HEADER RIBOSOME 18-MAR-01 1I96
TITLE CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS
TITLE 2 THERMOPHILUS IN COMPLEX WITH THE TRANSLATION INITIATION FACTOR IF3
TITLE 3 (C-TERMINAL DOMAIN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 16S RRNA;
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: TRANSLATION INITIATION FACTOR IF3;
COMPND 66 CHAIN: V;
COMPND 67 FRAGMENT: C-TERMINAL DOMAIN
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 6 ORGANISM_TAXID: 274;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 9 ORGANISM_TAXID: 274;
SOURCE 10 MOL_ID: 4;
SOURCE 11 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 12 ORGANISM_TAXID: 274;
SOURCE 13 MOL_ID: 5;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 15 ORGANISM_TAXID: 274;
SOURCE 16 MOL_ID: 6;
SOURCE 17 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 18 ORGANISM_TAXID: 274;
SOURCE 19 MOL_ID: 7;
SOURCE 20 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 21 ORGANISM_TAXID: 274;
SOURCE 22 MOL_ID: 8;
SOURCE 23 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 24 ORGANISM_TAXID: 274;
SOURCE 25 MOL_ID: 9;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 27 ORGANISM_TAXID: 274;
SOURCE 28 MOL_ID: 10;
SOURCE 29 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 30 ORGANISM_TAXID: 274;
SOURCE 31 MOL_ID: 11;
SOURCE 32 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 33 ORGANISM_TAXID: 274;
SOURCE 34 MOL_ID: 12;
SOURCE 35 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 36 ORGANISM_TAXID: 274;
SOURCE 37 MOL_ID: 13;
SOURCE 38 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 39 ORGANISM_TAXID: 274;
SOURCE 40 MOL_ID: 14;
SOURCE 41 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 42 ORGANISM_TAXID: 274;
SOURCE 43 MOL_ID: 15;
SOURCE 44 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 45 ORGANISM_TAXID: 274;
SOURCE 46 MOL_ID: 16;
SOURCE 47 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 48 ORGANISM_TAXID: 274;
SOURCE 49 MOL_ID: 17;
SOURCE 50 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 51 ORGANISM_TAXID: 274;
SOURCE 52 MOL_ID: 18;
SOURCE 53 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 54 ORGANISM_TAXID: 274;
SOURCE 55 MOL_ID: 19;
SOURCE 56 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 57 ORGANISM_TAXID: 274;
SOURCE 58 MOL_ID: 20;
SOURCE 59 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 60 ORGANISM_TAXID: 274;
SOURCE 61 MOL_ID: 21;
SOURCE 62 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 63 ORGANISM_TAXID: 274;
SOURCE 64 MOL_ID: 22;
SOURCE 65 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 66 ORGANISM_TAXID: 274
KEYWDS 30S RIBOSOME, TRANSLATION INITIATION FACTOR, IF3, RIBOSOME
EXPDTA X-RAY DIFFRACTION
MDLTYP CA ATOMS ONLY, CHAIN B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q,
MDLTYP 2R, S, T, U, V
AUTHOR M.PIOLETTI,F.SCHLUENZEN,J.HARMS,R.ZARIVACH,M.GLUEHMANN,H.AVILA,
AUTHOR 2 H.BARTELS,C.JACOBI,T.HARTSCH,A.YONATH,F.FRANCESCHI
REVDAT 4 07-FEB-24 1I96 1 REMARK
REVDAT 3 24-FEB-09 1I96 1 VERSN
REVDAT 2 01-APR-03 1I96 1 JRNL
REVDAT 1 12-APR-01 1I96 0
JRNL AUTH M.PIOLETTI,F.SCHLUNZEN,J.HARMS,R.ZARIVACH,M.GLUHMANN,
JRNL AUTH 2 H.AVILA,A.BASHAN,H.BARTELS,T.AUERBACH,C.JACOBI,T.HARTSCH,
JRNL AUTH 3 A.YONATH,F.FRANCESCHI
JRNL TITL CRYSTAL STRUCTURES OF COMPLEXES OF THE SMALL RIBOSOMAL
JRNL TITL 2 SUBUNIT WITH TETRACYCLINE, EDEINE AND IF3.
JRNL REF EMBO J. V. 20 1829 2001
JRNL REFN ISSN 0261-4189
JRNL PMID 11296217
JRNL DOI 10.1093/EMBOJ/20.8.1829
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH F.SCHLUENZEN,A.TOCILJ,R.ZARIVACH,J.HARMS,M.GLUEHMANN,
REMARK 1 AUTH 2 D.JANELL,A.BASHAN,H.BARTELS,I.AGMON,F.FRANCESCHI,A.YONATH
REMARK 1 TITL STRUCTURE OF FUNCTIONALLY ACTIVATED SMALL RIBOSOMAL SUBUNIT
REMARK 1 TITL 2 AT 3.3 A RESOLUTION
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 102 615 2000
REMARK 1 REFN ISSN 0092-8674
REMARK 1 DOI 10.1016/S0092-8674(00)00084-2
REMARK 2
REMARK 2 RESOLUTION. 4.20 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : NONE
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 83090
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 8300
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2496
REMARK 3 NUCLEIC ACID ATOMS : 32534
REMARK 3 HETEROGEN ATOMS : 1061
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I96 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013061.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-DEC-00; 01-JUL-00
REMARK 200 TEMPERATURE (KELVIN) : 85; 85
REMARK 200 PH : 7.8
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : APS; MPG/DESY, HAMBURG
REMARK 200 BEAMLINE : 19-ID; BW6
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033; 1.045
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL MONOCHROMATOR,
REMARK 200 SI(111) DOUBLE CRYSTAL
REMARK 200 MONOCHROMATOR, SI(222); DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR, SI(111)
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : SBC; MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83090
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.200
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 81.5
REMARK 200 DATA REDUNDANCY : 5.000
REMARK 200 R MERGE (I) : 0.09900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 69.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.35700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, MAGNESIUM CHLORIDE, SPERMIDINE,
REMARK 280 PH 7.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291.K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 87.40000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 203.75000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 203.75000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 43.70000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 203.75000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 203.75000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 131.10000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 203.75000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 203.75000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 43.70000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 203.75000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 203.75000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 131.10000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 87.40000
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: 22-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, U, V
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 GLU B 251
REMARK 465 SER B 252
REMARK 465 GLU B 253
REMARK 465 VAL B 254
REMARK 465 GLU B 255
REMARK 465 ALA B 256
REMARK 465 ILE C 208
REMARK 465 GLY C 209
REMARK 465 GLY C 210
REMARK 465 GLN C 211
REMARK 465 LYS C 212
REMARK 465 PRO C 213
REMARK 465 LYS C 214
REMARK 465 ALA C 215
REMARK 465 ARG C 216
REMARK 465 PRO C 217
REMARK 465 GLU C 218
REMARK 465 LEU C 219
REMARK 465 PRO C 220
REMARK 465 LYS C 221
REMARK 465 ALA C 222
REMARK 465 GLU C 223
REMARK 465 GLU C 224
REMARK 465 ARG C 225
REMARK 465 PRO C 226
REMARK 465 ARG C 227
REMARK 465 ARG C 228
REMARK 465 ARG C 229
REMARK 465 ARG C 230
REMARK 465 PRO C 231
REMARK 465 ALA C 232
REMARK 465 VAL C 233
REMARK 465 ARG C 234
REMARK 465 VAL C 235
REMARK 465 LYS C 236
REMARK 465 LYS C 237
REMARK 465 GLU C 238
REMARK 465 GLU C 239
REMARK 465 ALA E 158
REMARK 465 GLN E 159
REMARK 465 ALA E 160
REMARK 465 GLN E 161
REMARK 465 GLY E 162
REMARK 465 MET I 1
REMARK 465 PRO J 2
REMARK 465 VAL J 101
REMARK 465 GLY J 102
REMARK 465 GLY J 103
REMARK 465 GLY J 104
REMARK 465 ARG J 105
REMARK 465 ALA K 2
REMARK 465 LYS K 3
REMARK 465 LYS K 4
REMARK 465 PRO K 5
REMARK 465 SER K 6
REMARK 465 GLY M 95
REMARK 465 LEU M 96
REMARK 465 PRO M 97
REMARK 465 VAL M 98
REMARK 465 ARG M 99
REMARK 465 GLY M 100
REMARK 465 GLN M 101
REMARK 465 ARG M 102
REMARK 465 THR M 103
REMARK 465 ARG M 104
REMARK 465 THR M 105
REMARK 465 ASN M 106
REMARK 465 ALA M 107
REMARK 465 ARG M 108
REMARK 465 THR M 109
REMARK 465 ARG M 110
REMARK 465 LYS M 111
REMARK 465 GLY M 112
REMARK 465 PRO M 113
REMARK 465 ARG M 114
REMARK 465 LYS M 115
REMARK 465 THR M 116
REMARK 465 VAL M 117
REMARK 465 ALA M 118
REMARK 465 GLY M 119
REMARK 465 LYS M 120
REMARK 465 LYS M 121
REMARK 465 LYS M 122
REMARK 465 ALA M 123
REMARK 465 PRO M 124
REMARK 465 ARG M 125
REMARK 465 LYS M 126
REMARK 465 SER R 2
REMARK 465 THR R 3
REMARK 465 LYS R 4
REMARK 465 ASN R 5
REMARK 465 ALA R 6
REMARK 465 GLY S 82
REMARK 465 HIS S 83
REMARK 465 GLY S 84
REMARK 465 LYS S 85
REMARK 465 GLU S 86
REMARK 465 ALA S 87
REMARK 465 LYS S 88
REMARK 465 ALA S 89
REMARK 465 THR S 90
REMARK 465 LYS S 91
REMARK 465 LYS S 92
REMARK 465 LYS S 93
REMARK 465 ALA T 2
REMARK 465 GLN T 3
REMARK 465 LYS T 4
REMARK 465 LYS T 5
REMARK 465 PRO T 6
REMARK 465 LYS T 7
REMARK 465 LYS U 26
REMARK 465 LYS U 27
REMARK 465 VAL V 169
REMARK 465 SER V 170
REMARK 465 ALA V 171
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 504 O2' C A 519 2.18
REMARK 500 N2 G A 1205 O2 C A 1344 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 N4 C A 823 N4 C A 823 7556 1.09
REMARK 500 CA GLU T 50 O25 WO2 K 1014 3555 1.89
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 U A 4 O3' U A 5 P -0.124
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 G A 7 N9 - C1' - C2' ANGL. DEV. = 8.1 DEGREES
REMARK 500 G A 31 N9 - C1' - C2' ANGL. DEV. = 8.0 DEGREES
REMARK 500 A A 241 N9 - C1' - C2' ANGL. DEV. = 9.3 DEGREES
REMARK 500 G A 261 C2' - C3' - O3' ANGL. DEV. = 13.8 DEGREES
REMARK 500 C A 323 N1 - C1' - C2' ANGL. DEV. = 10.3 DEGREES
REMARK 500 C A 367 N1 - C1' - C2' ANGL. DEV. = 7.9 DEGREES
REMARK 500 G A 558 N9 - C1' - C2' ANGL. DEV. = 9.4 DEGREES
REMARK 500 U A 635 N1 - C1' - C2' ANGL. DEV. = 8.2 DEGREES
REMARK 500 A A 636 N9 - C1' - C2' ANGL. DEV. = 8.2 DEGREES
REMARK 500 C A 700 C2' - C3' - O3' ANGL. DEV. = 10.6 DEGREES
REMARK 500 C A 700 N1 - C1' - C2' ANGL. DEV. = 8.8 DEGREES
REMARK 500 A A 849 N9 - C1' - C2' ANGL. DEV. = 8.2 DEGREES
REMARK 500 U A 937 N1 - C1' - C2' ANGL. DEV. = 7.8 DEGREES
REMARK 500 G A1162 N9 - C1' - C2' ANGL. DEV. = 8.4 DEGREES
REMARK 500 A A1261 N9 - C1' - C2' ANGL. DEV. = 8.3 DEGREES
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 U A 13 0.07 SIDE CHAIN
REMARK 500 G A 31 0.06 SIDE CHAIN
REMARK 500 C A 47 0.06 SIDE CHAIN
REMARK 500 A A 203 0.07 SIDE CHAIN
REMARK 500 U A 239 0.08 SIDE CHAIN
REMARK 500 A A 241 0.06 SIDE CHAIN
REMARK 500 G A 346 0.06 SIDE CHAIN
REMARK 500 A A 516 0.06 SIDE CHAIN
REMARK 500 G A 558 0.06 SIDE CHAIN
REMARK 500 U A 635 0.08 SIDE CHAIN
REMARK 500 U A 669 0.08 SIDE CHAIN
REMARK 500 U A 706 0.10 SIDE CHAIN
REMARK 500 U A 968 0.08 SIDE CHAIN
REMARK 500 G A1121 0.05 SIDE CHAIN
REMARK 500 A A1261 0.06 SIDE CHAIN
REMARK 500 A A1479 0.06 SIDE CHAIN
REMARK 500 G A1481 0.06 SIDE CHAIN
REMARK 500 C A1513 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1527 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 67 O4'
REMARK 620 2 A A 166 O4' 133.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1524 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 78 O3'
REMARK 620 2 G A 78 O2' 76.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1529 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 190 O5'
REMARK 620 2 G A 190 O4' 85.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1576 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A1477 OP2
REMARK 620 2 G A1482 OP1 108.8
REMARK 620 3 G A1482 OP2 118.2 72.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1517
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1519
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1520
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1522
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1523
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1524
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1525
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1527
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1528
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1529
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 107
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1531
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG P 89
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 108
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 109
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1533
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1535
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1537
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 211
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG L 136
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1540
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1541
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1542
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1543
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1544
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1545
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1546
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1547
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1548
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG K 130
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1550
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1551
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1552
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1555
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1557
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1558
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1559
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1560
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1562
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1563
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1564
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1565
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1566
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1567
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1569
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1570
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1571
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1572
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1573
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1574
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG J 106
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1576
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN N 76
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 B 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 B 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 A 1578
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 B 1004
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 E 1005
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 J 1009
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 H 1010
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 A 1580
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 E 1012
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 T 1013
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WO2 K 1014
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1FKA RELATED DB: PDB
REMARK 900 STRUCTURE OF FUNCTIONALLY ACTIVATED SMALL RIBOSOMAL SUBUNIT AT 3.3
REMARK 900 A RESOLUTION
REMARK 900 RELATED ID: 1TIG RELATED DB: PDB
REMARK 900 TRANSLATION INITIATION FACTOR 3 C-TERMINAL DOMAIN
REMARK 900 RELATED ID: 1I94 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE SMALL RIBOSOMAL SUBUNIT
REMARK 900 RELATED ID: 1I95 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS
REMARK 900 THERMOPHILUS IN COMPLEX WITH EDEINE
REMARK 900 RELATED ID: 1I97 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS
REMARK 900 THERMOPHILUS IN COMPLEX WITH TETRACYCLINE
DBREF 1I96 A 2 1515 GB 155076 M26923 648 2161
DBREF 1I96 B 2 255 GB 13446664 CAC35061 2 256
DBREF 1I96 C 2 239 GB 13446666 CAC35062 2 239
DBREF 1I96 D 2 209 UNP P80373 RS4_THETH 1 208
DBREF 1I96 E 2 162 UNP P27152 RS5_THETH 1 161
DBREF 1I96 F 1 101 UNP P23370 RS6_THETH 1 101
DBREF 1I96 G 2 156 UNP P17291 P17291 1 155
DBREF 1I96 H 1 138 UNP P24319 RS8_THETH 1 138
DBREF 1I96 I 1 128 GB 13446668 CAC35063 1 128
DBREF 1I96 J 2 105 UNP P80375 RS10_THETH 1 104
DBREF 1I96 K 2 129 GB 4519421 BAA75547 2 129
DBREF 1I96 L 5 135 UNP P17293 RS12_THETH 5 135
DBREF 1I96 M 2 126 GB 4519420 BAA75546 2 126
DBREF 1I96 N 2 61 UNP P24320 RS14_THETH 1 60
DBREF 1I96 O 2 89 UNP P80378 RS15_THETH 1 88
DBREF 1I96 P 1 88 GB 12056104 CAC21226 1 88
DBREF 1I96 Q 2 105 UNP P24321 RS17_THETH 1 104
DBREF 1I96 R 2 88 GB 6739549 AAF27297 2 88
DBREF 1I96 S 2 93 UNP P80381 RS19_THETH 1 92
DBREF 1I96 T 2 106 GB 11125386 CAC15067 2 106
DBREF 1I96 U 2 27 GB 11125387 CAC15068 2 27
DBREF 1I96 V 83 171 GB 13508846 CAC35168 83 171
SEQRES 1 A 1514 U G U U G G A G A G U U U
SEQRES 2 A 1514 G A U C C U G G C U C A G
SEQRES 3 A 1514 G G U G A A C G C U G G C
SEQRES 4 A 1514 G G C G U G C C U A A G A
SEQRES 5 A 1514 C A U G C A A G U C G U G
SEQRES 6 A 1514 C G G G C C G C G G G G U
SEQRES 7 A 1514 U U U A C U C C G U G G U
SEQRES 8 A 1514 C A G C G G C G G A C G G
SEQRES 9 A 1514 G U G A G U A A C G C G U
SEQRES 10 A 1514 G G G U G A C C U A C C C
SEQRES 11 A 1514 G G A A G A G G G G G A C
SEQRES 12 A 1514 A A C C C G G G G A A A C
SEQRES 13 A 1514 U C G G G C U A A U C C C
SEQRES 14 A 1514 C C A U G U G G A C C C G
SEQRES 15 A 1514 C C C C U U G G G G U G U
SEQRES 16 A 1514 G U C C A A A G G G C U U
SEQRES 17 A 1514 U G C C C G C U U C C G G
SEQRES 18 A 1514 A U G G G C C C G C G U C
SEQRES 19 A 1514 C C A U C A G C U A G U U
SEQRES 20 A 1514 G G U G G G G U A A U G G
SEQRES 21 A 1514 C C C A C C A A G G C G A
SEQRES 22 A 1514 C G A C G G G U A G C C G
SEQRES 23 A 1514 G U C U G A G A G G A U G
SEQRES 24 A 1514 G C C G G C C A C A G G G
SEQRES 25 A 1514 G C A C U G A G A C A C G
SEQRES 26 A 1514 G G C C C C A C U C C U A
SEQRES 27 A 1514 C G G G A G G C A G C A G
SEQRES 28 A 1514 U U A G G A A U C U U C C
SEQRES 29 A 1514 G C A A U G G G C G C A A
SEQRES 30 A 1514 G C C U G A C G G A G C G
SEQRES 31 A 1514 A C G C C G C U U G G A G
SEQRES 32 A 1514 G A A G A A G C C C U U C
SEQRES 33 A 1514 G G G G U G U A A A C U C
SEQRES 34 A 1514 C U G A A C C C G G G A C
SEQRES 35 A 1514 G A A A C C C C C G A C G
SEQRES 36 A 1514 A G G G G A C U G A C G G
SEQRES 37 A 1514 U A C C G G G G U A A U A
SEQRES 38 A 1514 G C G C C G G C C A A C U
SEQRES 39 A 1514 C C G U G C C A G C A G C
SEQRES 40 A 1514 C G C G G U A A U A C G G
SEQRES 41 A 1514 A G G G C G C G A G C G U
SEQRES 42 A 1514 U A C C C G G A U U C A C
SEQRES 43 A 1514 U G G G C G U A A A G G G
SEQRES 44 A 1514 C G U G U A G G C G G C C
SEQRES 45 A 1514 U G G G G C G U C C C A U
SEQRES 46 A 1514 G U G A A A G A C C A C G
SEQRES 47 A 1514 G C U C A A C C G U G G G
SEQRES 48 A 1514 G G A G C G U G G G A U A
SEQRES 49 A 1514 C G C U C A G G C U A G A
SEQRES 50 A 1514 C G G U G G G A G A G G G
SEQRES 51 A 1514 U G G U G G A A U U C C C
SEQRES 52 A 1514 G G A G U A G C G G U G A
SEQRES 53 A 1514 A A U G C G C A G A U A C
SEQRES 54 A 1514 C G G G A G G A A C G C C
SEQRES 55 A 1514 G A U G G C G A A G G C A
SEQRES 56 A 1514 G C C A C C U G G U C C A
SEQRES 57 A 1514 C C C G U G A C G C U G A
SEQRES 58 A 1514 G G C G C G A A A G C G U
SEQRES 59 A 1514 G G G G A G C A A A C C G
SEQRES 60 A 1514 G A U U A G A U A C C C G
SEQRES 61 A 1514 G G U A G U C C A C G C C
SEQRES 62 A 1514 C U A A A C G A U G C G C
SEQRES 63 A 1514 G C U A G G U C U C U G G
SEQRES 64 A 1514 G U C U C C U G G G G G C
SEQRES 65 A 1514 C G A A G C U A A C G C G
SEQRES 66 A 1514 U U A A G C G C G C C G C
SEQRES 67 A 1514 C U G G G G A G U A C G G
SEQRES 68 A 1514 C C G C A A G G C U G A A
SEQRES 69 A 1514 A C U C A A A G G A A U U
SEQRES 70 A 1514 G A C G G G G G C C C G C
SEQRES 71 A 1514 A C A A G C G G U G G A G
SEQRES 72 A 1514 C A U G U G G U U U A A U
SEQRES 73 A 1514 U C G A A G C A A C G C G
SEQRES 74 A 1514 A A G A A C C U U A C C A
SEQRES 75 A 1514 G G C C U U G A C A U G C
SEQRES 76 A 1514 U A G G G A A C C C G G G
SEQRES 77 A 1514 U G A A A G C C U G G G G
SEQRES 78 A 1514 U G C C C C G C G A G G G
SEQRES 79 A 1514 G A G C C C U A G C A C A
SEQRES 80 A 1514 G G U G C U G C A U G G C
SEQRES 81 A 1514 C G U C G U C A G C U C G
SEQRES 82 A 1514 U G C C G U G A G G U G U
SEQRES 83 A 1514 U G G G U U A A G U C C C
SEQRES 84 A 1514 G C A A C G A G C G C A A
SEQRES 85 A 1514 C C C C C G C C G U U A G
SEQRES 86 A 1514 U U G C C A G C G G U U C
SEQRES 87 A 1514 G G C C G G G C A C U C U
SEQRES 88 A 1514 A A C G G G A C U G C C C
SEQRES 89 A 1514 G C G A A A G C G G G A G
SEQRES 90 A 1514 G A A G G A G G G G A C G
SEQRES 91 A 1514 A C G U C U G G U C A G C
SEQRES 92 A 1514 A U G G C C C U U A C G G
SEQRES 93 A 1514 C C U G G G C G A C A C A
SEQRES 94 A 1514 C G U G C U A C A A U G C
SEQRES 95 A 1514 C C A C U A C A A A G C G
SEQRES 96 A 1514 A U G C C A C C C G G C A
SEQRES 97 A 1514 A C G G G G A G C U A A U
SEQRES 98 A 1514 C G C A A A A A G G U G G
SEQRES 99 A 1514 G C C C A G U U C G G A U
SEQRES 100 A 1514 U G G G G U C U G C A A C
SEQRES 101 A 1514 C C G A C C C C A U G A A
SEQRES 102 A 1514 G C C G G A A U C G C U A
SEQRES 103 A 1514 G U A A U C G C G G A U C
SEQRES 104 A 1514 A G C C A U G C C G C G G
SEQRES 105 A 1514 U G A A U A C G U U C C C
SEQRES 106 A 1514 G G G C C U U G U A C A C
SEQRES 107 A 1514 A C C G C C C G U C A C G
SEQRES 108 A 1514 C C A U G G G A G C G G G
SEQRES 109 A 1514 C U C U A C C C G A A G U
SEQRES 110 A 1514 C G C C G G G A G C C U A
SEQRES 111 A 1514 C G G G C A G G C G C C G
SEQRES 112 A 1514 A G G G U A G G G C C C G
SEQRES 113 A 1514 U G A C U G G G G C G A A
SEQRES 114 A 1514 G U C G U A A C A A G G U
SEQRES 115 A 1514 A G C U G U A C C G G A A
SEQRES 116 A 1514 G G U G C G G C U G G A U
SEQRES 117 A 1514 C A C C U C
SEQRES 1 B 255 PRO VAL GLU ILE THR VAL LYS GLU LEU LEU GLU ALA GLY
SEQRES 2 B 255 VAL HIS PHE GLY HIS GLU ARG LYS ARG TRP ASN PRO LYS
SEQRES 3 B 255 PHE ALA ARG TYR ILE TYR ALA GLU ARG ASN GLY ILE HIS
SEQRES 4 B 255 ILE ILE ASP LEU GLN LYS THR MET GLU GLU LEU GLU ARG
SEQRES 5 B 255 THR PHE ARG PHE ILE GLU ASP LEU ALA MET ARG GLY GLY
SEQRES 6 B 255 THR ILE LEU PHE VAL GLY THR LYS LYS GLN ALA GLN ASP
SEQRES 7 B 255 ILE VAL ARG MET GLU ALA GLU ARG ALA GLY MET PRO TYR
SEQRES 8 B 255 VAL ASN GLN ARG TRP LEU GLY GLY MET LEU THR ASN PHE
SEQRES 9 B 255 LYS THR ILE SER GLN ARG VAL HIS ARG LEU GLU GLU LEU
SEQRES 10 B 255 GLU ALA LEU PHE ALA SER PRO GLU ILE GLU GLU ARG PRO
SEQRES 11 B 255 LYS LYS GLU GLN VAL ARG LEU LYS HIS GLU LEU GLU ARG
SEQRES 12 B 255 LEU GLN LYS TYR LEU SER GLY PHE ARG LEU LEU LYS ARG
SEQRES 13 B 255 LEU PRO ASP ALA ILE PHE VAL VAL ASP PRO THR LYS GLU
SEQRES 14 B 255 ALA ILE ALA VAL ARG GLU ALA ARG LYS LEU PHE ILE PRO
SEQRES 15 B 255 VAL ILE ALA LEU ALA ASP THR ASP SER ASP PRO ASP LEU
SEQRES 16 B 255 VAL ASP TYR ILE ILE PRO GLY ASN ASP ASP ALA ILE ARG
SEQRES 17 B 255 SER ILE GLN LEU ILE LEU SER ARG ALA VAL ASP LEU ILE
SEQRES 18 B 255 ILE GLN ALA ARG GLY GLY VAL VAL GLU PRO SER PRO SER
SEQRES 19 B 255 TYR ALA LEU VAL GLN GLU ALA GLU ALA THR GLU THR PRO
SEQRES 20 B 255 GLU GLY GLU SER GLU VAL GLU ALA
SEQRES 1 C 238 GLY ASN LYS ILE HIS PRO ILE GLY PHE ARG LEU GLY ILE
SEQRES 2 C 238 THR ARG ASP TRP GLU SER ARG TRP TYR ALA GLY LYS LYS
SEQRES 3 C 238 GLN TYR ARG HIS LEU LEU LEU GLU ASP GLN ARG ILE ARG
SEQRES 4 C 238 GLY LEU LEU GLU LYS GLU LEU TYR SER ALA GLY LEU ALA
SEQRES 5 C 238 ARG VAL ASP ILE GLU ARG ALA ALA ASP ASN VAL ALA VAL
SEQRES 6 C 238 THR VAL HIS VAL ALA LYS PRO GLY VAL VAL ILE GLY ARG
SEQRES 7 C 238 GLY GLY GLU ARG ILE ARG VAL LEU ARG GLU GLU LEU ALA
SEQRES 8 C 238 LYS LEU THR GLY LYS ASN VAL ALA LEU ASN VAL GLN GLU
SEQRES 9 C 238 VAL GLN ASN PRO ASN LEU SER ALA PRO LEU VAL ALA GLN
SEQRES 10 C 238 ARG VAL ALA GLU GLN ILE GLU ARG ARG PHE ALA VAL ARG
SEQRES 11 C 238 ARG ALA ILE LYS GLN ALA VAL GLN ARG VAL MET GLU SER
SEQRES 12 C 238 GLY ALA LYS GLY ALA LYS VAL ILE VAL SER GLY ARG ILE
SEQRES 13 C 238 GLY GLY ALA GLU GLN ALA ARG THR GLU TRP ALA ALA GLN
SEQRES 14 C 238 GLY ARG VAL PRO LEU HIS THR LEU ARG ALA ASN ILE ASP
SEQRES 15 C 238 TYR GLY PHE ALA LEU ALA ARG THR THR TYR GLY VAL LEU
SEQRES 16 C 238 GLY VAL LYS ALA TYR ILE PHE LEU GLY GLU VAL ILE GLY
SEQRES 17 C 238 GLY GLN LYS PRO LYS ALA ARG PRO GLU LEU PRO LYS ALA
SEQRES 18 C 238 GLU GLU ARG PRO ARG ARG ARG ARG PRO ALA VAL ARG VAL
SEQRES 19 C 238 LYS LYS GLU GLU
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 161 PRO GLU THR ASP PHE GLU GLU LYS MET ILE LEU ILE ARG
SEQRES 2 E 161 ARG THR ALA ARG MET GLN ALA GLY GLY ARG ARG PHE ARG
SEQRES 3 E 161 PHE GLY ALA LEU VAL VAL VAL GLY ASP ARG GLN GLY ARG
SEQRES 4 E 161 VAL GLY LEU GLY PHE GLY LYS ALA PRO GLU VAL PRO LEU
SEQRES 5 E 161 ALA VAL GLN LYS ALA GLY TYR TYR ALA ARG ARG ASN MET
SEQRES 6 E 161 VAL GLU VAL PRO LEU GLN ASN GLY THR ILE PRO HIS GLU
SEQRES 7 E 161 ILE GLU VAL GLU PHE GLY ALA SER LYS ILE VAL LEU LYS
SEQRES 8 E 161 PRO ALA ALA PRO GLY THR GLY VAL ILE ALA GLY ALA VAL
SEQRES 9 E 161 PRO ARG ALA ILE LEU GLU LEU ALA GLY VAL THR ASP ILE
SEQRES 10 E 161 LEU THR LYS GLU LEU GLY SER ARG ASN PRO ILE ASN ILE
SEQRES 11 E 161 ALA TYR ALA THR MET GLU ALA LEU ARG GLN LEU ARG THR
SEQRES 12 E 161 LYS ALA ASP VAL GLU ARG LEU ARG LYS GLY GLU ALA HIS
SEQRES 13 E 161 ALA GLN ALA GLN GLY
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 GLU VAL
SEQRES 3 H 138 PRO ALA SER ARG PHE LYS GLU GLU ILE LEU LYS ILE LEU
SEQRES 4 H 138 ALA ARG GLU GLY PHE ILE LYS GLY TYR GLU ARG VAL GLU
SEQRES 5 H 138 VAL ASP GLY LYS PRO TYR LEU ARG ILE HIS 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 LYS HIS ILE ARG ARG ILE SER ARG 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 PRO 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 128 MET GLU GLN TYR TYR GLY THR GLY ARG ARG LYS GLU ALA
SEQRES 2 I 128 VAL ALA ARG VAL PHE LEU ARG PRO GLY ASN GLY LYS VAL
SEQRES 3 I 128 THR VAL ASN GLY GLN ASP PHE ASN GLU TYR PHE GLN GLY
SEQRES 4 I 128 LEU VAL ARG ALA VAL ALA ALA LEU GLU PRO LEU ARG ALA
SEQRES 5 I 128 VAL ASP ALA LEU GLY ARG PHE ASP ALA TYR ILE THR VAL
SEQRES 6 I 128 ARG GLY GLY GLY LYS SER GLY GLN ILE ASP ALA ILE LYS
SEQRES 7 I 128 LEU GLY ILE ALA ARG ALA LEU VAL GLN TYR ASN PRO ASP
SEQRES 8 I 128 TYR ARG ALA LYS LEU LYS PRO LEU GLY PHE LEU THR ARG
SEQRES 9 I 128 ASP ALA ARG VAL VAL GLU ARG LYS LYS TYR GLY LYS HIS
SEQRES 10 I 128 LYS ALA ARG ARG ALA PRO GLN TYR SER LYS ARG
SEQRES 1 J 104 PRO LYS ILE ARG ILE LYS LEU ARG GLY PHE ASP HIS LYS
SEQRES 2 J 104 THR LEU ASP ALA SER ALA GLN LYS ILE VAL GLU ALA ALA
SEQRES 3 J 104 ARG ARG SER GLY ALA GLN VAL SER GLY PRO ILE PRO LEU
SEQRES 4 J 104 PRO THR ARG VAL ARG ARG PHE THR VAL ILE ARG GLY PRO
SEQRES 5 J 104 PHE LYS HIS LYS ASP SER ARG GLU HIS PHE GLU LEU ARG
SEQRES 6 J 104 THR HIS ASN ARG LEU VAL ASP ILE ILE ASN PRO ASN ARG
SEQRES 7 J 104 LYS THR ILE GLU GLN LEU MET THR LEU ASP LEU PRO THR
SEQRES 8 J 104 GLY VAL GLU ILE GLU ILE LYS THR VAL GLY GLY GLY ARG
SEQRES 1 K 128 ALA LYS LYS PRO SER LYS LYS LYS VAL LYS ARG GLN VAL
SEQRES 2 K 128 ALA SER GLY ARG ALA TYR ILE HIS ALA SER TYR ASN ASN
SEQRES 3 K 128 THR ILE VAL THR ILE THR ASP PRO ASP GLY ASN PRO ILE
SEQRES 4 K 128 THR TRP SER SER GLY GLY VAL ILE GLY TYR LYS GLY SER
SEQRES 5 K 128 ARG LYS GLY THR PRO TYR ALA ALA GLN LEU ALA ALA LEU
SEQRES 6 K 128 ASP ALA ALA LYS LYS ALA MET ALA TYR GLY MET GLN SER
SEQRES 7 K 128 VAL ASP VAL ILE VAL ARG GLY THR GLY ALA GLY ARG GLU
SEQRES 8 K 128 GLN ALA ILE ARG ALA LEU GLN ALA SER GLY LEU GLN VAL
SEQRES 9 K 128 LYS SER ILE VAL ASP ASP THR PRO VAL PRO HIS ASN GLY
SEQRES 10 K 128 CYS ARG PRO LYS LYS LYS PHE ARG LYS ALA SER
SEQRES 1 L 131 PRO THR ILE ASN GLN LEU VAL ARG LYS GLY ARG GLU LYS
SEQRES 2 L 131 VAL ARG LYS LYS SER LYS VAL PRO ALA LEU LYS GLY ALA
SEQRES 3 L 131 PRO PHE ARG ARG GLY VAL CYS THR VAL VAL ARG THR VAL
SEQRES 4 L 131 THR PRO LYS LYS PRO ASN SER ALA LEU ARG LYS VAL ALA
SEQRES 5 L 131 LYS VAL ARG LEU THR SER GLY TYR GLU VAL THR ALA TYR
SEQRES 6 L 131 ILE PRO GLY GLU GLY HIS ASN LEU GLN GLU HIS SER VAL
SEQRES 7 L 131 VAL LEU ILE ARG GLY GLY ARG VAL LYS ASP LEU PRO GLY
SEQRES 8 L 131 VAL ARG TYR HIS ILE VAL ARG GLY VAL TYR ASP ALA ALA
SEQRES 9 L 131 GLY VAL LYS ASP ARG LYS LYS SER ARG SER LYS TYR GLY
SEQRES 10 L 131 THR LYS LYS PRO LYS GLU ALA ALA LYS THR ALA ALA LYS
SEQRES 11 L 131 LYS
SEQRES 1 M 125 ALA ARG ILE ALA GLY VAL GLU ILE PRO ARG ASN LYS ARG
SEQRES 2 M 125 VAL ASP VAL ALA LEU THR TYR ILE TYR GLY ILE GLY LYS
SEQRES 3 M 125 ALA ARG ALA LYS GLU ALA LEU GLU LYS THR GLY ILE ASN
SEQRES 4 M 125 PRO ALA THR ARG VAL LYS ASP LEU THR GLU ALA GLU VAL
SEQRES 5 M 125 VAL ARG LEU ARG GLU TYR VAL GLU ASN THR TRP LYS LEU
SEQRES 6 M 125 GLU GLY GLU LEU ARG ALA GLU VAL ALA ALA ASN ILE LYS
SEQRES 7 M 125 ARG LEU MET ASP ILE GLY CYS TYR ARG GLY LEU ARG HIS
SEQRES 8 M 125 ARG ARG GLY LEU PRO VAL ARG GLY GLN ARG THR ARG THR
SEQRES 9 M 125 ASN ALA ARG THR ARG LYS GLY PRO ARG LYS THR VAL ALA
SEQRES 10 M 125 GLY LYS LYS LYS ALA PRO ARG LYS
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 88 MET VAL LYS ILE ARG LEU ALA ARG PHE GLY SER LYS HIS
SEQRES 2 P 88 ASN PRO HIS TYR ARG ILE VAL VAL THR ASP ALA ARG ARG
SEQRES 3 P 88 LYS ARG ASP GLY LYS TYR ILE GLU LYS ILE GLY TYR TYR
SEQRES 4 P 88 ASP PRO ARG LYS THR THR PRO ASP TRP LEU LYS VAL ASP
SEQRES 5 P 88 VAL GLU ARG ALA ARG TYR TRP LEU SER VAL GLY ALA GLN
SEQRES 6 P 88 PRO THR ASP THR ALA ARG ARG LEU LEU ARG GLN ALA GLY
SEQRES 7 P 88 VAL PHE ARG GLN GLU ALA ARG GLU GLY ALA
SEQRES 1 Q 104 PRO LYS LYS VAL LEU THR GLY VAL VAL VAL SER ASP LYS
SEQRES 2 Q 104 MET GLN LYS THR VAL THR VAL LEU VAL GLU ARG GLN PHE
SEQRES 3 Q 104 PRO HIS PRO LEU TYR GLY LYS VAL ILE LYS ARG SER LYS
SEQRES 4 Q 104 LYS TYR LEU ALA HIS ASP PRO GLU GLU ARG TYR LYS VAL
SEQRES 5 Q 104 GLY ASP VAL VAL GLU ILE ILE GLU ALA ARG PRO ILE SER
SEQRES 6 Q 104 LYS ARG LYS ARG PHE ARG VAL LEU ARG LEU VAL GLU GLU
SEQRES 7 Q 104 GLY ARG LEU ASP LEU VAL GLU LYS TYR LEU VAL ARG ARG
SEQRES 8 Q 104 GLN ASN TYR ALA SER LEU SER LYS ARG GLY GLY LYS ALA
SEQRES 1 R 87 SER THR LYS ASN ALA LYS PRO LYS LYS GLU ALA GLN ARG
SEQRES 2 R 87 ARG PRO SER ARG LYS ALA LYS VAL LYS ALA THR LEU GLY
SEQRES 3 R 87 GLU PHE ASP LEU ARG ASP TYR ARG ASN VAL GLU VAL LEU
SEQRES 4 R 87 LYS ARG PHE LEU SER GLU THR GLY LYS ILE LEU PRO ARG
SEQRES 5 R 87 ARG ARG THR GLY LEU SER GLY LYS GLU GLN ARG ILE LEU
SEQRES 6 R 87 ALA LYS THR ILE LYS ARG ALA ARG ILE LEU GLY LEU LEU
SEQRES 7 R 87 PRO PHE THR GLU LYS LEU VAL ARG LYS
SEQRES 1 S 92 PRO ARG SER LEU LYS LYS GLY VAL PHE VAL ASP ASP HIS
SEQRES 2 S 92 LEU LEU GLU LYS VAL LEU GLU LEU ASN ALA LYS GLY GLU
SEQRES 3 S 92 LYS ARG LEU ILE LYS THR TRP SER ARG ARG SER THR ILE
SEQRES 4 S 92 VAL PRO GLU MET VAL GLY HIS THR ILE ALA VAL TYR ASN
SEQRES 5 S 92 GLY LYS GLN HIS VAL PRO VAL TYR ILE THR GLU ASN MET
SEQRES 6 S 92 VAL GLY HIS LYS LEU GLY GLU PHE ALA PRO THR ARG THR
SEQRES 7 S 92 TYR ARG GLY HIS GLY LYS GLU ALA LYS ALA THR LYS LYS
SEQRES 8 S 92 LYS
SEQRES 1 T 105 ALA GLN LYS LYS PRO LYS ARG ASN LEU SER ALA LEU LYS
SEQRES 2 T 105 ARG HIS ARG GLN SER LEU LYS ARG ARG LEU ARG ASN LYS
SEQRES 3 T 105 ALA LYS LYS SER ALA ILE LYS THR LEU SER LYS LYS ALA
SEQRES 4 T 105 ILE GLN LEU ALA GLN GLU GLY LYS ALA GLU GLU ALA LEU
SEQRES 5 T 105 LYS ILE MET ARG LYS ALA GLU SER LEU ILE ASP LYS ALA
SEQRES 6 T 105 ALA LYS GLY SER THR LEU HIS LYS ASN ALA ALA ALA ARG
SEQRES 7 T 105 ARG LYS SER ARG LEU MET ARG LYS VAL ARG GLN LEU LEU
SEQRES 8 T 105 GLU ALA ALA GLY ALA PRO LEU ILE GLY GLY GLY LEU SER
SEQRES 9 T 105 ALA
SEQRES 1 U 26 GLY LYS GLY ASP ARG ARG THR ARG ARG GLY LYS ILE TRP
SEQRES 2 U 26 ARG GLY THR TYR GLY LYS TYR ARG PRO ARG LYS LYS LYS
SEQRES 1 V 89 GLU VAL LYS SER ILE LYS PHE ARG VAL LYS ILE ASP GLU
SEQRES 2 V 89 HIS ASP TYR GLN THR LYS LEU GLY HIS ILE LYS ARG PHE
SEQRES 3 V 89 LEU GLN GLU GLY HIS LYS VAL LYS VAL THR ILE MET PHE
SEQRES 4 V 89 ARG GLY ARG GLU VAL ALA HIS PRO GLU LEU GLY GLU ARG
SEQRES 5 V 89 ILE LEU ASN ARG VAL THR GLU ASP LEU LYS ASP LEU ALA
SEQRES 6 V 89 VAL VAL GLU MET LYS PRO GLU MET LEU GLY ARG ASP MET
SEQRES 7 V 89 ASN MET LEU LEU ALA PRO VAL LYS VAL SER ALA
HET MG A1516 1
HET MG A1517 1
HET MG A1518 1
HET MG A1519 1
HET MG A1520 1
HET MG A1521 1
HET MG A1522 1
HET MG A1523 1
HET MG A1524 1
HET MG A1525 1
HET MG A1526 1
HET MG A1527 1
HET MG A1528 1
HET MG A1529 1
HET MG A1530 1
HET MG A1531 1
HET MG A1532 1
HET MG A1533 1
HET MG A1534 1
HET MG A1535 1
HET MG A1536 1
HET MG A1537 1
HET MG A1538 1
HET MG A1539 1
HET MG A1540 1
HET MG A1541 1
HET MG A1542 1
HET MG A1543 1
HET MG A1544 1
HET MG A1545 1
HET MG A1546 1
HET MG A1547 1
HET MG A1548 1
HET MG A1549 1
HET MG A1550 1
HET MG A1551 1
HET MG A1552 1
HET MG A1553 1
HET MG A1554 1
HET MG A1555 1
HET MG A1556 1
HET MG A1557 1
HET MG A1558 1
HET MG A1559 1
HET MG A1560 1
HET MG A1561 1
HET MG A1562 1
HET MG A1563 1
HET MG A1564 1
HET MG A1565 1
HET MG A1566 1
HET MG A1567 1
HET MG A1568 1
HET MG A1569 1
HET MG A1570 1
HET MG A1571 1
HET MG A1572 1
HET MG A1573 1
HET MG A1574 1
HET MG A1575 1
HET MG A1576 1
HET MG A1577 1
HET WO2 A1578 82
HET WO2 A1579 82
HET WO2 A1580 82
HET WO2 B1001 82
HET WO2 B1002 82
HET WO2 B1004 82
HET MG D 210 1
HET MG D 211 1
HET ZN D 212 1
HET MG E 1 1
HET WO2 E1005 82
HET WO2 E1012 82
HET MG G 157 1
HET WO2 H1010 82
HET MG J 106 1
HET WO2 J1009 82
HET MG K 130 1
HET WO2 K1014 82
HET MG L 136 1
HET ZN N 76 1
HET MG P 89 1
HET MG Q 106 1
HET MG Q 107 1
HET MG T 107 1
HET MG T 108 1
HET MG T 109 1
HET WO2 T1013 82
HETNAM MG MAGNESIUM ION
HETNAM WO2 OCTADECATUNGSTENYL DIPHOSPHATE
HETNAM ZN ZINC ION
FORMUL 23 MG 75(MG 2+)
FORMUL 85 WO2 12(O62 P2 W18)
FORMUL 93 ZN 2(ZN 2+)
LINK OP1 G A 21 MG MG A1517 1555 1555 2.14
LINK O4' C A 67 MG MG A1527 1555 1555 2.32
LINK O3' G A 78 MG MG A1524 1555 1555 2.21
LINK O2' G A 78 MG MG A1524 1555 1555 2.31
LINK OP2 G A 104 MG MG A1522 1555 1555 2.20
LINK O4' A A 166 MG MG A1527 1555 1555 2.24
LINK OP2 C A 184 MG MG A1528 1555 1555 2.48
LINK O5' G A 190 MG MG A1529 1555 1555 2.21
LINK O4' G A 190 MG MG A1529 1555 1555 2.45
LINK O3' C A 526 MG MG A1540 1555 1555 2.35
LINK OP1 G A 541 MG MG A1531 1555 1555 2.31
LINK OP2 U A 543 MG MG A1541 1555 1555 2.18
LINK OP2 A A 555 MG MG A1542 1555 1555 2.16
LINK OP2 G A 571 MG MG A1544 1555 1555 2.37
LINK OP2 G A 580 MG MG A1545 1555 1555 2.20
LINK OP2 A A 591 MG MG A1546 1555 1555 2.50
LINK OP2 A A 751 MG MG A1552 1555 1555 2.50
LINK OP1 G A 921 MG MG A1566 1555 1555 2.28
LINK OP2 A A1164 MG MG A1572 1555 1555 2.06
LINK OP2 G A1179 MG MG A1569 1555 1555 2.20
LINK OP1 G A1205 MG MG A1567 1555 1555 2.26
LINK OP2 A A1477 MG MG A1576 1555 1555 2.15
LINK OP1 G A1482 MG MG A1576 1555 1555 2.15
LINK OP2 G A1482 MG MG A1576 1555 1555 2.23
SITE 1 AC1 1 LYS E 121
SITE 1 AC2 1 G A 21
SITE 1 AC3 2 U A 37 LYS L 124
SITE 1 AC4 1 U A 45
SITE 1 AC5 1 G A 104
SITE 1 AC6 1 C A 71
SITE 1 AC7 2 G A 78 U A 79
SITE 1 AC8 1 C A 93
SITE 1 AC9 3 C A 67 A A 165 A A 166
SITE 1 BC1 4 ALA T 77 ALA T 78 ARG T 79 ARG T 80
SITE 1 BC2 2 G A 183 C A 184
SITE 1 BC3 2 U A 189 G A 190
SITE 1 BC4 3 ARG Q 25 LYS Q 37 ARG Q 38
SITE 1 BC5 4 G A 249 LYS Q 67 ARG Q 68 LYS Q 69
SITE 1 BC6 2 G A 294 G A 541
SITE 1 BC7 3 LYS P 27 ARG P 28 ASP P 29
SITE 1 BC8 4 HIS T 16 ARG T 17 GLN T 18 SER T 19
SITE 1 BC9 1 LEU T 10
SITE 1 CC1 2 C A 325 C A 347
SITE 1 CC2 2 A A 358 ARG L 33
SITE 1 CC3 2 G A 375 A A 377
SITE 1 CC4 2 GLY D 2 ARG D 3
SITE 1 CC5 3 SER D 113 ARG D 114 ARG D 115
SITE 1 CC6 3 THR L 131 ALA L 132 ALA L 133
SITE 1 CC7 2 C A 526 G A 527
SITE 1 CC8 2 A A 542 U A 543
SITE 1 CC9 4 U A 554 A A 555 A A 556 A A 557
SITE 1 DC1 2 G A 564 G A 741
SITE 1 DC2 1 G A 571
SITE 1 DC3 4 G A 578 C A 579 G A 580 U A 581
SITE 1 DC4 1 A A 591
SITE 1 DC5 2 G A 3 U A 4
SITE 1 DC6 1 G A 633
SITE 1 DC7 2 U A 669 TRP K 42
SITE 1 DC8 1 G A 683
SITE 1 DC9 2 C A1512 C A1513
SITE 1 EC1 1 A A 751
SITE 1 EC2 2 G A 820 G A 821
SITE 1 EC3 2 G A 835 G A 846
SITE 1 EC4 1 A A 837
SITE 1 EC5 1 A A 841
SITE 1 EC6 1 G A 880
SITE 1 EC7 1 A A 555
SITE 1 EC8 1 A A 895
SITE 1 EC9 2 C A 911 U A1326
SITE 1 FC1 2 A A 914 G A 916
SITE 1 FC2 2 G A 921 G A 922
SITE 1 FC3 1 G A1205
SITE 1 FC4 3 C A1036 G A1178 G A1179
SITE 1 FC5 2 C A1048 A A1074
SITE 1 FC6 2 A A1092 C A1170
SITE 1 FC7 2 C A1153 A A1164
SITE 1 FC8 2 C A1284 G A1285
SITE 1 FC9 1 U A1289
SITE 1 GC1 1 HIS J 62
SITE 1 GC2 3 A A1477 G A1481 G A1482
SITE 1 GC3 1 CYS N 40
SITE 1 GC4 2 ASN B 37 WO2 B1004
SITE 1 GC5 1 LYS C 72
SITE 1 GC6 3 G A1088 GLY C 205 GLU C 206
SITE 1 GC7 2 LYS B 75 WO2 B1001
SITE 1 GC8 1 ALA E 156
SITE 1 GC9 1 LEU J 90
SITE 1 HC1 3 GLY D 167 ARG H 105 GLY H 106
SITE 1 HC2 1 U A1177
SITE 1 HC3 1 VAL E 51
SITE 1 HC4 1 WO2 K1014
SITE 1 HC5 5 LYS K 7 LYS K 8 LYS T 48 GLU T 50
SITE 2 HC5 5 WO2 T1013
CRYST1 407.500 407.500 174.800 90.00 90.00 90.00 P 41 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.002450 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002450 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005720 0.00000
(ATOM LINES ARE NOT SHOWN.)
END