HEADER RIBOSOME 29-APR-10 3MR8
TITLE RECOGNITION OF THE AMBER STOP CODON BY RELEASE FACTOR RF1. THIS ENTRY
TITLE 2 3MR8 CONTAINS 30S RIBOSOMAL SUBUNIT. THE 50S RIBOSOMAL SUBUNIT CAN BE
TITLE 3 FOUND IN PDB ENTRY 3MS1. MOLECULE B IN THE SAME ASYMMETRIC UNIT IS
TITLE 4 DEPOSITED AS 3MRZ (50S) AND 3MS0 (30S).
SPLIT 3MR8 3MRZ 3MS0 3MS1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 16S RRNA (1504-MER);
COMPND 3 CHAIN: A;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: 30S RIBOSOMAL PROTEIN S2;
COMPND 6 CHAIN: B;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: 30S RIBOSOMAL PROTEIN S3;
COMPND 9 CHAIN: C;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: 30S RIBOSOMAL PROTEIN S4;
COMPND 12 CHAIN: D;
COMPND 13 MOL_ID: 5;
COMPND 14 MOLECULE: 30S RIBOSOMAL PROTEIN S5;
COMPND 15 CHAIN: E;
COMPND 16 MOL_ID: 6;
COMPND 17 MOLECULE: 30S RIBOSOMAL PROTEIN S6;
COMPND 18 CHAIN: F;
COMPND 19 MOL_ID: 7;
COMPND 20 MOLECULE: 30S RIBOSOMAL PROTEIN S7;
COMPND 21 CHAIN: G;
COMPND 22 MOL_ID: 8;
COMPND 23 MOLECULE: 30S RIBOSOMAL PROTEIN S8;
COMPND 24 CHAIN: H;
COMPND 25 MOL_ID: 9;
COMPND 26 MOLECULE: 30S RIBOSOMAL PROTEIN S9;
COMPND 27 CHAIN: I;
COMPND 28 MOL_ID: 10;
COMPND 29 MOLECULE: 30S RIBOSOMAL PROTEIN S10;
COMPND 30 CHAIN: J;
COMPND 31 MOL_ID: 11;
COMPND 32 MOLECULE: 30S RIBOSOMAL PROTEIN S11;
COMPND 33 CHAIN: K;
COMPND 34 MOL_ID: 12;
COMPND 35 MOLECULE: 30S RIBOSOMAL PROTEIN S12;
COMPND 36 CHAIN: L;
COMPND 37 MOL_ID: 13;
COMPND 38 MOLECULE: 30S RIBOSOMAL PROTEIN S13;
COMPND 39 CHAIN: M;
COMPND 40 MOL_ID: 14;
COMPND 41 MOLECULE: 30S RIBOSOMAL PROTEIN S14;
COMPND 42 CHAIN: N;
COMPND 43 MOL_ID: 15;
COMPND 44 MOLECULE: 30S RIBOSOMAL PROTEIN S15;
COMPND 45 CHAIN: O;
COMPND 46 MOL_ID: 16;
COMPND 47 MOLECULE: 30S RIBOSOMAL PROTEIN S16;
COMPND 48 CHAIN: P;
COMPND 49 MOL_ID: 17;
COMPND 50 MOLECULE: 30S RIBOSOMAL PROTEIN S17;
COMPND 51 CHAIN: Q;
COMPND 52 MOL_ID: 18;
COMPND 53 MOLECULE: 30S RIBOSOMAL PROTEIN S18;
COMPND 54 CHAIN: R;
COMPND 55 MOL_ID: 19;
COMPND 56 MOLECULE: 30S RIBOSOMAL PROTEIN S19;
COMPND 57 CHAIN: S;
COMPND 58 MOL_ID: 20;
COMPND 59 MOLECULE: 30S RIBOSOMAL PROTEIN S20;
COMPND 60 CHAIN: T;
COMPND 61 MOL_ID: 21;
COMPND 62 MOLECULE: 30S RIBOSOMAL PROTEIN THX;
COMPND 63 CHAIN: U;
COMPND 64 MOL_ID: 22;
COMPND 65 MOLECULE: PEPTIDE CHAIN RELEASE FACTOR 1;
COMPND 66 CHAIN: V;
COMPND 67 SYNONYM: RF-1;
COMPND 68 MOL_ID: 23;
COMPND 69 MOLECULE: P-SITE TRNA-FMET;
COMPND 70 CHAIN: W;
COMPND 71 MOL_ID: 24;
COMPND 72 MOLECULE: MESSENGER RNA (5'-R(*AP*AP*UP*GP*UP*AP*G)-3');
COMPND 73 CHAIN: X
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 262724;
SOURCE 4 STRAIN: HB27;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 7 ORGANISM_TAXID: 262724;
SOURCE 8 STRAIN: HB27;
SOURCE 9 MOL_ID: 3;
SOURCE 10 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 11 ORGANISM_TAXID: 262724;
SOURCE 12 STRAIN: HB27;
SOURCE 13 MOL_ID: 4;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 15 ORGANISM_TAXID: 262724;
SOURCE 16 STRAIN: HB27;
SOURCE 17 MOL_ID: 5;
SOURCE 18 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 19 ORGANISM_TAXID: 262724;
SOURCE 20 STRAIN: HB27;
SOURCE 21 MOL_ID: 6;
SOURCE 22 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 23 ORGANISM_TAXID: 262724;
SOURCE 24 STRAIN: HB27;
SOURCE 25 MOL_ID: 7;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 27 ORGANISM_TAXID: 262724;
SOURCE 28 STRAIN: HB27;
SOURCE 29 MOL_ID: 8;
SOURCE 30 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 31 ORGANISM_TAXID: 262724;
SOURCE 32 STRAIN: HB27;
SOURCE 33 MOL_ID: 9;
SOURCE 34 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 35 ORGANISM_TAXID: 262724;
SOURCE 36 STRAIN: HB27;
SOURCE 37 MOL_ID: 10;
SOURCE 38 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 39 ORGANISM_TAXID: 262724;
SOURCE 40 STRAIN: HB27;
SOURCE 41 MOL_ID: 11;
SOURCE 42 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 43 ORGANISM_TAXID: 262724;
SOURCE 44 STRAIN: HB27;
SOURCE 45 MOL_ID: 12;
SOURCE 46 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 47 ORGANISM_TAXID: 262724;
SOURCE 48 STRAIN: HB27;
SOURCE 49 MOL_ID: 13;
SOURCE 50 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 51 ORGANISM_TAXID: 262724;
SOURCE 52 STRAIN: HB27;
SOURCE 53 MOL_ID: 14;
SOURCE 54 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 55 ORGANISM_TAXID: 262724;
SOURCE 56 STRAIN: HB27;
SOURCE 57 MOL_ID: 15;
SOURCE 58 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 59 ORGANISM_TAXID: 262724;
SOURCE 60 STRAIN: HB27;
SOURCE 61 MOL_ID: 16;
SOURCE 62 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 63 ORGANISM_TAXID: 262724;
SOURCE 64 STRAIN: HB27;
SOURCE 65 MOL_ID: 17;
SOURCE 66 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 67 ORGANISM_TAXID: 262724;
SOURCE 68 STRAIN: HB27;
SOURCE 69 MOL_ID: 18;
SOURCE 70 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 71 ORGANISM_TAXID: 262724;
SOURCE 72 STRAIN: HB27;
SOURCE 73 MOL_ID: 19;
SOURCE 74 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 75 ORGANISM_TAXID: 262724;
SOURCE 76 STRAIN: HB27;
SOURCE 77 MOL_ID: 20;
SOURCE 78 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 79 ORGANISM_TAXID: 262724;
SOURCE 80 STRAIN: HB27;
SOURCE 81 MOL_ID: 21;
SOURCE 82 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 83 ORGANISM_TAXID: 262724;
SOURCE 84 STRAIN: HB27;
SOURCE 85 MOL_ID: 22;
SOURCE 86 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 87 ORGANISM_TAXID: 262724;
SOURCE 88 STRAIN: HB27;
SOURCE 89 MOL_ID: 23;
SOURCE 90 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 91 ORGANISM_TAXID: 469008;
SOURCE 92 STRAIN: BL21(DE3);
SOURCE 93 MOL_ID: 24
KEYWDS 70S, RIBOSOME, TERMINATION, RELEASE FACTOR, RF1, AMBER, STOP CODON,
KEYWDS 2 UAG
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KOROSTELEV,J.ZHU,H.ASAHARA,H.F.NOLLER
REVDAT 2 18-AUG-10 3MR8 1 JRNL
REVDAT 1 14-JUL-10 3MR8 0
JRNL AUTH A.KOROSTELEV,J.ZHU,H.ASAHARA,H.F.NOLLER
JRNL TITL RECOGNITION OF THE AMBER UAG STOP CODON BY RELEASE FACTOR
JRNL TITL 2 RF1.
JRNL REF EMBO J. V. 29 2577 2010
JRNL REFN ISSN 0261-4189
JRNL PMID 20588254
JRNL DOI 10.1038/EMBOJ.2010.139
REMARK 2
REMARK 2 RESOLUTION. 3.62 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6_289)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.62
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.95
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 663328
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.260
REMARK 3 R VALUE (WORKING SET) : 0.260
REMARK 3 FREE R VALUE : 0.291
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.000
REMARK 3 FREE R VALUE TEST SET COUNT : 13271
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.20
REMARK 3 B_SOL : 68.41
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.590
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 319010
REMARK 3 ANGLE : 0.659 476570
REMARK 3 CHIRALITY : 0.041 60294
REMARK 3 PLANARITY : 0.002 26226
REMARK 3 DIHEDRAL : 18.407 172552
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 4
REMARK 3 NCS GROUP : 2
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 4
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 5
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 6
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 7
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 8
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 9
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 10
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 11
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 12
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 13
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 14
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 15
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 16
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 17
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 18
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 19
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 20
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : segid A16S or segid AS* or segid AT*
REMARK 3 ATOM PAIRS NUMBER : 51443
REMARK 3 RMSD : 0.005
REMARK 3 NCS OPERATOR : 21
REMARK 3 REFERENCE SELECTION: segid A16S or segid AS* or segid AT*
REMARK 3 SELECTION : NULL
REMARK 3 ATOM PAIRS NUMBER : NULL
REMARK 3 RMSD : NULL
REMARK 3 NCS GROUP : 3
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: segid APTN or segid AMRN
REMARK 3 SELECTION : segid APTN or segid AMRN
REMARK 3 ATOM PAIRS NUMBER : 1789
REMARK 3 RMSD : 0.006
REMARK 3 NCS GROUP : 4
REMARK 3 NCS GROUP : 5
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3MR8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JUN-10.
REMARK 100 THE RCSB ID CODE IS RCSB058899.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-AUG-09; NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL; NULL
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 8
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; SSRL
REMARK 200 BEAMLINE : 23-ID-D; BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332; 0.9795
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : NULL; NULL
REMARK 200 DETECTOR MANUFACTURER : NULL; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 723953
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.514
REMARK 200 RESOLUTION RANGE LOW (A) : 89.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: PDB ENTRIES 3F1E AND 3F1F
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN BY THE SITTING-
REMARK 280 DROP VAPOR DIFFUSION METHOD DISPENSED ROBOTICALLY USING 1-2 UL
REMARK 280 RIBOSOME COMPLEXES MIXED WITH 1-2 UL RESERVOIR SOLUTION (100 MM
REMARK 280 TRIS-OAC, PH 7.0, 200 MM KSCN, 3.4-4.8% PEG20,000, 2.5-11.5%
REMARK 280 PEG200) AT 22.5 C, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 295.5K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 105.19000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 308.54500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 226.35000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 308.54500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 105.19000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 226.35000
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 300 REMARK: THE BIOLOGICAL MOLECULE IS COMPOSED OF BOTH THE 30S AND 50S
REMARK 300 SUBUNITS. THIS FILE CONTAINS THE 30S SUBUNIT, RELEASE FACTOR 1
REMARK 300 (RF1), TRNA-FMET BOUND TO THE P SITE, AND MRNA MOLECULES OF ONE 70S
REMARK 300 RIBOSOME. THE ENTIRE CRYSTAL STRUCTURE CONTAINS TWO 70S RIBOSOMES
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: 24-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,
REMARK 350 AND CHAINS: J, K, L, M, N, O, P, Q, R,
REMARK 350 AND CHAINS: S, T, U, V, W, X
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 400
REMARK 400 COMPOUND
REMARK 400 THE COMPLETE ASYMMETRIC UNIT CONTAINS 30S AND 50S RIBOSOMAL
REMARK 400 SUBUNITS OF MOLECULE A AND B. THIS ENTRY 3MR8 CONTAINS 30S
REMARK 400 RIBOSOMAL SUBUNIT. THE 50S RIBOSOMAL SUBUNIT CAN BE FOUND IN PDB
REMARK 400 ENTRY 3MS1. MOLECULE B WAS DEPOSITED AS PDB 3MRZ AND 3MS0
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 O2' G A 438 O4 U A 494 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 A A 243 C3' - O3' - P ANGL. DEV. = 8.4 DEGREES
REMARK 500 G A 266 O4' - C1' - N9 ANGL. DEV. = -5.3 DEGREES
REMARK 500 C A 328 C3' - O3' - P ANGL. DEV. = 9.4 DEGREES
REMARK 500 A A 533 C3' - O3' - P ANGL. DEV. = 8.4 DEGREES
REMARK 500 C A 545 O4' - C1' - N1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 A A 687 C3' - O3' - P ANGL. DEV. = 8.9 DEGREES
REMARK 500 U A 833 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 G A1064 C3' - O3' - P ANGL. DEV. = 9.5 DEGREES
REMARK 500 A A1067 C3' - O3' - P ANGL. DEV. = 8.8 DEGREES
REMARK 500 G A1300 C3' - O3' - P ANGL. DEV. = 10.2 DEGREES
REMARK 500 U A1358 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 C A1397 O4' - C1' - N1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 U A1498 C3' - O3' - P ANGL. DEV. = 8.9 DEGREES
REMARK 500 G A1504 C3' - O3' - P ANGL. DEV. = 10.3 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 VAL B 15 60.66 -154.11
REMARK 500 HIS B 16 64.42 -154.78
REMARK 500 PHE B 17 149.32 -177.75
REMARK 500 HIS B 19 -41.33 -171.03
REMARK 500 ALA B 34 -176.03 -172.20
REMARK 500 GLU B 35 60.97 -160.78
REMARK 500 PHE B 122 -3.58 -149.06
REMARK 500 ALA B 123 7.14 -163.38
REMARK 500 PRO B 125 28.03 -71.16
REMARK 500 GLU B 129 -159.19 -79.98
REMARK 500 ARG B 130 104.42 62.28
REMARK 500 GLN B 135 -70.45 -63.27
REMARK 500 SER B 150 97.03 -55.85
REMARK 500 ASP B 166 92.81 -163.29
REMARK 500 ALA B 186 138.90 -172.78
REMARK 500 ASP B 198 -73.64 -61.64
REMARK 500 ASP B 205 -30.16 -147.11
REMARK 500 ASP B 206 36.34 -84.52
REMARK 500 ARG B 226 -76.23 -87.68
REMARK 500 PRO B 234 92.31 -62.79
REMARK 500 ASN C 3 -80.41 -119.52
REMARK 500 LYS C 4 81.88 54.11
REMARK 500 ILE C 14 -71.79 -78.84
REMARK 500 THR C 15 -101.73 -66.22
REMARK 500 TRP C 22 152.82 175.99
REMARK 500 LYS C 26 3.59 -67.40
REMARK 500 LYS C 45 -77.95 -72.78
REMARK 500 GLU C 46 57.94 -91.22
REMARK 500 LEU C 47 -14.23 -170.29
REMARK 500 ALA C 53 -94.46 -140.60
REMARK 500 ARG C 54 93.38 -69.52
REMARK 500 ALA C 60 -46.90 -161.70
REMARK 500 ALA C 61 90.73 -171.18
REMARK 500 ASP C 62 -9.33 67.72
REMARK 500 GLU C 82 -48.41 -145.13
REMARK 500 THR C 95 -158.62 -92.79
REMARK 500 GLU C 105 -166.82 -66.72
REMARK 500 ASN C 108 108.11 -169.13
REMARK 500 ARG C 127 92.44 55.14
REMARK 500 ALA C 129 97.01 -59.99
REMARK 500 ARG C 156 88.22 -68.49
REMARK 500 PRO C 174 84.90 -68.26
REMARK 500 ARG C 179 61.93 -69.35
REMARK 500 ALA C 187 145.32 -173.64
REMARK 500 ALA C 189 90.53 -173.84
REMARK 500 LEU C 204 -69.83 -146.89
REMARK 500 TYR D 20 50.44 -102.43
REMARK 500 LYS D 22 -151.25 -80.21
REMARK 500 LYS D 30 58.33 -170.71
REMARK 500 CYS D 31 1.29 -67.62
REMARK 500
REMARK 500 THIS ENTRY HAS 247 RAMACHANDRAN OUTLIERS.
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 D 210 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 26 SG
REMARK 620 2 CYS D 31 SG 117.5
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 210
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3F1E RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A TRANSLATION TERMINATION COMPLEX
REMARK 900 FORMED WITH RELEASE FACTOR RF2. THIS FILE CONTAINS THE 30S
REMARK 900 SUBUNIT, RF2, TWO TRNA, AND MRNA MOLECULES OF ONE 70S
REMARK 900 RIBOSOME. THE ENTIRE CRYSTAL STRUCTURE CONTAINS TWO 70S
REMARK 900 RIBOSOMES AS DESCRIBED IN REMARK 400.
REMARK 900 RELATED ID: 3D5A RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR TRANSLATION TERMINATION ON THE 70S
REMARK 900 RIBOSOME. THIS FILE CONTAINS THE 30S SUBUNIT, RELEASE
REMARK 900 FACTOR 1 (RF1), TWO TRNA, AND MRNA MOLECULES OF ONE 70S
REMARK 900 RIBOSOME. THE ENTIRE CRYSTAL STRUCTURE CONTAINS TWO 70S
REMARK 900 RIBOSOMES AS DESCRIBED IN REMARK 400.
REMARK 900 RELATED ID: 1ZBT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF PEPTIDE CHAIN RELEASE FACTOR 1 (RF-1)
REMARK 900 (SMU.1085) FROM STREPTOCOCCUS MUTANS AT 2.34 A RESOLUTION
REMARK 900 RELATED ID: 3MS1 RELATED DB: PDB
REMARK 900 50S SUBUNIT
REMARK 900 RELATED ID: 3MS0 RELATED DB: PDB
REMARK 900 30S SUBUNIT IN MOLECULE B
REMARK 900 RELATED ID: 3MRZ RELATED DB: PDB
REMARK 900 50S SUBUNIT IN MOLECULE B
DBREF1 3MR8 A 5 1531 GB AE017221.1
DBREF2 3MR8 A AE017221 1310206 1311709
DBREF 3MR8 B 7 240 UNP P62662 RS2_THET2 7 240
DBREF 3MR8 C 2 207 UNP P62663 RS3_THET2 2 207
DBREF 3MR8 D 2 209 UNP P62664 RS4_THET2 2 209
DBREF 3MR8 E 5 155 UNP P62665 RS5_THET2 5 155
DBREF 3MR8 F 1 101 UNP P62666 RS6_THET2 1 101
DBREF 3MR8 G 2 156 UNP P62667 RS7_THET2 2 156
DBREF 3MR8 H 1 138 UNP P62668 RS8_THET2 1 138
DBREF 3MR8 I 2 128 UNP P62669 RS9_THET2 2 128
DBREF 3MR8 J 3 100 UNP P62653 RS10_THET2 3 100
DBREF 3MR8 K 11 129 UNP P62654 RS11_THET2 11 129
DBREF 3MR8 L 4 127 UNP P61941 RS12_THET2 2 125
DBREF 3MR8 M 2 118 UNP P62655 RS13_THET2 2 118
DBREF 3MR8 N 2 61 UNP P62656 RS14Z_THET2 2 61
DBREF 3MR8 O 2 89 UNP P62657 RS15_THET2 2 89
DBREF 3MR8 P 1 83 UNP P62238 RS16_THET2 1 83
DBREF 3MR8 Q 2 100 UNP P62658 RS17_THET2 2 100
DBREF 3MR8 R 19 88 UNP P62659 RS18_THET2 19 88
DBREF 3MR8 S 4 81 UNP P62660 RS19_THET2 4 81
DBREF 3MR8 T 8 106 UNP P62661 RS20_THET2 8 106
DBREF 3MR8 U 2 25 UNP P62613 RSHX_THET2 2 25
DBREF 3MR8 V 1 354 UNP Q72HB8 RF1_THET2 1 354
DBREF1 3MR8 W 1 76 GB CP001509.3
DBREF2 3MR8 W CP001509 2785667 2785743
DBREF 3MR8 X 15 21 PDB 3MR8 3MR8 15 21
SEQRES 1 A 1504 U G G A G A G U U U G A U
SEQRES 2 A 1504 C C U G G C U C A G G G U
SEQRES 3 A 1504 G A A C G C U G G C G G C
SEQRES 4 A 1504 G U G C C U A A G A C A U
SEQRES 5 A 1504 G C A A G U C G U G C G G
SEQRES 6 A 1504 G C C G C G G G G U U U U
SEQRES 7 A 1504 A C U C C G U G G U C A G
SEQRES 8 A 1504 C G G C G G A C G G G U G
SEQRES 9 A 1504 A G U A A C G C G U G G G
SEQRES 10 A 1504 U G A C C U A C C C G G A
SEQRES 11 A 1504 A G A G G G G G A C A A C
SEQRES 12 A 1504 C C G G G G A A A C U C G
SEQRES 13 A 1504 G G C U A A U C C C C C A
SEQRES 14 A 1504 U G U G G A C C C G C C C
SEQRES 15 A 1504 C U U G G G G U G U G U C
SEQRES 16 A 1504 C A A A G G G C U U U G C
SEQRES 17 A 1504 C C G C U U C C G G A U G
SEQRES 18 A 1504 G G C C C G C G U C C C A
SEQRES 19 A 1504 U C A G C U A G U U G G U
SEQRES 20 A 1504 G G G G U A A U G G C C C
SEQRES 21 A 1504 A C C A A G G C G A C G A
SEQRES 22 A 1504 C G G G U A G C C G G U C
SEQRES 23 A 1504 U G A G A G G A U G G C C
SEQRES 24 A 1504 G G C C A C A G G G G C A
SEQRES 25 A 1504 C U G A G A C A C G G G C
SEQRES 26 A 1504 C C C A C U C C U A C G G
SEQRES 27 A 1504 G A G G C A G C A G U U A
SEQRES 28 A 1504 G G A A U C U U C C G C A
SEQRES 29 A 1504 A U G G G C G C A A G C C
SEQRES 30 A 1504 U G A C G G A G C G A C G
SEQRES 31 A 1504 C C G C U U G G A G G A A
SEQRES 32 A 1504 G A A G C C C U U C G G G
SEQRES 33 A 1504 G U G U A A A C U C C U G
SEQRES 34 A 1504 A A C C C G G G A C G A A
SEQRES 35 A 1504 A C C C C C G A G G A G G
SEQRES 36 A 1504 G G A C U G A C G G U A C
SEQRES 37 A 1504 C G G G G U A A U A G C G
SEQRES 38 A 1504 C C G G C C A A C U C C G
SEQRES 39 A 1504 U G C C A G C A G C C G C
SEQRES 40 A 1504 G G U A A U A C G G A G G
SEQRES 41 A 1504 G C G C G A G C G U U A C
SEQRES 42 A 1504 C C G G A U U C A C U G G
SEQRES 43 A 1504 G C G U A A A G G G C G U
SEQRES 44 A 1504 G U A G G C G G C C U G G
SEQRES 45 A 1504 G G C G U C C C A U G U G
SEQRES 46 A 1504 A A A G A C C A C G G C U
SEQRES 47 A 1504 C A A C C G U G G G G G A
SEQRES 48 A 1504 G C G U G G G A U A C G C
SEQRES 49 A 1504 U C A G G C U A G A C G G
SEQRES 50 A 1504 U G G G A G A G G G U G G
SEQRES 51 A 1504 U G G A A U U C C C G G A
SEQRES 52 A 1504 G U A G C G G U G A A A U
SEQRES 53 A 1504 G C G C A G A U A C C G G
SEQRES 54 A 1504 G A G G A A C G C C G A U
SEQRES 55 A 1504 G G C G A A G G C A G C C
SEQRES 56 A 1504 A C C U G G U C C A C C C
SEQRES 57 A 1504 G U G A C G C U G A G G C
SEQRES 58 A 1504 G C G A A A G C G U G G G
SEQRES 59 A 1504 G A G C A A A C C G G A U
SEQRES 60 A 1504 U A G A U A C C C G G G U
SEQRES 61 A 1504 A G U C C A C G C C C U A
SEQRES 62 A 1504 A A C G A U G C G C G C U
SEQRES 63 A 1504 A G G U C U C U G G G U C
SEQRES 64 A 1504 U C C U G G G G G C C G A
SEQRES 65 A 1504 A G C U A A C G C G U U A
SEQRES 66 A 1504 A G C G C G C C G C C U G
SEQRES 67 A 1504 G G G A G U A C G G C C G
SEQRES 68 A 1504 C A A G G C U G A A A C U
SEQRES 69 A 1504 C A A A G G A A U U G A C
SEQRES 70 A 1504 G G G G G C C C G C A C A
SEQRES 71 A 1504 A G C G G U G G A G C A U
SEQRES 72 A 1504 G U G G U U U A A U U C G
SEQRES 73 A 1504 A A G C A A C G C G A A G
SEQRES 74 A 1504 A A C C U U A C C A G G C
SEQRES 75 A 1504 C U U G A C A U G C U A G
SEQRES 76 A 1504 G G A A C C C G G G U G A
SEQRES 77 A 1504 A A G C C U G G G G U G C
SEQRES 78 A 1504 C C C G C G A G G G G A G
SEQRES 79 A 1504 C C C U A G C A C A G G U
SEQRES 80 A 1504 G C U G C A U G G C C G U
SEQRES 81 A 1504 C G U C A G C U C G U G C
SEQRES 82 A 1504 C G U G A G G U G U U G G
SEQRES 83 A 1504 G U U A A G U C C C G C A
SEQRES 84 A 1504 A C G A G C G C A A C C C
SEQRES 85 A 1504 C C G C C G U U A G U U G
SEQRES 86 A 1504 C C A G C G G U U C G G C
SEQRES 87 A 1504 C G G G C A C U C U A A C
SEQRES 88 A 1504 G G G A C U G C C C G C G
SEQRES 89 A 1504 A A A G C G G G A G G A A
SEQRES 90 A 1504 G G A G G G G A C G A C G
SEQRES 91 A 1504 U C U G G U C A G C A U G
SEQRES 92 A 1504 G C C C U U A C G G C C U
SEQRES 93 A 1504 G G G C G A C A C A C G U
SEQRES 94 A 1504 G C U A C A A U G C C C A
SEQRES 95 A 1504 C U A C A A A G C G A U G
SEQRES 96 A 1504 C C A C C C G G C A A C G
SEQRES 97 A 1504 G G G A G C U A A U C G C
SEQRES 98 A 1504 A A A A A G G U G G G C C
SEQRES 99 A 1504 C A G U U C G G A U U G G
SEQRES 100 A 1504 G G U C U G C A A C C C G
SEQRES 101 A 1504 A C C C C A U G A A G C C
SEQRES 102 A 1504 G G A A U C G C U A G U A
SEQRES 103 A 1504 A U C G C G G A U C A G C
SEQRES 104 A 1504 C A U G C C G C G G U G A
SEQRES 105 A 1504 A U A C G U U C C C G G G
SEQRES 106 A 1504 C C U U G U A C A C A C C
SEQRES 107 A 1504 G C C C G U C A C G C C A
SEQRES 108 A 1504 U G G G A G C G G G C U C
SEQRES 109 A 1504 U A C C C G A A G U C G C
SEQRES 110 A 1504 C G G G A G C C U A C G G
SEQRES 111 A 1504 G C A G G C G C C G A G G
SEQRES 112 A 1504 G U A G G G C C C G U G A
SEQRES 113 A 1504 C U G G G G C G A A G U C
SEQRES 114 A 1504 G U A A C A A G G U A G C
SEQRES 115 A 1504 U G U A C C G G A A G G U
SEQRES 116 A 1504 G C G G C U G G A
SEQRES 1 B 234 VAL LYS GLU LEU LEU GLU ALA GLY VAL HIS PHE GLY HIS
SEQRES 2 B 234 GLU ARG LYS ARG TRP ASN PRO LYS PHE ALA ARG TYR ILE
SEQRES 3 B 234 TYR ALA GLU ARG ASN GLY ILE HIS ILE ILE ASP LEU GLN
SEQRES 4 B 234 LYS THR MET GLU GLU LEU GLU ARG THR PHE ARG PHE ILE
SEQRES 5 B 234 GLU ASP LEU ALA MET ARG GLY GLY THR ILE LEU PHE VAL
SEQRES 6 B 234 GLY THR LYS LYS GLN ALA GLN ASP ILE VAL ARG MET GLU
SEQRES 7 B 234 ALA GLU ARG ALA GLY MET PRO TYR VAL ASN GLN ARG TRP
SEQRES 8 B 234 LEU GLY GLY MET LEU THR ASN PHE LYS THR ILE SER GLN
SEQRES 9 B 234 ARG VAL HIS ARG LEU GLU GLU LEU GLU ALA LEU PHE ALA
SEQRES 10 B 234 SER PRO GLU ILE GLU GLU ARG PRO LYS LYS GLU GLN VAL
SEQRES 11 B 234 ARG LEU LYS HIS GLU LEU GLU ARG LEU GLN LYS TYR LEU
SEQRES 12 B 234 SER GLY PHE ARG LEU LEU LYS ARG LEU PRO ASP ALA ILE
SEQRES 13 B 234 PHE VAL VAL ASP PRO THR LYS GLU ALA ILE ALA VAL ARG
SEQRES 14 B 234 GLU ALA ARG LYS LEU PHE ILE PRO VAL ILE ALA LEU ALA
SEQRES 15 B 234 ASP THR ASP SER ASP PRO ASP LEU VAL ASP TYR ILE ILE
SEQRES 16 B 234 PRO GLY ASN ASP ASP ALA ILE ARG SER ILE GLN LEU ILE
SEQRES 17 B 234 LEU SER ARG ALA VAL ASP LEU ILE ILE GLN ALA ARG GLY
SEQRES 18 B 234 GLY VAL VAL GLU PRO SER PRO SER TYR ALA LEU VAL GLN
SEQRES 1 C 206 GLY ASN LYS ILE HIS PRO ILE GLY PHE ARG LEU GLY ILE
SEQRES 2 C 206 THR ARG ASP TRP GLU SER ARG TRP TYR ALA GLY LYS LYS
SEQRES 3 C 206 GLN TYR ARG HIS LEU LEU LEU GLU ASP GLN ARG ILE ARG
SEQRES 4 C 206 GLY LEU LEU GLU LYS GLU LEU TYR SER ALA GLY LEU ALA
SEQRES 5 C 206 ARG VAL ASP ILE GLU ARG ALA ALA ASP ASN VAL ALA VAL
SEQRES 6 C 206 THR VAL HIS VAL ALA LYS PRO GLY VAL VAL ILE GLY ARG
SEQRES 7 C 206 GLY GLY GLU ARG ILE ARG VAL LEU ARG GLU GLU LEU ALA
SEQRES 8 C 206 LYS LEU THR GLY LYS ASN VAL ALA LEU ASN VAL GLN GLU
SEQRES 9 C 206 VAL GLN ASN PRO ASN LEU SER ALA PRO LEU VAL ALA GLN
SEQRES 10 C 206 ARG VAL ALA GLU GLN ILE GLU ARG ARG PHE ALA VAL ARG
SEQRES 11 C 206 ARG ALA ILE LYS GLN ALA VAL GLN ARG VAL MET GLU SER
SEQRES 12 C 206 GLY ALA LYS GLY ALA LYS VAL ILE VAL SER GLY ARG ILE
SEQRES 13 C 206 GLY GLY ALA GLU GLN ALA ARG THR GLU TRP ALA ALA GLN
SEQRES 14 C 206 GLY ARG VAL PRO LEU HIS THR LEU ARG ALA ASN ILE ASP
SEQRES 15 C 206 TYR GLY PHE ALA LEU ALA ARG THR THR TYR GLY VAL LEU
SEQRES 16 C 206 GLY VAL LYS ALA TYR ILE PHE LEU GLY GLU VAL
SEQRES 1 D 208 GLY ARG TYR ILE GLY PRO VAL CYS ARG LEU CYS ARG ARG
SEQRES 2 D 208 GLU GLY VAL LYS LEU TYR LEU LYS GLY GLU ARG CYS TYR
SEQRES 3 D 208 SER PRO LYS CYS ALA MET GLU ARG ARG PRO TYR PRO PRO
SEQRES 4 D 208 GLY GLN HIS GLY GLN LYS ARG ALA ARG ARG PRO SER ASP
SEQRES 5 D 208 TYR ALA VAL ARG LEU ARG GLU LYS GLN LYS LEU ARG ARG
SEQRES 6 D 208 ILE TYR GLY ILE SER GLU ARG GLN PHE ARG ASN LEU PHE
SEQRES 7 D 208 GLU GLU ALA SER LYS LYS LYS GLY VAL THR GLY SER VAL
SEQRES 8 D 208 PHE LEU GLY LEU LEU GLU SER ARG LEU ASP ASN VAL VAL
SEQRES 9 D 208 TYR ARG LEU GLY PHE ALA VAL SER ARG ARG GLN ALA ARG
SEQRES 10 D 208 GLN LEU VAL ARG HIS GLY HIS ILE THR VAL ASN GLY ARG
SEQRES 11 D 208 ARG VAL ASP LEU PRO SER TYR ARG VAL ARG PRO GLY ASP
SEQRES 12 D 208 GLU ILE ALA VAL ALA GLU LYS SER ARG ASN LEU GLU LEU
SEQRES 13 D 208 ILE ARG GLN ASN LEU GLU ALA MET LYS GLY ARG LYS VAL
SEQRES 14 D 208 GLY PRO TRP LEU SER LEU ASP VAL GLU GLY MET LYS GLY
SEQRES 15 D 208 LYS PHE LEU ARG LEU PRO ASP ARG GLU ASP LEU ALA LEU
SEQRES 16 D 208 PRO VAL ASN GLU GLN LEU VAL ILE GLU PHE TYR SER ARG
SEQRES 1 E 151 ASP PHE GLU GLU LYS MET ILE LEU ILE ARG ARG THR ALA
SEQRES 2 E 151 ARG MET GLN ALA GLY GLY ARG ARG PHE ARG PHE GLY ALA
SEQRES 3 E 151 LEU VAL VAL VAL GLY ASP ARG GLN GLY ARG VAL GLY LEU
SEQRES 4 E 151 GLY PHE GLY LYS ALA PRO GLU VAL PRO LEU ALA VAL GLN
SEQRES 5 E 151 LYS ALA GLY TYR TYR ALA ARG ARG ASN MET VAL GLU VAL
SEQRES 6 E 151 PRO LEU GLN ASN GLY THR ILE PRO HIS GLU ILE GLU VAL
SEQRES 7 E 151 GLU PHE GLY ALA SER LYS ILE VAL LEU LYS PRO ALA ALA
SEQRES 8 E 151 PRO GLY THR GLY VAL ILE ALA GLY ALA VAL PRO ARG ALA
SEQRES 9 E 151 ILE LEU GLU LEU ALA GLY VAL THR ASP ILE LEU THR LYS
SEQRES 10 E 151 GLU LEU GLY SER ARG ASN PRO ILE ASN ILE ALA TYR ALA
SEQRES 11 E 151 THR MET GLU ALA LEU ARG GLN LEU ARG THR LYS ALA ASP
SEQRES 12 E 151 VAL GLU ARG LEU ARG LYS GLY GLU
SEQRES 1 F 101 MET ARG ARG TYR GLU VAL ASN ILE VAL LEU ASN PRO ASN
SEQRES 2 F 101 LEU ASP GLN SER GLN LEU ALA LEU GLU LYS GLU ILE ILE
SEQRES 3 F 101 GLN ARG ALA LEU GLU ASN TYR GLY ALA ARG VAL GLU LYS
SEQRES 4 F 101 VAL GLU GLU LEU GLY LEU ARG ARG LEU ALA TYR PRO ILE
SEQRES 5 F 101 ALA LYS ASP PRO GLN GLY TYR PHE LEU TRP TYR GLN VAL
SEQRES 6 F 101 GLU MET PRO GLU ASP ARG VAL ASN ASP LEU ALA ARG GLU
SEQRES 7 F 101 LEU ARG ILE ARG ASP ASN VAL ARG ARG VAL MET VAL VAL
SEQRES 8 F 101 LYS SER GLN GLU PRO PHE LEU ALA ASN ALA
SEQRES 1 G 155 ALA ARG ARG ARG ARG ALA GLU VAL ARG GLN LEU GLN PRO
SEQRES 2 G 155 ASP LEU VAL TYR GLY ASP VAL LEU VAL THR ALA PHE ILE
SEQRES 3 G 155 ASN LYS ILE MET ARG ASP GLY LYS LYS ASN LEU ALA ALA
SEQRES 4 G 155 ARG ILE PHE TYR ASP ALA CYS LYS ILE ILE GLN GLU LYS
SEQRES 5 G 155 THR GLY GLN GLU PRO LEU LYS VAL PHE LYS GLN ALA VAL
SEQRES 6 G 155 GLU ASN VAL LYS PRO ARG MET GLU VAL ARG SER ARG ARG
SEQRES 7 G 155 VAL GLY GLY ALA ASN TYR GLN VAL PRO MET GLU VAL SER
SEQRES 8 G 155 PRO ARG ARG GLN GLN SER LEU ALA LEU ARG TRP LEU VAL
SEQRES 9 G 155 GLN ALA ALA ASN GLN ARG PRO GLU ARG ARG ALA ALA VAL
SEQRES 10 G 155 ARG ILE ALA HIS GLU LEU MET ASP ALA ALA GLU GLY LYS
SEQRES 11 G 155 GLY GLY ALA VAL LYS LYS LYS GLU ASP VAL GLU ARG MET
SEQRES 12 G 155 ALA GLU ALA ASN ARG ALA TYR ALA HIS TYR ARG TRP
SEQRES 1 H 138 MET LEU THR ASP PRO ILE ALA ASP MET LEU THR ARG ILE
SEQRES 2 H 138 ARG ASN ALA THR ARG VAL TYR LYS GLU SER THR ASP VAL
SEQRES 3 H 138 PRO ALA SER ARG PHE LYS GLU GLU ILE LEU ARG ILE LEU
SEQRES 4 H 138 ALA ARG GLU GLY PHE ILE LYS GLY TYR GLU ARG VAL ASP
SEQRES 5 H 138 VAL ASP GLY LYS PRO TYR LEU ARG VAL TYR LEU LYS TYR
SEQRES 6 H 138 GLY PRO ARG ARG GLN GLY PRO ASP PRO ARG PRO GLU GLN
SEQRES 7 H 138 VAL ILE HIS HIS ILE ARG ARG ILE SER LYS PRO GLY ARG
SEQRES 8 H 138 ARG VAL TYR VAL GLY VAL LYS GLU ILE PRO ARG VAL ARG
SEQRES 9 H 138 ARG GLY LEU GLY ILE ALA ILE LEU SER THR SER LYS GLY
SEQRES 10 H 138 VAL LEU THR ASP ARG GLU ALA ARG LYS LEU GLY VAL GLY
SEQRES 11 H 138 GLY GLU LEU ILE CYS GLU VAL TRP
SEQRES 1 I 127 GLU GLN TYR TYR GLY THR GLY ARG ARG LYS GLU ALA VAL
SEQRES 2 I 127 ALA ARG VAL PHE LEU ARG PRO GLY ASN GLY LYS VAL THR
SEQRES 3 I 127 VAL ASN GLY GLN ASP PHE ASN GLU TYR PHE GLN GLY LEU
SEQRES 4 I 127 VAL ARG ALA VAL ALA ALA LEU GLU PRO LEU ARG ALA VAL
SEQRES 5 I 127 ASP ALA LEU GLY ARG PHE ASP ALA TYR ILE THR VAL ARG
SEQRES 6 I 127 GLY GLY GLY LYS SER GLY GLN ILE ASP ALA ILE LYS LEU
SEQRES 7 I 127 GLY ILE ALA ARG ALA LEU VAL GLN TYR ASN PRO ASP TYR
SEQRES 8 I 127 ARG ALA LYS LEU LYS PRO LEU GLY PHE LEU THR ARG ASP
SEQRES 9 I 127 ALA ARG VAL VAL GLU ARG LYS LYS TYR GLY LYS HIS LYS
SEQRES 10 I 127 ALA ARG ARG ALA PRO GLN TYR SER LYS ARG
SEQRES 1 J 98 LYS ILE ARG ILE LYS LEU ARG GLY PHE ASP HIS LYS THR
SEQRES 2 J 98 LEU ASP ALA SER ALA GLN LYS ILE VAL GLU ALA ALA ARG
SEQRES 3 J 98 ARG SER GLY ALA GLN VAL SER GLY PRO ILE PRO LEU PRO
SEQRES 4 J 98 THR ARG VAL ARG ARG PHE THR VAL ILE ARG GLY PRO PHE
SEQRES 5 J 98 LYS HIS LYS ASP SER ARG GLU HIS PHE GLU LEU ARG THR
SEQRES 6 J 98 HIS ASN ARG LEU VAL ASP ILE ILE ASN PRO ASN ARG LYS
SEQRES 7 J 98 THR ILE GLU GLN LEU MET THR LEU ASP LEU PRO THR GLY
SEQRES 8 J 98 VAL GLU ILE GLU ILE LYS THR
SEQRES 1 K 119 LYS ARG GLN VAL ALA SER GLY ARG ALA TYR ILE HIS ALA
SEQRES 2 K 119 SER TYR ASN ASN THR ILE VAL THR ILE THR ASP PRO ASP
SEQRES 3 K 119 GLY ASN PRO ILE THR TRP SER SER GLY GLY VAL ILE GLY
SEQRES 4 K 119 TYR LYS GLY SER ARG LYS GLY THR PRO TYR ALA ALA GLN
SEQRES 5 K 119 LEU ALA ALA LEU ASP ALA ALA LYS LYS ALA MET ALA TYR
SEQRES 6 K 119 GLY MET GLN SER VAL ASP VAL ILE VAL ARG GLY THR GLY
SEQRES 7 K 119 ALA GLY ARG GLU GLN ALA ILE ARG ALA LEU GLN ALA SER
SEQRES 8 K 119 GLY LEU GLN VAL LYS SER ILE VAL ASP ASP THR PRO VAL
SEQRES 9 K 119 PRO HIS ASN GLY CYS ARG PRO LYS LYS LYS PHE ARG LYS
SEQRES 10 K 119 ALA SER
SEQRES 1 L 124 PRO THR ILE ASN GLN LEU VAL ARG LYS GLY ARG GLU LYS
SEQRES 2 L 124 VAL ARG LYS LYS SER LYS VAL PRO ALA LEU LYS GLY ALA
SEQRES 3 L 124 PRO PHE ARG ARG GLY VAL CYS THR VAL VAL ARG THR VAL
SEQRES 4 L 124 THR PRO LYS LYS PRO ASN SER ALA LEU ARG LYS VAL ALA
SEQRES 5 L 124 LYS VAL ARG LEU THR SER GLY TYR GLU VAL THR ALA TYR
SEQRES 6 L 124 ILE PRO GLY GLU GLY HIS ASN LEU GLN GLU HIS SER VAL
SEQRES 7 L 124 VAL LEU ILE ARG GLY GLY ARG VAL LYS ASP LEU PRO GLY
SEQRES 8 L 124 VAL ARG TYR HIS ILE VAL ARG GLY VAL TYR ASP ALA ALA
SEQRES 9 L 124 GLY VAL LYS ASP ARG LYS LYS SER ARG SER LYS TYR GLY
SEQRES 10 L 124 THR LYS LYS PRO LYS GLU ALA
SEQRES 1 M 117 ALA ARG ILE ALA GLY VAL GLU ILE PRO ARG ASN LYS ARG
SEQRES 2 M 117 VAL ASP VAL ALA LEU THR TYR ILE TYR GLY ILE GLY LYS
SEQRES 3 M 117 ALA ARG ALA LYS GLU ALA LEU GLU LYS THR GLY ILE ASN
SEQRES 4 M 117 PRO ALA THR ARG VAL LYS ASP LEU THR GLU ALA GLU VAL
SEQRES 5 M 117 VAL ARG LEU ARG GLU TYR VAL GLU ASN THR TRP LYS LEU
SEQRES 6 M 117 GLU GLY GLU LEU ARG ALA GLU VAL ALA ALA ASN ILE LYS
SEQRES 7 M 117 ARG LEU MET ASP ILE GLY CYS TYR ARG GLY LEU ARG HIS
SEQRES 8 M 117 ARG ARG GLY LEU PRO VAL ARG GLY GLN ARG THR ARG THR
SEQRES 9 M 117 ASN ALA ARG THR ARG LYS GLY PRO ARG LYS THR VAL ALA
SEQRES 1 N 60 ALA ARG LYS ALA LEU ILE GLU LYS ALA LYS ARG THR PRO
SEQRES 2 N 60 LYS PHE LYS VAL ARG ALA TYR THR ARG CYS VAL ARG CYS
SEQRES 3 N 60 GLY ARG ALA ARG SER VAL TYR ARG PHE PHE GLY LEU CYS
SEQRES 4 N 60 ARG ILE CYS LEU ARG GLU LEU ALA HIS LYS GLY GLN LEU
SEQRES 5 N 60 PRO GLY VAL ARG LYS ALA SER TRP
SEQRES 1 O 88 PRO ILE THR LYS GLU GLU LYS GLN LYS VAL ILE GLN GLU
SEQRES 2 O 88 PHE ALA ARG PHE PRO GLY ASP THR GLY SER THR GLU VAL
SEQRES 3 O 88 GLN VAL ALA LEU LEU THR LEU ARG ILE ASN ARG LEU SER
SEQRES 4 O 88 GLU HIS LEU LYS VAL HIS LYS LYS ASP HIS HIS SER HIS
SEQRES 5 O 88 ARG GLY LEU LEU MET MET VAL GLY GLN ARG ARG ARG LEU
SEQRES 6 O 88 LEU ARG TYR LEU GLN ARG GLU ASP PRO GLU ARG TYR ARG
SEQRES 7 O 88 ALA LEU ILE GLU LYS LEU GLY ILE ARG GLY
SEQRES 1 P 83 MET VAL LYS ILE ARG LEU ALA ARG PHE GLY SER LYS HIS
SEQRES 2 P 83 ASN PRO HIS TYR ARG ILE VAL VAL THR ASP ALA ARG ARG
SEQRES 3 P 83 LYS ARG ASP GLY LYS TYR ILE GLU LYS ILE GLY TYR TYR
SEQRES 4 P 83 ASP PRO ARG LYS THR THR PRO ASP TRP LEU LYS VAL ASP
SEQRES 5 P 83 VAL GLU ARG ALA ARG TYR TRP LEU SER VAL GLY ALA GLN
SEQRES 6 P 83 PRO THR ASP THR ALA ARG ARG LEU LEU ARG GLN ALA GLY
SEQRES 7 P 83 VAL PHE ARG GLN GLU
SEQRES 1 Q 99 PRO LYS LYS VAL LEU THR GLY VAL VAL VAL SER ASP LYS
SEQRES 2 Q 99 MET GLN LYS THR VAL THR VAL LEU VAL GLU ARG GLN PHE
SEQRES 3 Q 99 PRO HIS PRO LEU TYR GLY LYS VAL ILE LYS ARG SER LYS
SEQRES 4 Q 99 LYS TYR LEU ALA HIS ASP PRO GLU GLU LYS TYR LYS LEU
SEQRES 5 Q 99 GLY ASP VAL VAL GLU ILE ILE GLU SER ARG PRO ILE SER
SEQRES 6 Q 99 LYS ARG LYS ARG PHE ARG VAL LEU ARG LEU VAL GLU SER
SEQRES 7 Q 99 GLY ARG MET ASP LEU VAL GLU LYS TYR LEU ILE ARG ARG
SEQRES 8 Q 99 GLN ASN TYR GLN SER LEU SER LYS
SEQRES 1 R 70 LYS ALA LYS VAL LYS ALA THR LEU GLY GLU PHE ASP LEU
SEQRES 2 R 70 ARG ASP TYR ARG ASN VAL GLU VAL LEU LYS ARG PHE LEU
SEQRES 3 R 70 SER GLU THR GLY LYS ILE LEU PRO ARG ARG ARG THR GLY
SEQRES 4 R 70 LEU SER ALA LYS GLU GLN ARG ILE LEU ALA LYS THR ILE
SEQRES 5 R 70 LYS ARG ALA ARG ILE LEU GLY LEU LEU PRO PHE THR GLU
SEQRES 6 R 70 LYS LEU VAL ARG LYS
SEQRES 1 S 78 SER LEU LYS LYS GLY VAL PHE VAL ASP ASP HIS LEU LEU
SEQRES 2 S 78 GLU LYS VAL LEU GLU LEU ASN ALA LYS GLY GLU LYS ARG
SEQRES 3 S 78 LEU ILE LYS THR TRP SER ARG ARG SER THR ILE VAL PRO
SEQRES 4 S 78 GLU MET VAL GLY HIS THR ILE ALA VAL TYR ASN GLY LYS
SEQRES 5 S 78 GLN HIS VAL PRO VAL TYR ILE THR GLU ASN MET VAL GLY
SEQRES 6 S 78 HIS LYS LEU GLY GLU PHE ALA PRO THR ARG THR TYR ARG
SEQRES 1 T 99 ARG ASN LEU SER ALA LEU LYS ARG HIS ARG GLN SER LEU
SEQRES 2 T 99 LYS ARG ARG LEU ARG ASN LYS ALA LYS LYS SER ALA ILE
SEQRES 3 T 99 LYS THR LEU SER LYS LYS ALA VAL GLN LEU ALA GLN GLU
SEQRES 4 T 99 GLY LYS ALA GLU GLU ALA LEU LYS ILE MET ARG LYS ALA
SEQRES 5 T 99 GLU SER LEU ILE ASP LYS ALA ALA LYS GLY SER THR LEU
SEQRES 6 T 99 HIS LYS ASN ALA ALA ALA ARG ARG LYS SER ARG LEU MET
SEQRES 7 T 99 ARG LYS VAL ARG GLN LEU LEU GLU ALA ALA GLY ALA PRO
SEQRES 8 T 99 LEU ILE GLY GLY GLY LEU SER ALA
SEQRES 1 U 24 GLY LYS GLY ASP ARG ARG THR ARG ARG GLY LYS ILE TRP
SEQRES 2 U 24 ARG GLY THR TYR GLY LYS TYR ARG PRO ARG LYS
SEQRES 1 V 354 MET LEU ASP LYS LEU ASP ARG LEU GLU GLU GLU TYR ARG
SEQRES 2 V 354 GLU LEU GLU ALA LEU LEU SER ASP PRO GLU VAL LEU LYS
SEQRES 3 V 354 ASP LYS GLY ARG TYR GLN SER LEU SER ARG ARG TYR ALA
SEQRES 4 V 354 GLU MET GLY GLU VAL ILE GLY LEU ILE ARG GLU TYR ARG
SEQRES 5 V 354 LYS VAL LEU GLU ASP LEU GLU GLN ALA GLU SER LEU LEU
SEQRES 6 V 354 ASP ASP PRO GLU LEU LYS GLU MET ALA LYS ALA GLU ARG
SEQRES 7 V 354 GLU ALA LEU LEU ALA ARG LYS GLU ALA LEU GLU LYS GLU
SEQRES 8 V 354 LEU GLU ARG HIS LEU LEU PRO LYS ASP PRO MET ASP GLU
SEQRES 9 V 354 ARG ASP ALA ILE VAL GLU ILE ARG ALA GLY THR GLY GLY
SEQRES 10 V 354 GLU GLU ALA ALA LEU PHE ALA ARG ASP LEU PHE ASN MET
SEQRES 11 V 354 TYR LEU ARG PHE ALA GLU GLU MET GLY PHE GLU THR GLU
SEQRES 12 V 354 VAL LEU ASP SER HIS PRO THR ASP LEU GLY GLY PHE SER
SEQRES 13 V 354 LYS VAL VAL PHE GLU VAL ARG GLY PRO GLY ALA TYR GLY
SEQRES 14 V 354 THR PHE LYS TYR GLU SER GLY VAL HIS ARG VAL GLN ARG
SEQRES 15 V 354 VAL PRO VAL THR GLU THR GLN GLY ARG ILE HIS THR SER
SEQRES 16 V 354 THR ALA THR VAL ALA VAL LEU PRO LYS ALA GLU GLU GLU
SEQRES 17 V 354 ASP PHE ALA LEU ASN MET ASP GLU ILE ARG ILE ASP VAL
SEQRES 18 V 354 MET ARG ALA SER GLY PRO GLY GLY GLN GLY VAL ASN THR
SEQRES 19 V 354 THR ASP SER ALA VAL ARG VAL VAL HIS LEU PRO THR GLY
SEQRES 20 V 354 ILE MET VAL THR CYS GLN ASP SER ARG SER GLN ILE LYS
SEQRES 21 V 354 ASN ARG GLU LYS ALA LEU MET ILE LEU ARG SER ARG LEU
SEQRES 22 V 354 LEU GLU MET LYS ARG ALA GLU GLU ALA GLU ARG LEU ARG
SEQRES 23 V 354 LYS THR ARG LEU ALA GLN ILE GLY THR GLY GLU ARG SER
SEQRES 24 V 354 GLU LYS ILE ARG THR TYR ASN PHE PRO GLN SER ARG VAL
SEQRES 25 V 354 THR ASP HIS ARG ILE GLY PHE THR THR HIS ASP LEU GLU
SEQRES 26 V 354 GLY VAL LEU SER GLY HIS LEU THR PRO ILE LEU GLU ALA
SEQRES 27 V 354 LEU LYS ARG ALA ASP GLN GLU ARG GLN LEU ALA ALA LEU
SEQRES 28 V 354 ALA GLU GLY
SEQRES 1 W 77 C G C G G G G U G G A G C
SEQRES 2 W 77 A G C C U G G U A G C U C
SEQRES 3 W 77 G U C G G G C U C A U A A
SEQRES 4 W 77 C C C G A A G G U C G U C
SEQRES 5 W 77 G G U U C A A A U C C G G
SEQRES 6 W 77 C C C C C G C A A C C A
SEQRES 1 X 7 A A U G U A G
HET ZN N 1 1
HET ZN D 210 1
HETNAM ZN ZINC ION
FORMUL 25 ZN 2(ZN 2+)
HELIX 1 1 VAL B 7 HIS B 16 1 10
HELIX 2 2 ASN B 25 ARG B 30 1 6
HELIX 3 3 ASP B 43 GLY B 65 1 23
HELIX 4 4 LYS B 74 ARG B 87 1 14
HELIX 5 5 ASN B 104 LEU B 121 1 18
HELIX 6 6 PRO B 131 SER B 150 1 20
HELIX 7 7 GLU B 170 LEU B 180 1 11
HELIX 8 8 ASP B 193 VAL B 197 5 5
HELIX 9 9 ALA B 207 GLY B 227 1 21
HELIX 10 10 SER B 235 GLN B 240 1 6
HELIX 11 11 HIS C 6 LEU C 12 1 7
HELIX 12 12 GLN C 28 GLU C 46 1 19
HELIX 13 13 LEU C 47 ALA C 50 5 4
HELIX 14 14 GLU C 82 THR C 95 1 14
HELIX 15 15 SER C 112 ARG C 126 1 15
HELIX 16 16 ALA C 129 GLY C 145 1 17
HELIX 17 17 VAL D 8 GLY D 16 1 9
HELIX 18 18 GLY D 23 SER D 28 1 6
HELIX 19 19 SER D 52 GLY D 69 1 18
HELIX 20 20 SER D 71 LYS D 85 1 15
HELIX 21 21 VAL D 88 ARG D 100 1 13
HELIX 22 22 ARG D 100 ARG D 107 1 8
HELIX 23 23 SER D 113 HIS D 123 1 11
HELIX 24 24 GLU D 150 ASN D 154 5 5
HELIX 25 25 LEU D 155 MET D 165 1 11
HELIX 26 26 ASN D 199 SER D 208 1 10
HELIX 27 27 GLU E 50 ASN E 65 1 16
HELIX 28 28 GLY E 103 ALA E 113 1 11
HELIX 29 29 ASN E 127 ARG E 140 1 14
HELIX 30 30 THR E 144 GLY E 154 1 11
HELIX 31 31 ASP F 15 GLY F 34 1 20
HELIX 32 32 PRO F 51 ASP F 55 5 5
HELIX 33 33 ARG F 71 ILE F 81 1 11
HELIX 34 34 ASP G 20 MET G 31 1 12
HELIX 35 35 LYS G 35 THR G 54 1 20
HELIX 36 36 GLU G 57 VAL G 69 1 13
HELIX 37 37 SER G 92 ARG G 111 1 20
HELIX 38 38 ARG G 115 GLY G 130 1 16
HELIX 39 39 GLY G 132 ASN G 148 1 17
HELIX 40 40 ARG G 149 TYR G 154 5 6
HELIX 41 41 ASP H 4 VAL H 19 1 16
HELIX 42 42 SER H 29 GLU H 42 1 14
HELIX 43 43 GLY H 96 ILE H 100 5 5
HELIX 44 44 THR H 120 GLY H 128 1 9
HELIX 45 45 ASP I 32 PHE I 37 1 6
HELIX 46 46 VAL I 41 LEU I 47 1 7
HELIX 47 47 LEU I 47 VAL I 53 1 7
HELIX 48 48 GLY I 69 TYR I 88 1 20
HELIX 49 49 TYR I 92 LYS I 97 1 6
HELIX 50 50 ASP J 12 ARG J 29 1 18
HELIX 51 51 ASN J 78 LEU J 88 1 11
HELIX 52 52 GLY K 45 GLY K 49 1 5
HELIX 53 53 GLY K 52 THR K 57 1 6
HELIX 54 54 THR K 57 MET K 73 1 17
HELIX 55 55 ALA K 74 GLY K 76 5 3
HELIX 56 56 GLY K 90 GLY K 102 1 13
HELIX 57 57 THR L 5 LYS L 12 1 8
HELIX 58 58 ARG M 14 TYR M 21 1 8
HELIX 59 59 GLY M 26 LYS M 36 1 11
HELIX 60 60 ARG M 44 LEU M 48 5 5
HELIX 61 61 THR M 49 TRP M 64 1 16
HELIX 62 62 LEU M 66 ILE M 84 1 19
HELIX 63 63 CYS M 86 GLY M 95 1 10
HELIX 64 64 ALA M 107 GLY M 112 1 6
HELIX 65 65 ARG N 3 ALA N 10 1 8
HELIX 66 66 CYS N 40 GLY N 51 1 12
HELIX 67 67 THR O 4 PHE O 15 1 12
HELIX 68 68 SER O 24 HIS O 46 1 23
HELIX 69 69 ASP O 49 ASP O 74 1 26
HELIX 70 70 ASP O 74 GLY O 86 1 13
HELIX 71 71 ASP P 52 VAL P 62 1 11
HELIX 72 72 THR P 67 GLY P 78 1 12
HELIX 73 73 ARG Q 81 GLN Q 96 1 16
HELIX 74 74 LYS R 21 LEU R 26 1 6
HELIX 75 75 ASN R 36 ARG R 42 1 7
HELIX 76 76 PRO R 52 GLY R 57 1 6
HELIX 77 77 SER R 59 LEU R 76 1 18
HELIX 78 78 ASP S 12 ALA S 24 1 13
HELIX 79 79 VAL S 41 VAL S 45 5 5
HELIX 80 80 ALA T 12 GLY T 47 1 36
HELIX 81 81 ALA T 49 GLY T 69 1 21
HELIX 82 82 ASN T 75 GLU T 93 1 19
HELIX 83 83 THR U 8 ARG U 15 1 8
HELIX 84 84 MET V 1 ASP V 21 1 21
HELIX 85 85 GLU V 23 LYS V 26 5 4
HELIX 86 86 ASP V 27 SER V 63 1 37
HELIX 87 87 ASP V 67 LEU V 97 1 31
HELIX 88 88 GLY V 117 MET V 138 1 22
HELIX 89 89 ALA V 167 LYS V 172 1 6
HELIX 90 90 TYR V 173 SER V 175 5 3
HELIX 91 91 ASN V 213 ASP V 215 5 3
HELIX 92 92 GLY V 229 THR V 235 1 7
HELIX 93 93 SER V 257 ILE V 293 1 37
HELIX 94 94 ASP V 323 LEU V 328 1 6
HELIX 95 95 LEU V 332 ALA V 352 1 21
SHEET 1 A 2 ILE B 32 ALA B 34 0
SHEET 2 A 2 ILE B 41 ILE B 42 -1 O ILE B 41 N TYR B 33
SHEET 1 B 5 TYR B 92 VAL B 93 0
SHEET 2 B 5 ILE B 68 VAL B 71 1 N PHE B 70 O VAL B 93
SHEET 3 B 5 ALA B 161 VAL B 164 1 O ALA B 161 N LEU B 69
SHEET 4 B 5 VAL B 184 ALA B 188 1 O ILE B 185 N ILE B 162
SHEET 5 B 5 TYR B 199 PRO B 202 1 O ILE B 201 N ALA B 188
SHEET 1 C 4 ARG C 21 TRP C 22 0
SHEET 2 C 4 GLU C 58 ARG C 59 1 O ARG C 59 N ARG C 21
SHEET 3 C 4 ASN C 63 ALA C 65 -1 O ALA C 65 N GLU C 58
SHEET 4 C 4 ASN C 98 ALA C 100 1 O ASN C 98 N VAL C 64
SHEET 1 D 3 LEU C 52 VAL C 55 0
SHEET 2 D 3 VAL C 68 VAL C 70 -1 O HIS C 69 N ALA C 53
SHEET 3 D 3 VAL C 103 GLN C 104 1 O GLN C 104 N VAL C 70
SHEET 1 E 4 THR C 165 GLY C 171 0
SHEET 2 E 4 GLY C 148 SER C 154 -1 N ALA C 149 O GLN C 170
SHEET 3 E 4 GLY C 197 ILE C 202 -1 O GLY C 197 N SER C 154
SHEET 4 E 4 ASP C 183 TYR C 184 -1 N ASP C 183 O ILE C 202
SHEET 1 F 2 LEU D 174 ASP D 177 0
SHEET 2 F 2 LYS D 182 PHE D 185 -1 O LYS D 182 N ASP D 177
SHEET 1 G 3 GLU E 7 GLN E 20 0
SHEET 2 G 3 GLY E 23 GLY E 35 -1 O LEU E 31 N ILE E 11
SHEET 3 G 3 VAL E 41 ALA E 48 -1 O GLY E 42 N VAL E 34
SHEET 1 H 4 ILE E 80 PHE E 84 0
SHEET 2 H 4 SER E 87 PRO E 93 -1 O ILE E 89 N VAL E 82
SHEET 3 H 4 ASP E 117 GLY E 124 -1 O LEU E 119 N LYS E 92
SHEET 4 H 4 GLY E 99 ILE E 101 1 O ILE E 101 N ILE E 118
SHEET 1 I 3 ARG F 36 VAL F 37 0
SHEET 2 I 3 TYR F 59 GLU F 66 -1 O GLU F 66 N ARG F 36
SHEET 3 I 3 GLY F 44 LEU F 45 -1 N GLY F 44 O PHE F 60
SHEET 1 J 4 ARG F 36 VAL F 37 0
SHEET 2 J 4 TYR F 59 GLU F 66 -1 O GLU F 66 N ARG F 36
SHEET 3 J 4 ARG F 3 LEU F 10 -1 N TYR F 4 O VAL F 65
SHEET 4 J 4 VAL F 85 LYS F 92 -1 O VAL F 91 N GLU F 5
SHEET 1 K 2 LEU F 98 ALA F 99 0
SHEET 2 K 2 PHE R 29 ASP R 30 -1 O PHE R 29 N ALA F 99
SHEET 1 L 2 MET G 73 ARG G 76 0
SHEET 2 L 2 VAL G 87 GLU G 90 -1 O VAL G 87 N ARG G 76
SHEET 1 M 3 SER H 23 THR H 24 0
SHEET 2 M 3 PRO H 57 TYR H 62 -1 O VAL H 61 N THR H 24
SHEET 3 M 3 GLY H 47 ASP H 52 -1 N GLY H 47 O TYR H 62
SHEET 1 N 2 HIS H 82 ARG H 85 0
SHEET 2 N 2 CYS H 135 TRP H 138 -1 O TRP H 138 N HIS H 82
SHEET 1 O 4 TYR H 94 VAL H 95 0
SHEET 2 O 4 GLY H 131 GLU H 132 -1 O GLY H 131 N VAL H 95
SHEET 3 O 4 LEU H 112 THR H 114 -1 N SER H 113 O GLU H 132
SHEET 4 O 4 GLY H 117 LEU H 119 -1 O LEU H 119 N LEU H 112
SHEET 1 P 4 TYR I 4 GLY I 8 0
SHEET 2 P 4 VAL I 14 PRO I 21 -1 O ALA I 15 N GLY I 8
SHEET 3 P 4 PHE I 59 ARG I 66 -1 O ASP I 60 N ARG I 20
SHEET 4 P 4 THR I 27 VAL I 28 1 N THR I 27 O ALA I 61
SHEET 1 Q 4 VAL J 34 PRO J 39 0
SHEET 2 Q 4 ARG J 70 ILE J 74 -1 O LEU J 71 N ILE J 38
SHEET 3 Q 4 ILE J 4 LEU J 8 -1 N ILE J 6 O VAL J 72
SHEET 4 Q 4 ILE J 96 LYS J 99 -1 O GLU J 97 N LYS J 7
SHEET 1 R 3 ARG J 43 VAL J 49 0
SHEET 2 R 3 GLU J 61 THR J 67 -1 O PHE J 63 N PHE J 47
SHEET 3 R 3 VAL N 56 LYS N 58 -1 O ARG N 57 N GLU J 64
SHEET 1 S 5 PRO K 39 SER K 44 0
SHEET 2 S 5 THR K 28 THR K 33 -1 N ILE K 32 O THR K 41
SHEET 3 S 5 SER K 16 ALA K 23 -1 N HIS K 22 O ILE K 29
SHEET 4 S 5 SER K 79 ARG K 85 1 O ILE K 83 N ALA K 19
SHEET 5 S 5 ILE K 108 ASP K 110 1 O VAL K 109 N VAL K 84
SHEET 1 T 4 VAL L 65 TYR L 68 0
SHEET 2 T 4 ARG L 52 LEU L 59 -1 N VAL L 57 O VAL L 65
SHEET 3 T 4 GLY L 34 VAL L 42 -1 N VAL L 42 O ARG L 52
SHEET 4 T 4 VAL L 81 VAL L 82 -1 O VAL L 82 N GLY L 34
SHEET 1 U 3 VAL P 2 LEU P 6 0
SHEET 2 U 3 ILE P 19 ASP P 23 -1 O VAL P 20 N ARG P 5
SHEET 3 U 3 GLU P 34 LYS P 35 -1 O GLU P 34 N VAL P 21
SHEET 1 V 2 GLY P 37 TYR P 39 0
SHEET 2 V 2 LEU P 49 VAL P 51 -1 O LYS P 50 N TYR P 38
SHEET 1 W 6 VAL Q 5 MET Q 15 0
SHEET 2 W 6 THR Q 18 PRO Q 28 -1 O LEU Q 22 N VAL Q 9
SHEET 3 W 6 VAL Q 35 HIS Q 45 -1 O ALA Q 44 N VAL Q 19
SHEET 4 W 6 LYS Q 69 GLU Q 78 1 O PHE Q 71 N HIS Q 45
SHEET 5 W 6 VAL Q 56 SER Q 66 -1 N VAL Q 56 O VAL Q 77
SHEET 6 W 6 VAL Q 5 MET Q 15 -1 N GLY Q 8 O VAL Q 57
SHEET 1 X 3 LEU S 30 THR S 33 0
SHEET 2 X 3 THR S 48 VAL S 51 1 O ALA S 50 N ILE S 31
SHEET 3 X 3 VAL S 58 VAL S 60 -1 O VAL S 58 N VAL S 51
SHEET 1 Y 6 VAL V 144 PRO V 149 0
SHEET 2 Y 6 PHE V 155 PHE V 160 -1 O SER V 156 N HIS V 148
SHEET 3 Y 6 ALA V 107 ALA V 113 -1 N ILE V 111 O VAL V 158
SHEET 4 Y 6 HIS V 193 PRO V 203 -1 O THR V 198 N ARG V 112
SHEET 5 Y 6 VAL V 177 ARG V 182 -1 N ARG V 182 O HIS V 193
SHEET 6 Y 6 THR V 304 ASN V 306 1 O TYR V 305 N ARG V 179
SHEET 1 Z 3 ILE V 217 ARG V 223 0
SHEET 2 Z 3 SER V 237 HIS V 243 -1 O ARG V 240 N ASP V 220
SHEET 3 Z 3 MET V 249 CYS V 252 -1 O VAL V 250 N VAL V 241
LINK SG CYS D 26 ZN ZN D 210 1555 1555 2.49
LINK SG CYS D 31 ZN ZN D 210 1555 1555 2.54
LINK SG CYS N 24 ZN ZN N 1 1555 1555 2.54
SITE 1 AC1 5 CYS N 24 CYS N 27 GLY N 28 ARG N 29
SITE 2 AC1 5 CYS N 40
SITE 1 AC2 6 CYS D 9 CYS D 12 LEU D 19 LEU D 21
SITE 2 AC2 6 CYS D 26 CYS D 31
CRYST1 210.380 452.700 617.090 90.00 90.00 90.00 P 21 21 21 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 0.004753 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002209 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001621 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
