCE 85 MOL_ID: 11;
SOURCE 86 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 87 S288C);
SOURCE 88 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 89 ORGANISM_TAXID: 559292;
SOURCE 90 STRAIN: ATCC 204508 / S288C;
SOURCE 91 OTHER_DETAILS: CELL;
SOURCE 92 MOL_ID: 12;
SOURCE 93 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 94 S288C);
SOURCE 95 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 96 ORGANISM_TAXID: 559292;
SOURCE 97 STRAIN: ATCC 204508 / S288C;
SOURCE 98 OTHER_DETAILS: CELL;
SOURCE 99 MOL_ID: 13;
SOURCE 100 SYNTHETIC: YES;
SOURCE 101 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 102 ORGANISM_TAXID: 32630;
SOURCE 103 OTHER_DETAILS: SYNTHETIC RNA OLIGONUCLEOTIDE;
SOURCE 104 MOL_ID: 14;
SOURCE 105 SYNTHETIC: YES;
SOURCE 106 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 107 ORGANISM_TAXID: 32630;
SOURCE 108 OTHER_DETAILS: SYNTHETIC DNA OLIGONUCLEOTIDE;
SOURCE 109 MOL_ID: 15;
SOURCE 110 SYNTHETIC: YES;
SOURCE 111 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 112 ORGANISM_TAXID: 32630;
SOURCE 113 OTHER_DETAILS: SYNTHETIC DNA OLIGONUCLEOTIDE
KEYWDS PROTEIN-DNA COMPLEX, RNA POLYERMASE II, TRANSCRIBING COMPLEX,
KEYWDS 2 TRANSFERASE-DNA-RNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.O.BARNES,M.CALERO,I.MALIK,H.SPAHR,Q.ZHANG,F.PULLARA,C.D.KAPLAN,
AUTHOR 2 G.CALERO
REVDAT 1 26-AUG-15 5C44 0
JRNL AUTH C.O.BARNES,M.CALERO,I.MALIK,B.W.GRAHAM,H.SPAHR,G.LIN,
JRNL AUTH 2 A.E.COHEN,I.S.BROWN,Q.ZHANG,F.PULLARA,M.A.TRAKSELIS,
JRNL AUTH 3 C.D.KAPLAN,G.CALERO
JRNL TITL CRYSTAL STRUCTURE OF A TRANSCRIBING RNA POLYMERASE II
JRNL TITL 2 COMPLEX REVEALS A COMPLETE TRANSCRIPTION BUBBLE.
JRNL REF MOL.CELL V. 59 258 2015
JRNL REFN ISSN 1097-2765
JRNL PMID 26186291
JRNL DOI 10.1016/J.MOLCEL.2015.06.034
REMARK 2
REMARK 2 RESOLUTION. 3.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 79.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 3 NUMBER OF REFLECTIONS : 100677
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) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.216
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.990
REMARK 3 FREE R VALUE TEST SET COUNT : 3013
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.95
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 4.05
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 74.53
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 5819
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2451
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 5656
REMARK 3 BIN R VALUE (WORKING SET) : 0.2446
REMARK 3 BIN FREE R VALUE : 0.2628
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 2.80
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 163
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 31526
REMARK 3 NUCLEIC ACID ATOMS : 1014
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 83.64
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 197.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.08780
REMARK 3 B22 (A**2) : 5.28630
REMARK 3 B33 (A**2) : -16.37410
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.681
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.521
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.891
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.873
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 33228 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 45079 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 11795 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 878 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 4632 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 33228 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 4385 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 37043 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.01
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.74
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 22.28
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5C44 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-15.
REMARK 100 THE DEPOSITION ID IS D_1000210988.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 104726
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.852
REMARK 200 RESOLUTION RANGE LOW (A) : 195.608
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.23200
REMARK 200 R SYM (I) : 0.23200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.1
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.77300
REMARK 200 R SYM FOR SHELL (I) : 0.77300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 77.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, AMMONIUM ACETATE, SODIUM
REMARK 280 ACETATE, DTT, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 141.15600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 141.15600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 110.11050
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 195.92150
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 110.11050
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 195.92150
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 141.15600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 110.11050
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 195.92150
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 141.15600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 110.11050
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 195.92150
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTADECAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTADECAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 73900 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 165100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -360.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, R, S, U
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ASN A 1082
REMARK 465 THR A 1083
REMARK 465 LEU A 1176
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 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 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 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 SER B 248
REMARK 465 GLU B 262
REMARK 465 GLY B 263
REMARK 465 LYS B 270
REMARK 465 ARG B 337
REMARK 465 GLY B 338
REMARK 465 THR B 339
REMARK 465 ALA B 340
REMARK 465 LYS B 344
REMARK 465 LYS B 345
REMARK 465 GLU B 346
REMARK 465 LYS B 347
REMARK 465 LYS B 507
REMARK 465 LEU B 508
REMARK 465 ALA B 509
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 ASP B 722
REMARK 465 VAL B 723
REMARK 465 ASP B 724
REMARK 465 PRO B 725
REMARK 465 VAL B 731
REMARK 465 SER B 732
REMARK 465 HIS B 733
REMARK 465 HIS B 734
REMARK 465 GLN B 927
REMARK 465 ARG B 928
REMARK 465 MET C 1
REMARK 465 SER C 2
REMARK 465 GLU C 3
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 D 1
REMARK 465 ASN D 2
REMARK 465 VAL D 3
REMARK 465 HIS D 77
REMARK 465 LYS D 78
REMARK 465 LYS D 79
REMARK 465 LYS D 80
REMARK 465 HIS D 81
REMARK 465 LEU D 82
REMARK 465 LYS D 83
REMARK 465 HIS D 84
REMARK 465 GLU D 85
REMARK 465 ASN D 86
REMARK 465 ALA D 87
REMARK 465 ASN D 88
REMARK 465 ASP D 89
REMARK 465 GLU D 90
REMARK 465 THR D 91
REMARK 465 THR D 92
REMARK 465 ALA D 93
REMARK 465 VAL D 94
REMARK 465 GLU D 95
REMARK 465 ASP D 96
REMARK 465 GLU D 97
REMARK 465 ASP D 98
REMARK 465 ASP D 99
REMARK 465 ASP D 100
REMARK 465 LEU D 101
REMARK 465 ASP D 102
REMARK 465 GLU D 103
REMARK 465 ASP D 104
REMARK 465 ASP D 105
REMARK 465 VAL D 106
REMARK 465 ASN D 107
REMARK 465 ALA D 108
REMARK 465 ASP D 109
REMARK 465 ASP D 110
REMARK 465 ASP D 111
REMARK 465 ASP D 112
REMARK 465 PHE D 113
REMARK 465 MET D 114
REMARK 465 HIS D 115
REMARK 465 SER D 116
REMARK 465 MET E 1
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 ASP F 3
REMARK 465 TYR F 4
REMARK 465 GLU F 5
REMARK 465 GLU F 6
REMARK 465 ALA F 7
REMARK 465 PHE F 8
REMARK 465 ASN F 9
REMARK 465 ASP F 10
REMARK 465 GLY F 11
REMARK 465 ASN F 12
REMARK 465 GLU F 13
REMARK 465 ASN F 14
REMARK 465 PHE F 15
REMARK 465 GLU F 16
REMARK 465 ASP F 17
REMARK 465 PHE F 18
REMARK 465 ASP F 19
REMARK 465 VAL F 20
REMARK 465 GLU F 21
REMARK 465 HIS F 22
REMARK 465 PHE F 23
REMARK 465 SER F 24
REMARK 465 ASP F 25
REMARK 465 GLU F 26
REMARK 465 GLU F 27
REMARK 465 THR F 28
REMARK 465 TYR F 29
REMARK 465 GLU F 30
REMARK 465 GLU F 31
REMARK 465 LYS F 32
REMARK 465 PRO F 33
REMARK 465 GLN F 34
REMARK 465 PHE F 35
REMARK 465 LYS F 36
REMARK 465 ASP F 37
REMARK 465 GLY F 38
REMARK 465 GLU F 39
REMARK 465 THR F 40
REMARK 465 THR F 41
REMARK 465 ASP F 42
REMARK 465 ALA F 43
REMARK 465 ASN F 44
REMARK 465 GLY F 45
REMARK 465 LYS F 46
REMARK 465 THR F 47
REMARK 465 ILE F 48
REMARK 465 VAL F 49
REMARK 465 THR F 50
REMARK 465 GLY F 51
REMARK 465 GLY F 52
REMARK 465 ASN F 53
REMARK 465 GLY F 54
REMARK 465 PRO F 55
REMARK 465 GLU F 56
REMARK 465 ASP F 57
REMARK 465 PHE F 58
REMARK 465 GLN F 59
REMARK 465 GLN F 60
REMARK 465 HIS F 61
REMARK 465 GLU F 62
REMARK 465 GLN F 63
REMARK 465 ILE F 64
REMARK 465 ARG F 65
REMARK 465 ARG F 66
REMARK 465 LYS F 67
REMARK 465 THR F 68
REMARK 465 LEU G 172
REMARK 465 GLU G 173
REMARK 465 HIS G 174
REMARK 465 HIS G 175
REMARK 465 HIS G 176
REMARK 465 HIS G 177
REMARK 465 HIS G 178
REMARK 465 HIS G 179
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 LYS H 136
REMARK 465 MET I 1
REMARK 465 ASN I 116
REMARK 465 LYS I 117
REMARK 465 ARG I 118
REMARK 465 THR I 119
REMARK 465 GLN I 120
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 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 465 ALA L 25
REMARK 465 THR L 26
REMARK 465 DC S -12
REMARK 465 DG S -11
REMARK 465 DC S -10
REMARK 465 DT S -9
REMARK 465 DT S -8
REMARK 465 DG S -7
REMARK 465 DT S -6
REMARK 465 DA S -5
REMARK 465 DT S -4
REMARK 465 DA S -3
REMARK 465 DT S -2
REMARK 465 DA S -1
REMARK 465 DA S 0
REMARK 465 DA S 1
REMARK 465 DG S 2
REMARK 465 DA S 3
REMARK 465 DG S 4
REMARK 465 DT S 5
REMARK 465 DC S 6
REMARK 465 DC S 7
REMARK 465 DG S 8
REMARK 465 DT S 9
REMARK 465 DG S 10
REMARK 465 DG S 11
REMARK 465 DA S 12
REMARK 465 DA S 13
REMARK 465 DG S 14
REMARK 465 DC S 15
REMARK 465 DT S 16
REMARK 465 DC S 17
REMARK 465 DT S 18
REMARK 465 DC S 19
REMARK 465 DC S 20
REMARK 465 DT S 21
REMARK 465 DA S 22
REMARK 465 DG S 23
REMARK 465 DC S 24
REMARK 465 DA S 25
REMARK 465 DG S 26
REMARK 465 DG S 40
REMARK 465 DC U 1
REMARK 465 DA U 29
REMARK 465 DC U 30
REMARK 465 DC U 31
REMARK 465 DA U 32
REMARK 465 DC U 33
REMARK 465 DG U 34
REMARK 465 DG U 35
REMARK 465 DA U 36
REMARK 465 DC U 37
REMARK 465 DT U 38
REMARK 465 DC U 39
REMARK 465 DT U 40
REMARK 465 DT U 41
REMARK 465 DT U 42
REMARK 465 DA U 43
REMARK 465 DT U 44
REMARK 465 DA U 45
REMARK 465 DT U 46
REMARK 465 DA U 47
REMARK 465 DC U 48
REMARK 465 DA U 49
REMARK 465 DA U 50
REMARK 465 DG U 51
REMARK 465 DC U 52
REMARK 465 DG U 53
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 ARG A 175 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 176 CG CD CE NZ
REMARK 470 ILE A 308 CG1 CG2 CD1
REMARK 470 PHE A1084 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 VAL A1089 CG1 CG2
REMARK 470 LYS A1092 CG CD CE NZ
REMARK 470 LYS A1093 CG CD CE NZ
REMARK 470 LEU B 71 CG CD1 CD2
REMARK 470 TYR B 88 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG B 135 CG CD NE CZ NH1 NH2
REMARK 470 TYR B 149 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 358 CG CD CE NZ
REMARK 470 PHE B 442 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 884 CG CD NE CZ NH1 NH2
REMARK 470 THR B 929 OG1 CG2
REMARK 470 LYS B 934 CB CG CD CE NZ
REMARK 470 ARG D 13 CG CD NE CZ NH1 NH2
REMARK 470 VAL D 18 CB CG1 CG2
REMARK 470 GLU D 19 CB CG CD OE1 OE2
REMARK 470 GLU D 20 CB CG CD OE1 OE2
REMARK 470 ARG I 5 CG CD NE CZ NH1 NH2
REMARK 470 ARG L 54 CG CD NE CZ NH1 NH2
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 N6 DA S 38 N4 DC U 2 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 DT S 27 P DT S 27 O5' 0.113
REMARK 500 DT S 27 O5' DT S 27 C5' 0.149
REMARK 500 DT S 27 C5' DT S 27 C4' 0.089
REMARK 500 DT S 27 C4' DT S 27 C3' 0.066
REMARK 500 DT S 27 N1 DT S 27 C2 0.071
REMARK 500 DT S 27 C4 DT S 27 C5 0.064
REMARK 500 DG S 28 N1 DG S 28 C2 0.049
REMARK 500 DG S 28 N3 DG S 28 C4 0.049
REMARK 500 DG S 28 C4 DG S 28 C5 0.064
REMARK 500 DG S 28 C8 DG S 28 N9 0.047
REMARK 500 DC S 29 C1' DC S 29 N1 0.082
REMARK 500 DC S 29 N1 DC S 29 C2 0.069
REMARK 500 DT S 30 N1 DT S 30 C2 0.068
REMARK 500 DT S 30 C4 DT S 30 C5 0.059
REMARK 500 DA S 32 N1 DA S 32 C2 0.055
REMARK 500 DA S 32 C2 DA S 32 N3 0.063
REMARK 500 DA S 32 N3 DA S 32 C4 0.066
REMARK 500 DA S 32 C4 DA S 32 C5 0.068
REMARK 500 DA S 32 C5 DA S 32 C6 0.055
REMARK 500 DA S 32 C6 DA S 32 N1 0.051
REMARK 500 DA S 32 C5 DA S 32 N7 0.039
REMARK 500 DA S 32 C8 DA S 32 N9 0.048
REMARK 500 DA S 32 N9 DA S 32 C4 0.067
REMARK 500 DT S 33 N1 DT S 33 C2 0.056
REMARK 500 DC S 34 N1 DC S 34 C6 0.037
REMARK 500 DG S 35 N3 DG S 35 C4 0.053
REMARK 500 DG S 35 C4 DG S 35 C5 0.051
REMARK 500 DG S 35 C5 DG S 35 N7 0.039
REMARK 500 DG S 35 C8 DG S 35 N9 0.050
REMARK 500 DT S 37 N1 DT S 37 C2 0.065
REMARK 500 DT S 37 C4 DT S 37 C5 0.061
REMARK 500 DT S 37 C6 DT S 37 N1 0.043
REMARK 500 DA S 38 N3 DA S 38 C4 0.051
REMARK 500 DG S 39 N3 DG S 39 C4 0.047
REMARK 500 DG S 39 C4 DG S 39 C5 0.047
REMARK 500 DG S 39 C5 DG S 39 N7 0.039
REMARK 500 DG S 39 C8 DG S 39 N9 0.043
REMARK 500 DC U 2 N1 DC U 2 C2 0.074
REMARK 500 DC U 2 N1 DC U 2 C6 0.055
REMARK 500 DC U 2 C2 DC U 2 N3 0.054
REMARK 500 DC U 2 N3 DC U 2 C4 0.049
REMARK 500 DC U 2 C4 DC U 2 C5 0.053
REMARK 500 DT U 3 C5 DT U 3 C6 0.046
REMARK 500 DT U 3 C6 DT U 3 N1 0.047
REMARK 500 DA U 4 N3 DA U 4 C4 0.077
REMARK 500 DA U 4 C4 DA U 4 C5 0.053
REMARK 500 DA U 4 C5 DA U 4 C6 0.055
REMARK 500 DA U 4 C6 DA U 4 N1 0.066
REMARK 500 DA U 4 C5 DA U 4 N7 0.046
REMARK 500 DA U 4 N9 DA U 4 C4 0.059
REMARK 500
REMARK 500 THIS ENTRY HAS 79 BOND DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 GLY B 260 O - C - N ANGL. DEV. = -13.5 DEGREES
REMARK 500 DT S 27 O4' - C1' - N1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 DT S 31 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DG S 35 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DG S 39 O4' - C1' - N9 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DG U 7 O4' - C1' - N9 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DA U 16 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC U 22 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG U 27 O4' - C1' - N9 ANGL. DEV. = 1.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLN A 4 145.92 72.60
REMARK 500 GLN A 5 156.35 77.87
REMARK 500 ILE A 35 105.68 69.97
REMARK 500 ARG A 36 -58.31 -134.23
REMARK 500 ASP A 42 122.17 62.97
REMARK 500 THR A 44 50.88 -152.94
REMARK 500 THR A 46 -85.67 -104.68
REMARK 500 ALA A 48 96.52 67.69
REMARK 500 LYS A 49 124.48 -4.34
REMARK 500 ASN A 54 116.54 68.56
REMARK 500 ARG A 57 46.92 -171.91
REMARK 500 LEU A 58 -157.24 -153.78
REMARK 500 ILE A 61 -125.31 -116.54
REMARK 500 ARG A 63 30.20 36.78
REMARK 500 LYS A 66 -88.91 31.27
REMARK 500 CYS A 67 67.88 36.14
REMARK 500 GLN A 68 59.37 33.14
REMARK 500 THR A 69 -20.19 66.73
REMARK 500 GLN A 71 -117.30 52.87
REMARK 500 GLU A 72 -24.39 69.76
REMARK 500 GLU A 76 -18.38 101.22
REMARK 500 CYS A 105 -66.76 -93.33
REMARK 500 HIS A 109 -53.81 71.08
REMARK 500 ASP A 130 -124.78 -100.40
REMARK 500 SER A 131 -57.11 -165.57
REMARK 500 MET A 146 81.56 -63.09
REMARK 500 VAL A 147 134.18 -174.31
REMARK 500 ASP A 156 -28.47 -164.90
REMARK 500 PRO A 158 -73.03 -29.82
REMARK 500 THR A 159 -51.64 -138.58
REMARK 500 ARG A 164 -43.72 -147.91
REMARK 500 LYS A 186 -86.43 -81.20
REMARK 500 LYS A 187 -111.54 62.12
REMARK 500 ASP A 188 -12.87 57.21
REMARK 500 ARG A 189 91.47 -66.12
REMARK 500 THR A 191 -140.52 -134.14
REMARK 500 ASP A 193 9.09 59.84
REMARK 500 ALA A 194 -74.48 53.44
REMARK 500 ILE A 250 -75.54 61.26
REMARK 500 SER A 251 95.49 55.69
REMARK 500 ASN A 253 -98.73 61.20
REMARK 500 GLU A 254 -62.43 -160.34
REMARK 500 SER A 255 47.24 -90.99
REMARK 500 ARG A 257 -72.65 -88.27
REMARK 500 ASN A 282 -161.63 -76.99
REMARK 500 HIS A 286 -83.73 52.79
REMARK 500 ALA A 288 -26.48 -158.19
REMARK 500 ILE A 308 -53.31 -148.05
REMARK 500 ALA A 309 -158.32 -132.77
REMARK 500 GLN A 313 -52.84 -129.53
REMARK 500
REMARK 500 THIS ENTRY HAS 334 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 DA S 32 0.06 SIDE CHAIN
REMARK 500 DA U 8 0.05 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5C4A RELATED DB: PDB
REMARK 900 RELATED ID: 5C4X RELATED DB: PDB
REMARK 900 RELATED ID: 5C3E RELATED DB: PDB
REMARK 900 RELATED ID: 5C4J RELATED DB: PDB
DBREF 5C44 A 1 1733 UNP P04050 RPB1_YEAST 1 1733
DBREF 5C44 B 1 1224 UNP P08518 RPB2_YEAST 1 1224
DBREF 5C44 C 1 318 UNP P16370 RPB3_YEAST 1 318
DBREF 5C44 D 1 221 UNP P20433 RPB4_YEAST 1 221
DBREF 5C44 E 1 215 UNP P20434 RPAB1_YEAST 1 215
DBREF 5C44 F 1 155 UNP P20435 RPAB2_YEAST 1 155
DBREF 5C44 G 1 171 UNP P34087 RPB7_YEAST 1 171
DBREF 5C44 H 1 146 UNP P20436 RPAB3_YEAST 1 146
DBREF 5C44 I 1 120 UNP P27999 RPB9_YEAST 1 120
DBREF 5C44 J 1 70 UNP P22139 RPAB5_YEAST 1 70
DBREF 5C44 K 1 120 UNP P38902 RPB11_YEAST 1 120
DBREF 5C44 L 1 70 UNP P40422 RPAB4_YEAST 1 70
DBREF 5C44 R 2 10 PDB 5C44 5C44 2 10
DBREF 5C44 S -12 40 PDB 5C44 5C44 -12 40
DBREF 5C44 U 1 53 PDB 5C44 5C44 1 53
SEQADV 5C44 LEU G 172 UNP P34087 EXPRESSION TAG
SEQADV 5C44 GLU G 173 UNP P34087 EXPRESSION TAG
SEQADV 5C44 HIS G 174 UNP P34087 EXPRESSION TAG
SEQADV 5C44 HIS G 175 UNP P34087 EXPRESSION TAG
SEQADV 5C44 HIS G 176 UNP P34087 EXPRESSION TAG
SEQADV 5C44 HIS G 177 UNP P34087 EXPRESSION TAG
SEQADV 5C44 HIS G 178 UNP P34087 EXPRESSION TAG
SEQADV 5C44 HIS G 179 UNP P34087 EXPRESSION TAG
SEQRES 1 A 1733 MET VAL GLY GLN GLN TYR SER SER ALA PRO LEU ARG THR
SEQRES 2 A 1733 VAL LYS GLU VAL GLN PHE GLY LEU PHE SER PRO GLU GLU
SEQRES 3 A 1733 VAL ARG ALA ILE SER VAL ALA LYS ILE ARG PHE PRO GLU
SEQRES 4 A 1733 THR MET ASP GLU THR GLN THR ARG ALA LYS ILE GLY GLY
SEQRES 5 A 1733 LEU ASN ASP PRO ARG LEU GLY SER ILE ASP ARG ASN LEU
SEQRES 6 A 1733 LYS CYS GLN THR CYS GLN GLU GLY MET ASN GLU CYS PRO
SEQRES 7 A 1733 GLY HIS PHE GLY HIS ILE ASP LEU ALA LYS PRO VAL PHE
SEQRES 8 A 1733 HIS VAL GLY PHE ILE ALA LYS ILE LYS LYS VAL CYS GLU
SEQRES 9 A 1733 CYS VAL CYS MET HIS CYS GLY LYS LEU LEU LEU ASP GLU
SEQRES 10 A 1733 HIS ASN GLU LEU MET ARG GLN ALA LEU ALA ILE LYS ASP
SEQRES 11 A 1733 SER LYS LYS ARG PHE ALA ALA ILE TRP THR LEU CYS LYS
SEQRES 12 A 1733 THR LYS MET VAL CYS GLU THR ASP VAL PRO SER GLU ASP
SEQRES 13 A 1733 ASP PRO THR GLN LEU VAL SER ARG GLY GLY CYS GLY ASN
SEQRES 14 A 1733 THR GLN PRO THR ILE ARG LYS ASP GLY LEU LYS LEU VAL
SEQRES 15 A 1733 GLY SER TRP LYS LYS ASP ARG ALA THR GLY ASP ALA ASP
SEQRES 16 A 1733 GLU PRO GLU LEU ARG VAL LEU SER THR GLU GLU ILE LEU
SEQRES 17 A 1733 ASN ILE PHE LYS HIS ILE SER VAL LYS ASP PHE THR SER
SEQRES 18 A 1733 LEU GLY PHE ASN GLU VAL PHE SER ARG PRO GLU TRP MET
SEQRES 19 A 1733 ILE LEU THR CYS LEU PRO VAL PRO PRO PRO PRO VAL ARG
SEQRES 20 A 1733 PRO SER ILE SER PHE ASN GLU SER GLN ARG GLY GLU ASP
SEQRES 21 A 1733 ASP LEU THR PHE LYS LEU ALA ASP ILE LEU LYS ALA ASN
SEQRES 22 A 1733 ILE SER LEU GLU THR LEU GLU HIS ASN GLY ALA PRO HIS
SEQRES 23 A 1733 HIS ALA ILE GLU GLU ALA GLU SER LEU LEU GLN PHE HIS
SEQRES 24 A 1733 VAL ALA THR TYR MET ASP ASN ASP ILE ALA GLY GLN PRO
SEQRES 25 A 1733 GLN ALA LEU GLN LYS SER GLY ARG PRO VAL LYS SER ILE
SEQRES 26 A 1733 ARG ALA ARG LEU LYS GLY LYS GLU GLY ARG ILE ARG GLY
SEQRES 27 A 1733 ASN LEU MET GLY LYS ARG VAL ASP PHE SER ALA ARG THR
SEQRES 28 A 1733 VAL ILE SER GLY ASP PRO ASN LEU GLU LEU ASP GLN VAL
SEQRES 29 A 1733 GLY VAL PRO LYS SER ILE ALA LYS THR LEU THR TYR PRO
SEQRES 30 A 1733 GLU VAL VAL THR PRO TYR ASN ILE ASP ARG LEU THR GLN
SEQRES 31 A 1733 LEU VAL ARG ASN GLY PRO ASN GLU HIS PRO GLY ALA LYS
SEQRES 32 A 1733 TYR VAL ILE ARG ASP SER GLY ASP ARG ILE ASP LEU ARG
SEQRES 33 A 1733 TYR SER LYS ARG ALA GLY ASP ILE GLN LEU GLN TYR GLY
SEQRES 34 A 1733 TRP LYS VAL GLU ARG HIS ILE MET ASP ASN ASP PRO VAL
SEQRES 35 A 1733 LEU PHE ASN ARG GLN PRO SER LEU HIS LYS MET SER MET
SEQRES 36 A 1733 MET ALA HIS ARG VAL LYS VAL ILE PRO TYR SER THR PHE
SEQRES 37 A 1733 ARG LEU ASN LEU SER VAL THR SER PRO TYR ASN ALA ASP
SEQRES 38 A 1733 PHE ASP GLY ASP GLU MET ASN LEU HIS VAL PRO GLN SER
SEQRES 39 A 1733 GLU GLU THR ARG ALA GLU LEU SER GLN LEU CYS ALA VAL
SEQRES 40 A 1733 PRO LEU GLN ILE VAL SER PRO GLN SER ASN LYS PRO CYS
SEQRES 41 A 1733 MET GLY ILE VAL GLN ASP THR LEU CYS GLY ILE ARG LYS
SEQRES 42 A 1733 LEU THR LEU ARG ASP THR PHE ILE GLU LEU ASP GLN VAL
SEQRES 43 A 1733 LEU ASN MET LEU TYR TRP VAL PRO ASP TRP ASP GLY VAL
SEQRES 44 A 1733 ILE PRO THR PRO ALA ILE ILE LYS PRO LYS PRO LEU TRP
SEQRES 45 A 1733 SER GLY LYS GLN ILE LEU SER VAL ALA ILE PRO ASN GLY
SEQRES 46 A 1733 ILE HIS LEU GLN ARG PHE ASP GLU GLY THR THR LEU LEU
SEQRES 47 A 1733 SER PRO LYS ASP ASN GLY MET LEU ILE ILE ASP GLY GLN
SEQRES 48 A 1733 ILE ILE PHE GLY VAL VAL GLU LYS LYS THR VAL GLY SER
SEQRES 49 A 1733 SER ASN GLY GLY LEU ILE HIS VAL VAL THR ARG GLU LYS
SEQRES 50 A 1733 GLY PRO GLN VAL CYS ALA LYS LEU PHE GLY ASN ILE GLN
SEQRES 51 A 1733 LYS VAL VAL ASN PHE TRP LEU LEU HIS ASN GLY PHE SER
SEQRES 52 A 1733 THR GLY ILE GLY ASP THR ILE ALA ASP GLY PRO THR MET
SEQRES 53 A 1733 ARG GLU ILE THR GLU THR ILE ALA GLU ALA LYS LYS LYS
SEQRES 54 A 1733 VAL LEU ASP VAL THR LYS GLU ALA GLN ALA ASN LEU LEU
SEQRES 55 A 1733 THR ALA LYS HIS GLY MET THR LEU ARG GLU SER PHE GLU
SEQRES 56 A 1733 ASP ASN VAL VAL ARG PHE LEU ASN GLU ALA ARG ASP LYS
SEQRES 57 A 1733 ALA GLY ARG LEU ALA GLU VAL ASN LEU LYS ASP LEU ASN
SEQRES 58 A 1733 ASN VAL LYS GLN MET VAL MET ALA GLY SER LYS GLY SER
SEQRES 59 A 1733 PHE ILE ASN ILE ALA GLN MET SER ALA CYS VAL GLY GLN
SEQRES 60 A 1733 GLN SER VAL GLU GLY LYS ARG ILE ALA PHE GLY PHE VAL
SEQRES 61 A 1733 ASP ARG THR LEU PRO HIS PHE SER LYS ASP ASP TYR SER
SEQRES 62 A 1733 PRO GLU SER LYS GLY PHE VAL GLU ASN SER TYR LEU ARG
SEQRES 63 A 1733 GLY LEU THR PRO GLN GLU PHE PHE PHE HIS ALA MET GLY
SEQRES 64 A 1733 GLY ARG GLU GLY LEU ILE ASP THR ALA VAL LYS THR ALA
SEQRES 65 A 1733 GLU THR GLY TYR ILE GLN ARG ARG LEU VAL LYS ALA LEU
SEQRES 66 A 1733 GLU ASP ILE MET VAL HIS TYR ASP ASN THR THR ARG ASN
SEQRES 67 A 1733 SER LEU GLY ASN VAL ILE GLN PHE ILE TYR GLY GLU ASP
SEQRES 68 A 1733 GLY MET ASP ALA ALA HIS ILE GLU LYS GLN SER LEU ASP
SEQRES 69 A 1733 THR ILE GLY GLY SER ASP ALA ALA PHE GLU LYS ARG TYR
SEQRES 70 A 1733 ARG VAL ASP LEU LEU ASN THR ASP HIS THR LEU ASP PRO
SEQRES 71 A 1733 SER LEU LEU GLU SER GLY SER GLU ILE LEU GLY ASP LEU
SEQRES 72 A 1733 LYS LEU GLN VAL LEU LEU ASP GLU GLU TYR LYS GLN LEU
SEQRES 73 A 1733 VAL LYS ASP ARG LYS PHE LEU ARG GLU VAL PHE VAL ASP
SEQRES 74 A 1733 GLY GLU ALA ASN TRP PRO LEU PRO VAL ASN ILE ARG ARG
SEQRES 75 A 1733 ILE ILE GLN ASN ALA GLN GLN THR PHE HIS ILE ASP HIS
SEQRES 76 A 1733 THR LYS PRO SER ASP LEU THR ILE LYS ASP ILE VAL LEU
SEQRES 77 A 1733 GLY VAL LYS ASP LEU GLN GLU ASN LEU LEU VAL LEU ARG
SEQRES 78 A 1733 GLY LYS ASN GLU ILE ILE GLN ASN ALA GLN ARG ASP ALA
SEQRES 79 A 1733 VAL THR LEU PHE CYS CYS LEU LEU ARG SER ARG LEU ALA
SEQRES 80 A 1733 THR ARG ARG VAL LEU GLN GLU TYR ARG LEU THR LYS GLN
SEQRES 81 A 1733 ALA PHE ASP TRP VAL LEU SER ASN ILE GLU ALA GLN PHE
SEQRES 82 A 1733 LEU ARG SER VAL VAL HIS PRO GLY GLU MET VAL GLY VAL
SEQRES 83 A 1733 LEU ALA ALA GLN SER ILE GLY GLU PRO ALA THR GLN MET
SEQRES 84 A 1733 THR LEU ASN THR PHE HIS PHE ALA GLY VAL ALA SER LYS
SEQRES 85 A 1733 LYS VAL THR SER GLY VAL PRO ARG LEU LYS GLU ILE LEU
SEQRES 86 A 1733 ASN VAL ALA LYS ASN MET LYS THR PRO SER LEU THR VAL
SEQRES 87 A 1733 TYR LEU GLU PRO GLY HIS ALA ALA ASP GLN GLU GLN ALA
SEQRES 88 A 1733 LYS LEU ILE ARG SER ALA ILE GLU HIS THR THR LEU LYS
SEQRES 89 A 1733 SER VAL THR ILE ALA SER GLU ILE TYR TYR ASP PRO ASP
SEQRES 90 A 1733 PRO ARG SER THR VAL ILE PRO GLU ASP GLU GLU ILE ILE
SEQRES 91 A 1733 GLN LEU HIS PHE SER LEU LEU ASP GLU GLU ALA GLU GLN
SEQRES 92 A 1733 SER PHE ASP GLN GLN SER PRO TRP LEU LEU ARG LEU GLU
SEQRES 93 A 1733 LEU ASP ARG ALA ALA MET ASN ASP LYS ASP LEU THR MET
SEQRES 94 A 1733 GLY GLN VAL GLY GLU ARG ILE LYS GLN THR PHE LYS ASN
SEQRES 95 A 1733 ASP LEU PHE VAL ILE TRP SER GLU ASP ASN ASP GLU LYS
SEQRES 96 A 1733 LEU ILE ILE ARG CYS ARG VAL VAL ARG PRO LYS SER LEU
SEQRES 97 A 1733 ASP ALA GLU THR GLU ALA GLU GLU ASP HIS MET LEU LYS
SEQRES 98 A 1733 LYS ILE GLU ASN THR MET LEU GLU ASN ILE THR LEU ARG
SEQRES 99 A 1733 GLY VAL GLU ASN ILE GLU ARG VAL VAL MET MET LYS TYR
SEQRES 100 A 1733 ASP ARG LYS VAL PRO SER PRO THR GLY GLU TYR VAL LYS
SEQRES 101 A 1733 GLU PRO GLU TRP VAL LEU GLU THR ASP GLY VAL ASN LEU
SEQRES 102 A 1733 SER GLU VAL MET THR VAL PRO GLY ILE ASP PRO THR ARG
SEQRES 103 A 1733 ILE TYR THR ASN SER PHE ILE ASP ILE MET GLU VAL LEU
SEQRES 104 A 1733 GLY ILE GLU ALA GLY ARG ALA ALA LEU TYR LYS GLU VAL
SEQRES 105 A 1733 TYR ASN VAL ILE ALA SER ASP GLY SER TYR VAL ASN TYR
SEQRES 106 A 1733 ARG HIS MET ALA LEU LEU VAL ASP VAL MET THR THR GLN
SEQRES 107 A 1733 GLY GLY LEU THR SER VAL THR ARG HIS GLY PHE ASN ARG
SEQRES 108 A 1733 SER ASN THR GLY ALA LEU MET ARG CYS SER PHE GLU GLU
SEQRES 109 A 1733 THR VAL GLU ILE LEU PHE GLU ALA GLY ALA SER ALA GLU
SEQRES 110 A 1733 LEU ASP ASP CYS ARG GLY VAL SER GLU ASN VAL ILE LEU
SEQRES 111 A 1733 GLY GLN MET ALA PRO ILE GLY THR GLY ALA PHE ASP VAL
SEQRES 112 A 1733 MET ILE ASP GLU GLU SER LEU VAL LYS TYR MET PRO GLU
SEQRES 113 A 1733 GLN LYS ILE THR GLU ILE GLU ASP GLY GLN ASP GLY GLY
SEQRES 114 A 1733 VAL THR PRO TYR SER ASN GLU SER GLY LEU VAL ASN ALA
SEQRES 115 A 1733 ASP LEU ASP VAL LYS ASP GLU LEU MET PHE SER PRO LEU
SEQRES 116 A 1733 VAL ASP SER GLY SER ASN ASP ALA MET ALA GLY GLY PHE
SEQRES 117 A 1733 THR ALA TYR GLY GLY ALA ASP TYR GLY GLU ALA THR SER
SEQRES 118 A 1733 PRO PHE GLY ALA TYR GLY GLU ALA PRO THR SER PRO GLY
SEQRES 119 A 1733 PHE GLY VAL SER SER PRO GLY PHE SER PRO THR SER PRO
SEQRES 120 A 1733 THR TYR SER PRO THR SER PRO ALA TYR SER PRO THR SER
SEQRES 121 A 1733 PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO THR
SEQRES 122 A 1733 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 123 A 1733 THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 124 A 1733 PRO THR SER PRO SER TYR SER PRO THR SER PRO SER TYR
SEQRES 125 A 1733 SER PRO THR SER PRO SER TYR SER PRO THR SER PRO SER
SEQRES 126 A 1733 TYR SER PRO THR SER PRO SER TYR SER PRO THR SER PRO
SEQRES 127 A 1733 SER TYR SER PRO THR SER PRO SER TYR SER PRO THR SER
SEQRES 128 A 1733 PRO SER TYR SER PRO THR SER PRO ALA TYR SER PRO THR
SEQRES 129 A 1733 SER PRO SER TYR SER PRO THR SER PRO SER TYR SER PRO
SEQRES 130 A 1733 THR SER PRO SER TYR SER PRO THR SER PRO SER TYR SER
SEQRES 131 A 1733 PRO THR SER PRO ASN TYR SER PRO THR SER PRO SER TYR
SEQRES 132 A 1733 SER PRO THR SER PRO GLY TYR SER PRO GLY SER PRO ALA
SEQRES 133 A 1733 TYR SER PRO LYS GLN ASP GLU GLN LYS HIS ASN GLU ASN
SEQRES 134 A 1733 GLU ASN SER ARG
SEQRES 1 B 1224 MET SER ASP LEU ALA ASN SER GLU LYS TYR TYR ASP GLU
SEQRES 2 B 1224 ASP PRO TYR GLY PHE GLU ASP GLU SER ALA PRO ILE THR
SEQRES 3 B 1224 ALA GLU ASP SER TRP ALA VAL ILE SER ALA PHE PHE ARG
SEQRES 4 B 1224 GLU LYS GLY LEU VAL SER GLN GLN LEU ASP SER PHE ASN
SEQRES 5 B 1224 GLN PHE VAL ASP TYR THR LEU GLN ASP ILE ILE CYS GLU
SEQRES 6 B 1224 ASP SER THR LEU ILE LEU GLU GLN LEU ALA GLN HIS THR
SEQRES 7 B 1224 THR GLU SER ASP ASN ILE SER ARG LYS TYR GLU ILE SER
SEQRES 8 B 1224 PHE GLY LYS ILE TYR VAL THR LYS PRO MET VAL ASN GLU
SEQRES 9 B 1224 SER ASP GLY VAL THR HIS ALA LEU TYR PRO GLN GLU ALA
SEQRES 10 B 1224 ARG LEU ARG ASN LEU THR TYR SER SER GLY LEU PHE VAL
SEQRES 11 B 1224 ASP VAL LYS LYS ARG THR TYR GLU ALA ILE ASP VAL PRO
SEQRES 12 B 1224 GLY ARG GLU LEU LYS TYR GLU LEU ILE ALA GLU GLU SER
SEQRES 13 B 1224 GLU ASP ASP SER GLU SER GLY LYS VAL PHE ILE GLY ARG
SEQRES 14 B 1224 LEU PRO ILE MET LEU ARG SER LYS ASN CYS TYR LEU SER
SEQRES 15 B 1224 GLU ALA THR GLU SER ASP LEU TYR LYS LEU LYS GLU CYS
SEQRES 16 B 1224 PRO PHE ASP MET GLY GLY TYR PHE ILE ILE ASN GLY SER
SEQRES 17 B 1224 GLU LYS VAL LEU ILE ALA GLN GLU ARG SER ALA GLY ASN
SEQRES 18 B 1224 ILE VAL GLN VAL PHE LYS LYS ALA ALA PRO SER PRO ILE
SEQRES 19 B 1224 SER HIS VAL ALA GLU ILE ARG SER ALA LEU GLU LYS GLY
SEQRES 20 B 1224 SER ARG PHE ILE SER THR LEU GLN VAL LYS LEU TYR GLY
SEQRES 21 B 1224 ARG GLU GLY SER SER ALA ARG THR ILE LYS ALA THR LEU
SEQRES 22 B 1224 PRO TYR ILE LYS GLN ASP ILE PRO ILE VAL ILE ILE PHE
SEQRES 23 B 1224 ARG ALA LEU GLY ILE ILE PRO ASP GLY GLU ILE LEU GLU
SEQRES 24 B 1224 HIS ILE CYS TYR ASP VAL ASN ASP TRP GLN MET LEU GLU
SEQRES 25 B 1224 MET LEU LYS PRO CYS VAL GLU ASP GLY PHE VAL ILE GLN
SEQRES 26 B 1224 ASP ARG GLU THR ALA LEU ASP PHE ILE GLY ARG ARG GLY
SEQRES 27 B 1224 THR ALA LEU GLY ILE LYS LYS GLU LYS ARG ILE GLN TYR
SEQRES 28 B 1224 ALA LYS ASP ILE LEU GLN LYS GLU PHE LEU PRO HIS ILE
SEQRES 29 B 1224 THR GLN LEU GLU GLY PHE GLU SER ARG LYS ALA PHE PHE
SEQRES 30 B 1224 LEU GLY TYR MET ILE ASN ARG LEU LEU LEU CYS ALA LEU
SEQRES 31 B 1224 ASP ARG LYS ASP GLN ASP ASP ARG ASP HIS PHE GLY LYS
SEQRES 32 B 1224 LYS ARG LEU ASP LEU ALA GLY PRO LEU LEU ALA GLN LEU
SEQRES 33 B 1224 PHE LYS THR LEU PHE LYS LYS LEU THR LYS ASP ILE PHE
SEQRES 34 B 1224 ARG TYR MET GLN ARG THR VAL GLU GLU ALA HIS ASP PHE
SEQRES 35 B 1224 ASN MET LYS LEU ALA ILE ASN ALA LYS THR ILE THR SER
SEQRES 36 B 1224 GLY LEU LYS TYR ALA LEU ALA THR GLY ASN TRP GLY GLU
SEQRES 37 B 1224 GLN LYS LYS ALA MET SER SER ARG ALA GLY VAL SER GLN
SEQRES 38 B 1224 VAL LEU ASN ARG TYR THR TYR SER SER THR LEU SER HIS
SEQRES 39 B 1224 LEU ARG ARG THR ASN THR PRO ILE GLY ARG ASP GLY LYS
SEQRES 40 B 1224 LEU ALA LYS PRO ARG GLN LEU HIS ASN THR HIS TRP GLY
SEQRES 41 B 1224 LEU VAL CYS PRO ALA GLU THR PRO GLU GLY GLN ALA CYS
SEQRES 42 B 1224 GLY LEU VAL LYS ASN LEU SER LEU MET SER CYS ILE SER
SEQRES 43 B 1224 VAL GLY THR ASP PRO MET PRO ILE ILE THR PHE LEU SER
SEQRES 44 B 1224 GLU TRP GLY MET GLU PRO LEU GLU ASP TYR VAL PRO HIS
SEQRES 45 B 1224 GLN SER PRO ASP ALA THR ARG VAL PHE VAL ASN GLY VAL
SEQRES 46 B 1224 TRP HIS GLY VAL HIS ARG ASN PRO ALA ARG LEU MET GLU
SEQRES 47 B 1224 THR LEU ARG THR LEU ARG ARG LYS GLY ASP ILE ASN PRO
SEQRES 48 B 1224 GLU VAL SER MET ILE ARG ASP ILE ARG GLU LYS GLU LEU
SEQRES 49 B 1224 LYS ILE PHE THR ASP ALA GLY ARG VAL TYR ARG PRO LEU
SEQRES 50 B 1224 PHE ILE VAL GLU ASP ASP GLU SER LEU GLY HIS LYS GLU
SEQRES 51 B 1224 LEU LYS VAL ARG LYS GLY HIS ILE ALA LYS LEU MET ALA
SEQRES 52 B 1224 THR GLU TYR GLN ASP ILE GLU GLY GLY PHE GLU ASP VAL
SEQRES 53 B 1224 GLU GLU TYR THR TRP SER SER LEU LEU ASN GLU GLY LEU
SEQRES 54 B 1224 VAL GLU TYR ILE ASP ALA GLU GLU GLU GLU SER ILE LEU
SEQRES 55 B 1224 ILE ALA MET GLN PRO GLU ASP LEU GLU PRO ALA GLU ALA
SEQRES 56 B 1224 ASN GLU GLU ASN ASP LEU ASP VAL ASP PRO ALA LYS ARG
SEQRES 57 B 1224 ILE ARG VAL SER HIS HIS ALA THR THR PHE THR HIS CYS
SEQRES 58 B 1224 GLU ILE HIS PRO SER MET ILE LEU GLY VAL ALA ALA SER
SEQRES 59 B 1224 ILE ILE PRO PHE PRO ASP HIS ASN GLN SER PRO ARG ASN
SEQRES 60 B 1224 THR TYR GLN SER ALA MET GLY LYS GLN ALA MET GLY VAL
SEQRES 61 B 1224 PHE LEU THR ASN TYR ASN VAL ARG MET ASP THR MET ALA
SEQRES 62 B 1224 ASN ILE LEU TYR TYR PRO GLN LYS PRO LEU GLY THR THR
SEQRES 63 B 1224 ARG ALA MET GLU TYR LEU LYS PHE ARG GLU LEU PRO ALA
SEQRES 64 B 1224 GLY GLN ASN ALA ILE VAL ALA ILE ALA CYS TYR SER GLY
SEQRES 65 B 1224 TYR ASN GLN GLU ASP SER MET ILE MET ASN GLN SER SER
SEQRES 66 B 1224 ILE ASP ARG GLY LEU PHE ARG SER LEU PHE PHE ARG SER
SEQRES 67 B 1224 TYR MET ASP GLN GLU LYS LYS TYR GLY MET SER ILE THR
SEQRES 68 B 1224 GLU THR PHE GLU LYS PRO GLN ARG THR ASN THR LEU ARG
SEQRES 69 B 1224 MET LYS HIS GLY THR TYR ASP LYS LEU ASP ASP ASP GLY
SEQRES 70 B 1224 LEU ILE ALA PRO GLY VAL ARG VAL SER GLY GLU ASP VAL
SEQRES 71 B 1224 ILE ILE GLY LYS THR THR PRO ILE SER PRO ASP GLU GLU
SEQRES 72 B 1224 GLU LEU GLY GLN ARG THR ALA TYR HIS SER LYS ARG ASP
SEQRES 73 B 1224 ALA SER THR PRO LEU ARG SER THR GLU ASN GLY ILE VAL
SEQRES 74 B 1224 ASP GLN VAL LEU VAL THR THR ASN GLN ASP GLY LEU LYS
SEQRES 75 B 1224 PHE VAL LYS VAL ARG VAL ARG THR THR LYS ILE PRO GLN
SEQRES 76 B 1224 ILE GLY ASP LYS PHE ALA SER ARG HIS GLY GLN LYS GLY
SEQRES 77 B 1224 THR ILE GLY ILE THR TYR ARG ARG GLU ASP MET PRO PHE
SEQRES 78 B 1224 THR ALA GLU GLY ILE VAL PRO ASP LEU ILE ILE ASN PRO
SEQRES 79 B 1224 HIS ALA ILE PRO SER ARG MET THR VAL ALA HIS LEU ILE
SEQRES 80 B 1224 GLU CYS LEU LEU SER LYS VAL ALA ALA LEU SER GLY ASN
SEQRES 81 B 1224 GLU GLY ASP ALA SER PRO PHE THR ASP ILE THR VAL GLU
SEQRES 82 B 1224 GLY ILE SER LYS LEU LEU ARG GLU HIS GLY TYR GLN SER
SEQRES 83 B 1224 ARG GLY PHE GLU VAL MET TYR ASN GLY HIS THR GLY LYS
SEQRES 84 B 1224 LYS LEU MET ALA GLN ILE PHE PHE GLY PRO THR TYR TYR
SEQRES 85 B 1224 GLN ARG LEU ARG HIS MET VAL ASP ASP LYS ILE HIS ALA
SEQRES 86 B 1224 ARG ALA ARG GLY PRO MET GLN VAL LEU THR ARG GLN PRO
SEQRES 87 B 1224 VAL GLU GLY ARG SER ARG ASP GLY GLY LEU ARG PHE GLY
SEQRES 88 B 1224 GLU MET GLU ARG ASP CYS MET ILE ALA HIS GLY ALA ALA
SEQRES 89 B 1224 SER PHE LEU LYS GLU ARG LEU MET GLU ALA SER ASP ALA
SEQRES 90 B 1224 PHE ARG VAL HIS ILE CYS GLY ILE CYS GLY LEU MET THR
SEQRES 91 B 1224 VAL ILE ALA LYS LEU ASN HIS ASN GLN PHE GLU CYS LYS
SEQRES 92 B 1224 GLY CYS ASP ASN LYS ILE ASP ILE TYR GLN ILE HIS ILE
SEQRES 93 B 1224 PRO TYR ALA ALA LYS LEU LEU PHE GLN GLU LEU MET ALA
SEQRES 94 B 1224 MET ASN ILE THR PRO ARG LEU TYR THR ASP ARG SER ARG
SEQRES 95 B 1224 ASP PHE
SEQRES 1 C 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 D 221 MET ASN VAL SER THR SER THR PHE GLN THR ARG ARG ARG
SEQRES 2 D 221 ARG LEU LYS LYS VAL GLU GLU GLU GLU ASN ALA ALA THR
SEQRES 3 D 221 LEU GLN LEU GLY GLN GLU PHE GLN LEU LYS GLN ILE ASN
SEQRES 4 D 221 HIS GLN GLY GLU GLU GLU GLU LEU ILE ALA LEU ASN LEU
SEQRES 5 D 221 SER GLU ALA ARG LEU VAL ILE LYS GLU ALA LEU VAL GLU
SEQRES 6 D 221 ARG ARG ARG ALA PHE LYS ARG SER GLN LYS LYS HIS LYS
SEQRES 7 D 221 LYS LYS HIS LEU LYS HIS GLU ASN ALA ASN ASP GLU THR
SEQRES 8 D 221 THR ALA VAL GLU ASP GLU ASP ASP ASP LEU ASP GLU ASP
SEQRES 9 D 221 ASP VAL ASN ALA ASP ASP ASP ASP PHE MET HIS SER GLU
SEQRES 10 D 221 THR ARG GLU LYS GLU LEU GLU SER ILE ASP VAL LEU LEU
SEQRES 11 D 221 GLU GLN THR THR GLY GLY ASN ASN LYS ASP LEU LYS ASN
SEQRES 12 D 221 THR MET GLN TYR LEU THR ASN PHE SER ARG PHE ARG ASP
SEQRES 13 D 221 GLN GLU THR VAL GLY ALA VAL ILE GLN LEU LEU LYS SER
SEQRES 14 D 221 THR GLY LEU HIS PRO PHE GLU VAL ALA GLN LEU GLY SER
SEQRES 15 D 221 LEU ALA CYS ASP THR ALA ASP GLU ALA LYS THR LEU ILE
SEQRES 16 D 221 PRO SER LEU ASN ASN LYS ILE SER ASP ASP GLU LEU GLU
SEQRES 17 D 221 ARG ILE LEU LYS GLU LEU SER ASN LEU GLU THR LEU TYR
SEQRES 1 E 215 MET ASP GLN GLU ASN GLU ARG ASN ILE SER ARG LEU TRP
SEQRES 2 E 215 ARG ALA PHE ARG THR VAL LYS GLU MET VAL LYS ASP ARG
SEQRES 3 E 215 GLY TYR PHE ILE THR GLN GLU GLU VAL GLU LEU PRO LEU
SEQRES 4 E 215 GLU ASP PHE LYS ALA LYS TYR CYS ASP SER MET GLY ARG
SEQRES 5 E 215 PRO GLN ARG LYS MET MET SER PHE GLN ALA ASN PRO THR
SEQRES 6 E 215 GLU GLU SER ILE SER LYS PHE PRO ASP MET GLY SER LEU
SEQRES 7 E 215 TRP VAL GLU PHE CYS ASP GLU PRO SER VAL GLY VAL LYS
SEQRES 8 E 215 THR MET LYS THR PHE VAL ILE HIS ILE GLN GLU LYS ASN
SEQRES 9 E 215 PHE GLN THR GLY ILE PHE VAL TYR GLN ASN ASN ILE THR
SEQRES 10 E 215 PRO SER ALA MET LYS LEU VAL PRO SER ILE PRO PRO ALA
SEQRES 11 E 215 THR ILE GLU THR PHE ASN GLU ALA ALA LEU VAL VAL ASN
SEQRES 12 E 215 ILE THR HIS HIS GLU LEU VAL PRO LYS HIS ILE ARG LEU
SEQRES 13 E 215 SER SER ASP GLU LYS ARG GLU LEU LEU LYS ARG TYR ARG
SEQRES 14 E 215 LEU LYS GLU SER GLN LEU PRO ARG ILE GLN ARG ALA ASP
SEQRES 15 E 215 PRO VAL ALA LEU TYR LEU GLY LEU LYS ARG GLY GLU VAL
SEQRES 16 E 215 VAL LYS ILE ILE ARG LYS SER GLU THR SER GLY ARG TYR
SEQRES 17 E 215 ALA SER TYR ARG ILE CYS MET
SEQRES 1 F 155 MET SER ASP TYR GLU GLU ALA PHE ASN ASP GLY ASN GLU
SEQRES 2 F 155 ASN PHE GLU ASP PHE ASP VAL GLU HIS PHE SER ASP GLU
SEQRES 3 F 155 GLU THR TYR GLU GLU LYS PRO GLN PHE LYS ASP GLY GLU
SEQRES 4 F 155 THR THR ASP ALA ASN GLY LYS THR ILE VAL THR GLY GLY
SEQRES 5 F 155 ASN GLY PRO GLU ASP PHE GLN GLN HIS GLU GLN ILE ARG
SEQRES 6 F 155 ARG LYS THR LEU LYS GLU LYS ALA ILE PRO LYS ASP GLN
SEQRES 7 F 155 ARG ALA THR THR PRO TYR MET THR LYS TYR GLU ARG ALA
SEQRES 8 F 155 ARG ILE LEU GLY THR ARG ALA LEU GLN ILE SER MET ASN
SEQRES 9 F 155 ALA PRO VAL PHE VAL ASP LEU GLU GLY GLU THR ASP PRO
SEQRES 10 F 155 LEU ARG ILE ALA MET LYS GLU LEU ALA GLU LYS LYS ILE
SEQRES 11 F 155 PRO LEU VAL ILE ARG ARG TYR LEU PRO ASP GLY SER PHE
SEQRES 12 F 155 GLU ASP TRP SER VAL GLU GLU LEU ILE VAL ASP LEU
SEQRES 1 G 179 MET PHE PHE ILE LYS ASP LEU SER LEU ASN ILE THR LEU
SEQRES 2 G 179 HIS PRO SER PHE PHE GLY PRO ARG MET LYS GLN TYR LEU
SEQRES 3 G 179 LYS THR LYS LEU LEU GLU GLU VAL GLU GLY SER CYS THR
SEQRES 4 G 179 GLY LYS PHE GLY TYR ILE LEU CYS VAL LEU ASP TYR ASP
SEQRES 5 G 179 ASN ILE ASP ILE GLN ARG GLY ARG ILE LEU PRO THR ASP
SEQRES 6 G 179 GLY SER ALA GLU PHE ASN VAL LYS TYR ARG ALA VAL VAL
SEQRES 7 G 179 PHE LYS PRO PHE LYS GLY GLU VAL VAL ASP GLY THR VAL
SEQRES 8 G 179 VAL SER CYS SER GLN HIS GLY PHE GLU VAL GLN VAL GLY
SEQRES 9 G 179 PRO MET LYS VAL PHE VAL THR LYS HIS LEU MET PRO GLN
SEQRES 10 G 179 ASP LEU THR PHE ASN ALA GLY SER ASN PRO PRO SER TYR
SEQRES 11 G 179 GLN SER SER GLU ASP VAL ILE THR ILE LYS SER ARG ILE
SEQRES 12 G 179 ARG VAL LYS ILE GLU GLY CYS ILE SER GLN VAL SER SER
SEQRES 13 G 179 ILE HIS ALA ILE GLY SER ILE LYS GLU ASP TYR LEU GLY
SEQRES 14 G 179 ALA ILE LEU GLU HIS HIS HIS HIS HIS HIS
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 120 MET THR THR PHE ARG PHE CYS ARG ASP CYS ASN ASN MET
SEQRES 2 I 120 LEU TYR PRO ARG GLU ASP LYS GLU ASN ASN ARG LEU LEU
SEQRES 3 I 120 PHE GLU CYS ARG THR CYS SER TYR VAL GLU GLU ALA GLY
SEQRES 4 I 120 SER PRO LEU VAL TYR ARG HIS GLU LEU ILE THR ASN ILE
SEQRES 5 I 120 GLY GLU THR ALA GLY VAL VAL GLN ASP ILE GLY SER ASP
SEQRES 6 I 120 PRO THR LEU PRO ARG SER ASP ARG GLU CYS PRO LYS CYS
SEQRES 7 I 120 HIS SER ARG GLU ASN VAL PHE PHE GLN SER GLN GLN ARG
SEQRES 8 I 120 ARG LYS ASP THR SER MET VAL LEU PHE PHE VAL CYS LEU
SEQRES 9 I 120 SER CYS SER HIS ILE PHE THR SER ASP GLN LYS ASN LYS
SEQRES 10 I 120 ARG THR GLN
SEQRES 1 J 70 MET ILE VAL PRO VAL ARG CYS PHE SER CYS GLY LYS VAL
SEQRES 2 J 70 VAL GLY ASP LYS TRP GLU SER TYR LEU ASN LEU LEU GLN
SEQRES 3 J 70 GLU ASP GLU LEU ASP GLU GLY THR ALA LEU SER ARG LEU
SEQRES 4 J 70 GLY LEU LYS ARG TYR CYS CYS ARG ARG MET ILE LEU THR
SEQRES 5 J 70 HIS VAL ASP LEU ILE GLU LYS PHE LEU ARG TYR ASN PRO
SEQRES 6 J 70 LEU GLU LYS ARG ASP
SEQRES 1 K 120 MET ASN ALA PRO ASP ARG PHE GLU LEU PHE LEU LEU GLY
SEQRES 2 K 120 GLU GLY GLU SER LYS LEU LYS ILE ASP PRO ASP THR LYS
SEQRES 3 K 120 ALA PRO ASN ALA VAL VAL ILE THR PHE GLU LYS GLU ASP
SEQRES 4 K 120 HIS THR LEU GLY ASN LEU ILE ARG ALA GLU LEU LEU ASN
SEQRES 5 K 120 ASP ARG LYS VAL LEU PHE ALA ALA TYR LYS VAL GLU HIS
SEQRES 6 K 120 PRO PHE PHE ALA ARG PHE LYS LEU ARG ILE GLN THR THR
SEQRES 7 K 120 GLU GLY TYR ASP PRO LYS ASP ALA LEU LYS ASN ALA CYS
SEQRES 8 K 120 ASN SER ILE ILE ASN LYS LEU GLY ALA LEU LYS THR ASN
SEQRES 9 K 120 PHE GLU THR GLU TRP ASN LEU GLN THR LEU ALA ALA ASP
SEQRES 10 K 120 ASP ALA PHE
SEQRES 1 L 70 MET SER ARG GLU GLY PHE GLN ILE PRO THR ASN LEU ASP
SEQRES 2 L 70 ALA ALA ALA ALA GLY THR SER GLN ALA ARG THR ALA THR
SEQRES 3 L 70 LEU LYS TYR ILE CYS ALA GLU CYS SER SER LYS LEU SER
SEQRES 4 L 70 LEU SER ARG THR ASP ALA VAL ARG CYS LYS ASP CYS GLY
SEQRES 5 L 70 HIS ARG ILE LEU LEU LYS ALA ARG THR LYS ARG LEU VAL
SEQRES 6 L 70 GLN PHE GLU ALA ARG
SEQRES 1 R 9 U C G A G A G G A
SEQRES 1 S 53 DC DG DC DT DT DG DT DA DT DA DT DA DA
SEQRES 2 S 53 DA DG DA DG DT DC DC DG DT DG DG DA DA
SEQRES 3 S 53 DG DC DT DC DT DC DC DT DA DG DC DA DG
SEQRES 4 S 53 DT DG DC DT DT DA DT DC DG DG DT DA DG
SEQRES 5 S 53 DG
SEQRES 1 U 53 DC DC DT DA DC DC DG DA DT DA DA DG DC
SEQRES 2 U 53 DA DG DA DC DG DA DT DC DC DT DC DT DC
SEQRES 3 U 53 DG DA DA DC DC DA DC DG DG DA DC DT DC
SEQRES 4 U 53 DT DT DT DA DT DA DT DA DC DA DA DG DC
SEQRES 5 U 53 DG
HELIX 1 AA1 SER A 23 SER A 31 1 9
HELIX 2 AA2 LYS A 66 CYS A 70 5 5
HELIX 3 AA3 PHE A 95 CYS A 105 1 11
HELIX 4 AA4 ASN A 119 ALA A 127 1 9
HELIX 5 AA5 SER A 131 THR A 144 1 14
HELIX 6 AA6 SER A 203 ILE A 214 1 12
HELIX 7 AA7 SER A 215 LEU A 222 1 8
HELIX 8 AA8 ARG A 230 TRP A 233 5 4
HELIX 9 AA9 ASP A 260 ASN A 282 1 23
HELIX 10 AB1 ILE A 289 ASP A 305 1 17
HELIX 11 AB2 SER A 324 LEU A 329 1 6
HELIX 12 AB3 ARG A 335 LEU A 340 1 6
HELIX 13 AB4 LYS A 368 THR A 373 1 6
HELIX 14 AB5 ILE A 385 GLY A 395 1 11
HELIX 15 AB6 SER A 473 SER A 476 5 4
HELIX 16 AB7 SER A 494 GLN A 503 1 10
HELIX 17 AB8 GLN A 525 THR A 535 1 11
HELIX 18 AB9 GLU A 542 TRP A 552 1 11
HELIX 19 AC1 GLY A 574 SER A 579 1 6
HELIX 20 AC2 GLU A 618 GLY A 623 1 6
HELIX 21 AC3 LEU A 629 GLY A 638 1 10
HELIX 22 AC4 GLN A 640 GLY A 661 1 22
HELIX 23 AC5 GLY A 665 ILE A 670 5 6
HELIX 24 AC6 ASP A 672 ALA A 699 1 28
HELIX 25 AC7 THR A 709 LEU A 737 1 29
HELIX 26 AC8 ASN A 741 GLY A 750 1 10
HELIX 27 AC9 SER A 754 ALA A 763 1 10
HELIX 28 AD1 SER A 793 LYS A 797 5 5
HELIX 29 AD2 THR A 809 LEU A 845 1 37
HELIX 30 AD3 ASP A 874 ALA A 876 5 3
HELIX 31 AD4 SER A 889 ARG A 898 1 10
HELIX 32 AD5 SER A 915 LEU A 920 1 6
HELIX 33 AD6 ASP A 922 PHE A 947 1 26
HELIX 34 AD7 ASN A 959 HIS A 972 1 14
HELIX 35 AD8 THR A 982 LEU A 997 1 16
HELIX 36 AD9 ASN A 1004 THR A 1016 1 13
HELIX 37 AE1 THR A 1016 LEU A 1026 1 11
HELIX 38 AE2 ALA A 1027 GLU A 1034 1 8
HELIX 39 AE3 THR A 1038 SER A 1056 1 19
HELIX 40 AE4 VAL A 1064 GLU A 1074 1 11
HELIX 41 AE5 GLY A 1097 VAL A 1107 1 11
HELIX 42 AE6 ASP A 1127 GLU A 1139 1 13
HELIX 43 AE7 GLU A 1167 PHE A 1174 1 8
HELIX 44 AE8 ASP A 1198 LYS A 1205 1 8
HELIX 45 AE9 THR A 1208 LYS A 1221 1 14
HELIX 46 AF1 GLU A 1256 ASN A 1270 1 15
HELIX 47 AF2 SER A 1331 LEU A 1339 1 9
HELIX 48 AF3 GLY A 1340 ASP A 1359 1 20
HELIX 49 AF4 ASN A 1364 THR A 1377 1 14
HELIX 50 AF5 GLY A 1395 SER A 1401 1 7
HELIX 51 AF6 THR A 1405 SER A 1415 1 11
HELIX 52 AF7 VAL A 1424 GLY A 1431 1 8
HELIX 53 AF8 ILE A 1436 GLY A 1439 5 4
HELIX 54 AF9 ASP A 1446 MET A 1454 1 9
HELIX 55 AG1 THR B 26 LYS B 41 1 16
HELIX 56 AG2 VAL B 44 TYR B 57 1 14
HELIX 57 AG3 TYR B 57 CYS B 64 1 8
HELIX 58 AG4 TYR B 113 ASN B 121 1 9
HELIX 59 AG5 CYS B 179 GLU B 183 5 5
HELIX 60 AG6 THR B 185 TYR B 190 1 6
HELIX 61 AG7 PRO B 281 LEU B 289 1 9
HELIX 62 AG8 PRO B 293 CYS B 302 1 10
HELIX 63 AG9 TRP B 308 LYS B 315 1 8
HELIX 64 AH1 LYS B 315 ASP B 320 1 6
HELIX 65 AH2 ASP B 326 ASP B 332 1 7
HELIX 66 AH3 ILE B 349 LYS B 358 1 10
HELIX 67 AH4 PHE B 370 LEU B 390 1 21
HELIX 68 AH5 LEU B 408 THR B 435 1 28
HELIX 69 AH6 PHE B 442 GLY B 464 1 23
HELIX 70 AH7 THR B 487 ARG B 496 1 10
HELIX 71 AH8 HIS B 515 TRP B 519 5 5
HELIX 72 AH9 PRO B 551 GLU B 560 1 10
HELIX 73 AI1 GLU B 567 TYR B 569 5 3
HELIX 74 AI2 ASN B 592 GLY B 607 1 16
HELIX 75 AI3 ARG B 654 ASP B 668 1 15
HELIX 76 AI4 TRP B 681 ASN B 686 1 6
HELIX 77 AI5 GLU B 696 ILE B 701 5 6
HELIX 78 AI6 HIS B 744 LEU B 749 5 6
HELIX 79 AI7 GLY B 750 ILE B 756 1 7
HELIX 80 AI8 PHE B 758 ASN B 762 5 5
HELIX 81 AI9 GLN B 763 GLY B 774 1 12
HELIX 82 AJ1 THR B 783 VAL B 787 5 5
HELIX 83 AJ2 ALA B 808 LYS B 813 1 6
HELIX 84 AJ3 GLN B 843 GLY B 849 1 7
HELIX 85 AJ4 THR B 889 LEU B 893 5 5
HELIX 86 AJ5 PRO B 1014 ILE B 1017 5 4
HELIX 87 AJ6 THR B 1022 GLY B 1039 1 18
HELIX 88 AJ7 THR B 1051 GLY B 1063 1 13
HELIX 89 AJ8 GLY B 1121 ASP B 1125 5 5
HELIX 90 AJ9 GLY B 1131 GLY B 1142 1 12
HELIX 91 AK1 ALA B 1143 MET B 1152 1 10
HELIX 92 AK2 PRO B 1197 ALA B 1209 1 13
HELIX 93 AK3 ASP C 26 ALA C 39 1 14
HELIX 94 AK4 GLU C 61 ILE C 70 1 10
HELIX 95 AK5 HIS C 167 GLY C 171 5 5
HELIX 96 AK6 ASP C 196 TRP C 201 1 6
HELIX 97 AK7 SER C 204 TYR C 209 5 6
HELIX 98 AK8 PRO C 239 MET C 265 1 27
HELIX 99 AK9 ASN D 51 SER D 73 1 23
HELIX 100 AL1 ARG D 119 THR D 134 1 16
HELIX 101 AL2 ASN D 138 PHE D 151 1 14
HELIX 102 AL3 ASP D 156 LYS D 168 1 13
HELIX 103 AL4 HIS D 173 GLY D 181 1 9
HELIX 104 AL5 THR D 187 ILE D 195 1 9
HELIX 105 AL6 SER D 203 GLU D 218 1 16
HELIX 106 AL7 GLU E 4 GLY E 27 1 24
HELIX 107 AL8 THR E 31 GLU E 36 1 6
HELIX 108 AL9 PRO E 38 CYS E 47 1 10
HELIX 109 AM1 ARG E 55 SER E 59 5 5
HELIX 110 AM2 THR E 65 PHE E 72 1 8
HELIX 111 AM3 GLY E 89 ASN E 104 1 16
HELIX 112 AM4 THR E 117 LEU E 123 1 7
HELIX 113 AM5 GLU E 137 VAL E 141 1 5
HELIX 114 AM6 SER E 157 TYR E 168 1 12
HELIX 115 AM7 ASP E 182 LEU E 188 1 7
HELIX 116 AM8 THR F 86 MET F 103 1 18
HELIX 117 AM9 ASP F 116 GLU F 127 1 12
HELIX 118 AN1 HIS G 14 PHE G 18 5 5
HELIX 119 AN2 MET G 22 VAL G 34 1 13
HELIX 120 AN3 VAL I 59 ASP I 65 5 7
HELIX 121 AN4 ASP J 16 GLU J 27 1 12
HELIX 122 AN5 ASP J 31 GLY J 40 1 10
HELIX 123 AN6 ARG J 43 THR J 52 1 10
HELIX 124 AN7 LEU J 56 ARG J 62 1 7
HELIX 125 AN8 ASP K 5 PHE K 10 5 6
HELIX 126 AN9 ASP K 39 ASN K 52 1 14
HELIX 127 AO1 ASP K 82 GLN K 112 1 31
SHEET 1 AA1 3 LEU A1418 ASP A1419 0
SHEET 2 AA1 3 GLU A 16 GLN A 18 -1 N VAL A 17 O ASP A1419
SHEET 3 AA1 3 ARG B1215 TYR B1217 -1 O ARG B1215 N GLN A 18
SHEET 1 AA2 2 GLY A 82 PHE A 91 0
SHEET 2 AA2 2 ILE A 235 VAL A 241 -1 O LEU A 239 N ILE A 84
SHEET 1 AA3 2 VAL A 106 CYS A 107 0
SHEET 2 AA3 2 LYS A 112 LEU A 113 -1 O LYS A 112 N CYS A 107
SHEET 1 AA4 3 THR A 173 ASP A 177 0
SHEET 2 AA4 3 LYS A 180 TRP A 185 -1 O SER A 184 N THR A 173
SHEET 3 AA4 3 GLU A 198 LEU A 202 -1 O GLU A 198 N TRP A 185
SHEET 1 AA5 2 LYS A 343 ARG A 344 0
SHEET 2 AA5 2 ARG B1129 PHE B1130 -1 O PHE B1130 N LYS A 343
SHEET 1 AA6 7 SER A 348 ASP A 356 0
SHEET 2 AA6 7 PHE A 468 ASN A 471 1 O PHE A 468 N SER A 354
SHEET 3 AA6 7 GLN A 363 PRO A 367 -1 N GLY A 365 O ARG A 469
SHEET 4 AA6 7 MET A 456 ILE A 463 1 O ILE A 463 N VAL A 366
SHEET 5 AA6 7 PRO A 441 PHE A 444 -1 N PHE A 444 O MET A 456
SHEET 6 AA6 7 GLU A 486 HIS A 490 -1 O HIS A 490 N LEU A 443
SHEET 7 AA6 7 SER A 348 ASP A 356 -1 N ALA A 349 O LEU A 489
SHEET 1 AA7 4 THR A 375 VAL A 379 0
SHEET 2 AA7 4 LYS A 431 HIS A 435 -1 O ARG A 434 N TYR A 376
SHEET 3 AA7 4 ALA A 402 ILE A 406 -1 N TYR A 404 O GLU A 433
SHEET 4 AA7 4 ARG A 412 ASP A 414 -1 O ILE A 413 N VAL A 405
SHEET 1 AA8 2 VAL A 512 SER A 513 0
SHEET 2 AA8 2 LYS A 518 PRO A 519 -1 O LYS A 518 N SER A 513
SHEET 1 AA9 2 PHE A 540 ILE A 541 0
SHEET 2 AA9 2 TRP A 572 SER A 573 -1 O TRP A 572 N ILE A 541
SHEET 1 AB1 3 HIS A 587 GLN A 589 0
SHEET 2 AB1 3 MET A 605 ILE A 608 -1 O ILE A 607 N LEU A 588
SHEET 3 AB1 3 GLN A 611 GLY A 615 -1 O ILE A 613 N LEU A 606
SHEET 1 AB2 2 GLY A 766 GLN A 767 0
SHEET 2 AB2 2 PHE A 799 VAL A 800 -1 O VAL A 800 N GLY A 766
SHEET 1 AB3 2 SER A 769 VAL A 770 0
SHEET 2 AB3 2 LYS A 773 ARG A 774 -1 O LYS A 773 N VAL A 770
SHEET 1 AB4 2 MET A 849 VAL A 850 0
SHEET 2 AB4 2 THR A 856 ARG A 857 -1 O ARG A 857 N MET A 849
SHEET 1 AB5 2 ILE A 878 GLN A 881 0
SHEET 2 AB5 2 TRP A 954 PRO A 957 -1 O LEU A 956 N GLU A 879
SHEET 1 AB6 3 THR A1117 TYR A1119 0
SHEET 2 AB6 3 TYR A1298 GLU A1307 -1 O LEU A1306 N VAL A1118
SHEET 3 AB6 3 VAL A1283 PRO A1292 -1 N VAL A1291 O VAL A1299
SHEET 1 AB7 2 THR A1141 THR A1142 0
SHEET 2 AB7 2 THR A1272 ARG A1274 -1 O LEU A1273 N THR A1141
SHEET 1 AB8 5 LEU A1224 TRP A1228 0
SHEET 2 AB8 5 ILE A1238 VAL A1242 -1 O ARG A1241 N PHE A1225
SHEET 3 AB8 5 TRP A1191 LEU A1197 -1 N LEU A1193 O CYS A1240
SHEET 4 AB8 5 THR A1147 TYR A1154 -1 N GLU A1151 O ARG A1194
SHEET 5 AB8 5 LEU I 42 ARG I 45 -1 O VAL I 43 N ILE A1152
SHEET 1 AB9 7 ALA D 49 LEU D 50 0
SHEET 2 AB9 7 PHE G 2 LEU G 13 -1 O PHE G 2 N LEU D 50
SHEET 3 AB9 7 ALA G 68 PHE G 79 -1 O PHE G 70 N ILE G 11
SHEET 4 AB9 7 GLY G 59 ILE G 61 -1 N ARG G 60 O GLU G 69
SHEET 5 AB9 7 PHE A1441 ILE A1445 -1 N VAL A1443 O ILE G 61
SHEET 6 AB9 7 LEU F 132 TYR F 137 -1 O VAL F 133 N MET A1444
SHEET 7 AB9 7 PHE F 143 SER F 147 -1 O TRP F 146 N ILE F 134
SHEET 1 AC1 5 ALA D 49 LEU D 50 0
SHEET 2 AC1 5 PHE G 2 LEU G 13 -1 O PHE G 2 N LEU D 50
SHEET 3 AC1 5 ALA G 68 PHE G 79 -1 O PHE G 70 N ILE G 11
SHEET 4 AC1 5 GLY G 43 LEU G 49 -1 N LEU G 46 O VAL G 77
SHEET 5 AC1 5 CYS G 38 THR G 39 -1 N THR G 39 O GLY G 43
SHEET 1 AC2 4 THR B 68 GLN B 73 0
SHEET 2 AC2 4 ARG B 86 VAL B 97 -1 O TYR B 88 N LEU B 71
SHEET 3 AC2 4 SER B 125 ARG B 135 -1 O ARG B 135 N GLU B 89
SHEET 4 AC2 4 VAL B 165 PRO B 171 -1 O LEU B 170 N SER B 126
SHEET 1 AC3 2 VAL B 102 ASN B 103 0
SHEET 2 AC3 2 THR B 109 HIS B 110 -1 O HIS B 110 N VAL B 102
SHEET 1 AC4 3 PHE B 203 ILE B 205 0
SHEET 2 AC4 3 SER B 208 LEU B 212 -1 O LYS B 210 N PHE B 203
SHEET 3 AC4 3 SER B 480 VAL B 482 -1 O GLN B 481 N VAL B 211
SHEET 1 AC5 4 LYS B 404 ASP B 407 0
SHEET 2 AC5 4 ALA B 214 SER B 218 -1 N ARG B 217 O ARG B 405
SHEET 3 AC5 4 ARG B 497 ASN B 499 1 O ASN B 499 N ALA B 214
SHEET 4 AC5 4 LYS B 537 ASN B 538 -1 O LYS B 537 N THR B 498
SHEET 1 AC6 3 VAL B 223 LYS B 227 0
SHEET 2 AC6 3 ILE B 234 ILE B 240 -1 O VAL B 237 N PHE B 226
SHEET 3 AC6 3 VAL B 256 TYR B 259 -1 O VAL B 256 N ALA B 238
SHEET 1 AC7 3 CYS B 544 ILE B 545 0
SHEET 2 AC7 3 VAL B 633 GLU B 641 -1 O TYR B 634 N CYS B 544
SHEET 3 AC7 3 VAL B 690 ASP B 694 -1 O GLU B 691 N LEU B 637
SHEET 1 AC8 4 GLU B 650 LEU B 651 0
SHEET 2 AC8 4 VAL B 633 GLU B 641 -1 N GLU B 641 O GLU B 650
SHEET 3 AC8 4 HIS B 740 CYS B 741 -1 O CYS B 741 N PHE B 638
SHEET 4 AC8 4 ILE B 703 ALA B 704 1 N ALA B 704 O HIS B 740
SHEET 1 AC9 5 GLU B 564 PRO B 565 0
SHEET 2 AC9 5 TRP B 586 HIS B 590 -1 O VAL B 589 N GLU B 564
SHEET 3 AC9 5 THR B 578 VAL B 582 -1 N VAL B 580 O GLY B 588
SHEET 4 AC9 5 GLU B 623 PHE B 627 1 O LEU B 624 N PHE B 581
SHEET 5 AC9 5 SER B 614 ASP B 618 -1 N ILE B 616 O LYS B 625
SHEET 1 AD1 4 ALA B 793 LEU B 796 0
SHEET 2 AD1 4 SER B 853 GLN B 862 -1 O PHE B 856 N ALA B 793
SHEET 3 AD1 4 LYS B 962 THR B 970 -1 O VAL B 964 N ASP B 861
SHEET 4 AD1 4 ILE B 948 THR B 956 -1 N THR B 955 O PHE B 963
SHEET 1 AD2 7 GLN B 821 ILE B 827 0
SHEET 2 AD2 7 LEU B1010 ILE B1012 1 O LEU B1010 N ILE B 824
SHEET 3 AD2 7 MET B 839 ASN B 842 -1 N ILE B 840 O ILE B1011
SHEET 4 AD2 7 LYS B 987 TYR B 994 1 O GLY B 991 N MET B 839
SHEET 5 AD2 7 LYS B 979 SER B 982 -1 N PHE B 980 O GLY B 988
SHEET 6 AD2 7 PRO B1089 ARG B1094 -1 O GLN B1093 N ALA B 981
SHEET 7 AD2 7 GLN B 821 ILE B 827 -1 N ALA B 823 O THR B1090
SHEET 1 AD3 2 PHE B1001 THR B1002 0
SHEET 2 AD3 2 MET B1072 TYR B1073 -1 O TYR B1073 N PHE B1001
SHEET 1 AD4 2 PHE B1069 GLU B1070 0
SHEET 2 AD4 2 ILE B1085 PHE B1086 -1 O ILE B1085 N GLU B1070
SHEET 1 AD5 2 PHE B1158 CYS B1163 0
SHEET 2 AD5 2 ILE B1191 ILE B1196 -1 O TYR B1192 N ILE B1162
SHEET 1 AD6 3 VAL C 8 ALA C 13 0
SHEET 2 AD6 3 VAL C 18 LEU C 22 -1 O ILE C 21 N LYS C 9
SHEET 3 AD6 3 PHE C 228 ASN C 231 -1 O PHE C 228 N LEU C 22
SHEET 1 AD7 3 ALA C 45 ASN C 54 0
SHEET 2 AD7 3 GLU C 152 LYS C 160 -1 O VAL C 158 N ASP C 47
SHEET 3 AD7 3 ALA C 103 PHE C 104 -1 N ALA C 103 O LEU C 153
SHEET 1 AD8 4 ALA C 45 ASN C 54 0
SHEET 2 AD8 4 GLU C 152 LYS C 160 -1 O VAL C 158 N ASP C 47
SHEET 3 AD8 4 VAL C 97 THR C 100 -1 N VAL C 97 O ALA C 159
SHEET 4 AD8 4 VAL C 119 ILE C 120 -1 O VAL C 119 N THR C 100
SHEET 1 AD9 2 THR C 111 ASN C 112 0
SHEET 2 AD9 2 LYS C 146 LEU C 147 -1 O LEU C 147 N THR C 111
SHEET 1 AE1 2 LYS D 36 GLN D 37 0
SHEET 2 AE1 2 GLU D 45 GLU D 46 -1 O GLU D 45 N GLN D 37
SHEET 1 AE2 4 GLN E 61 ALA E 62 0
SHEET 2 AE2 4 LEU E 78 GLU E 81 -1 O LEU E 78 N ALA E 62
SHEET 3 AE2 4 THR E 107 TYR E 112 1 O ILE E 109 N TRP E 79
SHEET 4 AE2 4 THR E 131 ASN E 136 1 O GLU E 133 N PHE E 110
SHEET 1 AE3 4 LYS E 152 ARG E 155 0
SHEET 2 AE3 4 VAL E 195 ARG E 200 -1 O LYS E 197 N ILE E 154
SHEET 3 AE3 4 TYR E 208 CYS E 214 -1 O SER E 210 N ILE E 198
SHEET 4 AE3 4 ARG E 177 ILE E 178 1 N ILE E 178 O ILE E 213
SHEET 1 AE4 6 VAL G 86 CYS G 94 0
SHEET 2 AE4 6 GLY G 98 VAL G 103 -1 O GLN G 102 N THR G 90
SHEET 3 AE4 6 MET G 106 THR G 111 -1 O VAL G 108 N VAL G 101
SHEET 4 AE4 6 HIS G 158 SER G 162 1 O ALA G 159 N PHE G 109
SHEET 5 AE4 6 ARG G 142 ILE G 151 -1 N ILE G 151 O HIS G 158
SHEET 6 AE4 6 VAL G 86 CYS G 94 -1 N VAL G 87 O VAL G 145
SHEET 1 AE5 2 PHE G 121 ASN G 122 0
SHEET 2 AE5 2 SER G 129 TYR G 130 -1 O SER G 129 N ASN G 122
SHEET 1 AE6 9 THR H 4 ASP H 16 0
SHEET 2 AE6 9 VAL H 23 SER H 30 -1 O GLU H 27 N SER H 13
SHEET 3 AE6 9 LYS H 37 ASN H 43 -1 O ILE H 42 N CYS H 24
SHEET 4 AE6 9 LEU H 121 LEU H 125 -1 O ARG H 124 N THR H 39
SHEET 5 AE6 9 ILE H 112 PHE H 118 -1 N PHE H 118 O LEU H 121
SHEET 6 AE6 9 TYR H 95 GLU H 106 -1 N GLU H 105 O ALA H 113
SHEET 7 AE6 9 ASN H 139 ARG H 145 -1 O ILE H 144 N TYR H 95
SHEET 8 AE6 9 SER H 54 ALA H 60 -1 N THR H 58 O LEU H 143
SHEET 9 AE6 9 THR H 4 ASP H 16 -1 N LEU H 5 O ILE H 59
SHEET 1 AE7 3 TYR I 15 GLU I 18 0
SHEET 2 AE7 3 LEU I 25 GLU I 28 -1 O LEU I 26 N ARG I 17
SHEET 3 AE7 3 VAL I 35 GLU I 37 -1 O GLU I 36 N PHE I 27
SHEET 1 AE8 4 ARG I 70 SER I 71 0
SHEET 2 AE8 4 ASN I 83 PHE I 86 -1 O ASN I 83 N SER I 71
SHEET 3 AE8 4 PHE I 100 CYS I 103 -1 O VAL I 102 N VAL I 84
SHEET 4 AE8 4 ILE I 109 THR I 111 -1 O PHE I 110 N PHE I 101
SHEET 1 AE9 4 LEU K 19 PRO K 23 0
SHEET 2 AE9 4 VAL K 31 GLU K 36 -1 O VAL K 32 N ASP K 22
SHEET 3 AE9 4 ARG K 70 THR K 77 -1 O LEU K 73 N ILE K 33
SHEET 4 AE9 4 VAL K 56 LYS K 62 -1 N PHE K 58 O GLN K 76
SSBOND 1 CYS A 67 CYS A 77 1555 1555 2.84
SSBOND 2 CYS I 10 CYS I 32 1555 1555 2.96
CISPEP 1 ASP A 307 ILE A 308 0 -1.14
CISPEP 2 LYS A 317 SER A 318 0 3.44
CISPEP 3 GLN A 447 PRO A 448 0 3.61
CISPEP 4 MET A 1079 THR A 1080 0 1.53
CISPEP 5 ALA A 1087 GLY A 1088 0 -1.08
CISPEP 6 GLY A 1088 VAL A 1089 0 1.40
CISPEP 7 VAL A 1107 ALA A 1108 0 0.70
CISPEP 8 THR B 79 GLU B 80 0 -2.39
CISPEP 9 SER B 81 ASP B 82 0 1.42
CISPEP 10 ASP B 82 ASN B 83 0 -0.56
CISPEP 11 THR B 136 TYR B 137 0 6.40
CISPEP 12 GLY B 144 ARG B 145 0 0.54
CISPEP 13 ARG B 145 GLU B 146 0 4.66
CISPEP 14 GLU B 150 LEU B 151 0 -8.96
CISPEP 15 GLU B 245 LYS B 246 0 -1.22
CISPEP 16 PRO B 274 TYR B 275 0 -1.69
CISPEP 17 GLU B 438 ALA B 439 0 3.43
CISPEP 18 ARG B 504 ASP B 505 0 -0.08
CISPEP 19 ASP B 505 GLY B 506 0 0.00
CISPEP 20 GLY B 867 MET B 868 0 0.74
CISPEP 21 SER B 919 PRO B 920 0 4.63
CISPEP 22 GLU B 923 GLU B 924 0 1.95
CISPEP 23 THR B 929 ALA B 930 0 -1.03
CISPEP 24 ALA B 930 TYR B 931 0 7.04
CISPEP 25 ARG D 11 ARG D 12 0 2.29
CISPEP 26 PRO E 128 PRO E 129 0 0.25
CISPEP 27 ASN G 126 PRO G 127 0 3.01
CRYST1 220.221 391.843 282.312 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.004541 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002552 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003542 0.00000
(ATOM LINES ARE NOT SHOWN.)
END