HEADER RIBOSOME 01-AUG-16 5LMR
TITLE STRUCTURE OF BACTERIAL 30S-IF1-IF3-MRNA-TRNA TRANSLATION PRE-
TITLE 2 INITIATION COMPLEX(STATE-2B)
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 SYNONYM: TS9;
COMPND 20 MOL_ID: 7;
COMPND 21 MOLECULE: 30S RIBOSOMAL PROTEIN S7;
COMPND 22 CHAIN: G;
COMPND 23 MOL_ID: 8;
COMPND 24 MOLECULE: 30S RIBOSOMAL PROTEIN S8;
COMPND 25 CHAIN: H;
COMPND 26 MOL_ID: 9;
COMPND 27 MOLECULE: 30S RIBOSOMAL PROTEIN S9;
COMPND 28 CHAIN: I;
COMPND 29 MOL_ID: 10;
COMPND 30 MOLECULE: 30S RIBOSOMAL PROTEIN S10;
COMPND 31 CHAIN: J;
COMPND 32 MOL_ID: 11;
COMPND 33 MOLECULE: 30S RIBOSOMAL PROTEIN S11;
COMPND 34 CHAIN: K;
COMPND 35 MOL_ID: 12;
COMPND 36 MOLECULE: 30S RIBOSOMAL PROTEIN S12;
COMPND 37 CHAIN: L;
COMPND 38 MOL_ID: 13;
COMPND 39 MOLECULE: 30S RIBOSOMAL PROTEIN S13;
COMPND 40 CHAIN: M;
COMPND 41 MOL_ID: 14;
COMPND 42 MOLECULE: 30S RIBOSOMAL PROTEIN S14 TYPE Z;
COMPND 43 CHAIN: N;
COMPND 44 MOL_ID: 15;
COMPND 45 MOLECULE: 30S RIBOSOMAL PROTEIN S15;
COMPND 46 CHAIN: O;
COMPND 47 MOL_ID: 16;
COMPND 48 MOLECULE: 30S RIBOSOMAL PROTEIN S16;
COMPND 49 CHAIN: P;
COMPND 50 MOL_ID: 17;
COMPND 51 MOLECULE: 30S RIBOSOMAL PROTEIN S17;
COMPND 52 CHAIN: Q;
COMPND 53 MOL_ID: 18;
COMPND 54 MOLECULE: 30S RIBOSOMAL PROTEIN S18;
COMPND 55 CHAIN: R;
COMPND 56 MOL_ID: 19;
COMPND 57 MOLECULE: 30S RIBOSOMAL PROTEIN S19;
COMPND 58 CHAIN: S;
COMPND 59 MOL_ID: 20;
COMPND 60 MOLECULE: 30S RIBOSOMAL PROTEIN S20;
COMPND 61 CHAIN: T;
COMPND 62 MOL_ID: 21;
COMPND 63 MOLECULE: 30S RIBOSOMAL PROTEIN THX;
COMPND 64 CHAIN: V;
COMPND 65 SYNONYM: S31;
COMPND 66 MOL_ID: 22;
COMPND 67 MOLECULE: TRANSLATION INITIATION FACTOR IF-1;
COMPND 68 CHAIN: W;
COMPND 69 ENGINEERED: YES;
COMPND 70 MOL_ID: 23;
COMPND 71 MOLECULE: TRANSLATION INITIATION FACTOR IF-3;
COMPND 72 CHAIN: X;
COMPND 73 ENGINEERED: YES;
COMPND 74 MOL_ID: 24;
COMPND 75 MOLECULE: MRNA;
COMPND 76 CHAIN: Y;
COMPND 77 ENGINEERED: YES;
COMPND 78 MOL_ID: 25;
COMPND 79 MOLECULE: TRNAI;
COMPND 80 CHAIN: Z
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 3 ORGANISM_TAXID: 300852;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 6 ORGANISM_TAXID: 300852;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 9 ORGANISM_TAXID: 300852;
SOURCE 10 MOL_ID: 4;
SOURCE 11 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 12 ORGANISM_TAXID: 300852;
SOURCE 13 MOL_ID: 5;
SOURCE 14 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 15 ORGANISM_TAXID: 300852;
SOURCE 16 MOL_ID: 6;
SOURCE 17 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 18 ORGANISM_TAXID: 300852;
SOURCE 19 MOL_ID: 7;
SOURCE 20 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 21 ORGANISM_TAXID: 300852;
SOURCE 22 MOL_ID: 8;
SOURCE 23 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 24 ORGANISM_TAXID: 300852;
SOURCE 25 MOL_ID: 9;
SOURCE 26 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 27 ORGANISM_TAXID: 300852;
SOURCE 28 MOL_ID: 10;
SOURCE 29 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 30 ORGANISM_TAXID: 300852;
SOURCE 31 MOL_ID: 11;
SOURCE 32 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 33 ORGANISM_TAXID: 300852;
SOURCE 34 MOL_ID: 12;
SOURCE 35 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 36 ORGANISM_TAXID: 300852;
SOURCE 37 MOL_ID: 13;
SOURCE 38 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 39 ORGANISM_TAXID: 300852;
SOURCE 40 MOL_ID: 14;
SOURCE 41 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 42 ORGANISM_TAXID: 300852;
SOURCE 43 MOL_ID: 15;
SOURCE 44 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 45 ORGANISM_TAXID: 300852;
SOURCE 46 MOL_ID: 16;
SOURCE 47 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 48 ORGANISM_TAXID: 300852;
SOURCE 49 MOL_ID: 17;
SOURCE 50 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 51 ORGANISM_TAXID: 300852;
SOURCE 52 MOL_ID: 18;
SOURCE 53 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 54 ORGANISM_TAXID: 300852;
SOURCE 55 MOL_ID: 19;
SOURCE 56 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 57 ORGANISM_TAXID: 300852;
SOURCE 58 MOL_ID: 20;
SOURCE 59 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 60 ORGANISM_TAXID: 300852;
SOURCE 61 MOL_ID: 21;
SOURCE 62 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 63 ORGANISM_TAXID: 300852;
SOURCE 64 MOL_ID: 22;
SOURCE 65 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 66 ORGANISM_TAXID: 300852;
SOURCE 67 GENE: INFA, TTHA1669;
SOURCE 68 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 69 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 70 EXPRESSION_SYSTEM_PLASMID: PET13A;
SOURCE 71 MOL_ID: 23;
SOURCE 72 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 73 ORGANISM_TAXID: 300852;
SOURCE 74 GENE: INFC, TTHA0551;
SOURCE 75 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 76 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 77 EXPRESSION_SYSTEM_PLASMID: PET13A;
SOURCE 78 MOL_ID: 24;
SOURCE 79 SYNTHETIC: YES;
SOURCE 80 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 81 ORGANISM_TAXID: 300852;
SOURCE 82 MOL_ID: 25;
SOURCE 83 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS HB8;
SOURCE 84 ORGANISM_TAXID: 300852
KEYWDS RIBOSOME, TRANSLATION, INITIATION FACTORS, 30S, IF1, IF3, TRNAI, PIC,
KEYWDS 2 THERMUS THERMOPHILUS
EXPDTA ELECTRON MICROSCOPY
AUTHOR T.HUSSAIN,J.L.LLACER,B.T.WIMBERLY,V.RAMAKRISHNAN
REVDAT 3 02-OCT-19 5LMR 1 CRYST1 SCALE
REVDAT 2 02-AUG-17 5LMR 1
REVDAT 1 05-OCT-16 5LMR 0
JRNL AUTH T.HUSSAIN,J.L.LLACER,B.T.WIMBERLY,J.S.KIEFT,V.RAMAKRISHNAN
JRNL TITL LARGE-SCALE MOVEMENTS OF IF3 AND TRNA DURING BACTERIAL
JRNL TITL 2 TRANSLATION INITIATION.
JRNL REF CELL V. 167 133 2016
JRNL REFN ISSN 1097-4172
JRNL PMID 27662086
JRNL DOI 10.1016/J.CELL.2016.08.074
REMARK 2
REMARK 2 RESOLUTION. 4.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 SOFTWARE PACKAGES : RELION, EMAN, EPU, CTFFIND, UCSF
REMARK 3 CHIMERA, COOT, REFMAC, RELION, RELION,
REMARK 3 RELION, RELION
REMARK 3 RECONSTRUCTION SCHEMA : FOURIER SPACE
REMARK 3
REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT
REMARK 3 PDB ENTRY : NULL
REMARK 3 REFINEMENT SPACE : RECIPROCAL
REMARK 3 REFINEMENT PROTOCOL : OTHER
REMARK 3 REFINEMENT TARGET : FSC
REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL
REMARK 3
REMARK 3 FITTING PROCEDURE : NULL
REMARK 3
REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS
REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL
REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 4.450
REMARK 3 NUMBER OF PARTICLES : 17176
REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE
REMARK 3 CORRECTION
REMARK 3
REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL
REMARK 3
REMARK 3 OTHER DETAILS: NULL
REMARK 4
REMARK 4 5LMR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-AUG-16.
REMARK 100 THE DEPOSITION ID IS D_1200000980.
REMARK 245
REMARK 245 EXPERIMENTAL DETAILS
REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE
REMARK 245 SPECIMEN TYPE : NULL
REMARK 245
REMARK 245 ELECTRON MICROSCOPE SAMPLE
REMARK 245 SAMPLE TYPE : PARTICLE
REMARK 245 PARTICLE TYPE : POINT
REMARK 245 NAME OF SAMPLE : 30S-IF1-IF3-MRNA-TRNA PRE
REMARK 245 -INITIATION COMPLEX (STATE-2B)
REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.08
REMARK 245 SAMPLE SUPPORT DETAILS : NULL
REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL
REMARK 245 SAMPLE BUFFER : NULL
REMARK 245 PH : 7.50
REMARK 245 SAMPLE DETAILS : NULL
REMARK 245
REMARK 245 DATA ACQUISITION
REMARK 245 DATE OF EXPERIMENT : NULL
REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 4400
REMARK 245 TEMPERATURE (KELVIN) : NULL
REMARK 245 MICROSCOPE MODEL : FEI POLARA 300
REMARK 245 DETECTOR TYPE : OTHER
REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00
REMARK 245 MAXIMUM DEFOCUS (NM) : 3500.00
REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL
REMARK 245 NOMINAL CS : 2.00
REMARK 245 IMAGING MODE : BRIGHT FIELD
REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 30.00
REMARK 245 ILLUMINATION MODE : FLOOD BEAM
REMARK 245 NOMINAL MAGNIFICATION : 78000
REMARK 245 CALIBRATED MAGNIFICATION : 104478
REMARK 245 SOURCE : FIELD EMISSION GUN
REMARK 245 ACCELERATION VOLTAGE (KV) : 300
REMARK 245 IMAGING DETAILS : NULL
REMARK 247
REMARK 247 ELECTRON MICROSCOPY
REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON
REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE
REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES
REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION
REMARK 247 OF THE STRUCTURE FACTORS.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 25-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 113490 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 284380 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -909.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,
REMARK 350 AND CHAINS: K, L, M, N, O, P, Q, R, S,
REMARK 350 AND CHAINS: T, V, W, X, Y, Z
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 U A 0
REMARK 465 U A 1
REMARK 465 U A 2
REMARK 465 G A 3
REMARK 465 U A 4
REMARK 465 C A 1543
REMARK 465 U A 1544
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 VAL B 3
REMARK 465 GLU B 4
REMARK 465 ILE B 5
REMARK 465 THR B 6
REMARK 465 GLU B 241
REMARK 465 ALA B 242
REMARK 465 GLU B 243
REMARK 465 ALA B 244
REMARK 465 THR B 245
REMARK 465 GLU B 246
REMARK 465 THR B 247
REMARK 465 PRO B 248
REMARK 465 GLU B 249
REMARK 465 GLY B 250
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 MET C 1
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 MET D 1
REMARK 465 MET E 1
REMARK 465 PRO E 2
REMARK 465 GLU E 3
REMARK 465 THR E 4
REMARK 465 GLU E 155
REMARK 465 ALA E 156
REMARK 465 HIS E 157
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 G 1
REMARK 465 MET I 1
REMARK 465 MET J 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 MET K 1
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 LYS K 7
REMARK 465 LYS K 8
REMARK 465 LYS K 9
REMARK 465 VAL K 10
REMARK 465 MET L 4
REMARK 465 ALA L 129
REMARK 465 LYS L 130
REMARK 465 THR L 131
REMARK 465 ALA L 132
REMARK 465 ALA L 133
REMARK 465 LYS L 134
REMARK 465 LYS L 135
REMARK 465 MET M 1
REMARK 465 ALA M 123
REMARK 465 PRO M 124
REMARK 465 ARG M 125
REMARK 465 LYS M 126
REMARK 465 MET N 1
REMARK 465 MET O 1
REMARK 465 ALA P 84
REMARK 465 ARG P 85
REMARK 465 GLU P 86
REMARK 465 GLY P 87
REMARK 465 ALA P 88
REMARK 465 MET Q 1
REMARK 465 ARG Q 101
REMARK 465 GLY Q 102
REMARK 465 GLY Q 103
REMARK 465 LYS Q 104
REMARK 465 ALA Q 105
REMARK 465 MET R 1
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 LYS R 7
REMARK 465 PRO R 8
REMARK 465 LYS R 9
REMARK 465 LYS R 10
REMARK 465 GLU R 11
REMARK 465 ALA R 12
REMARK 465 GLN R 13
REMARK 465 ARG R 14
REMARK 465 ARG R 15
REMARK 465 MET S 1
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 MET T 1
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 MET V 1
REMARK 465 LYS V 26
REMARK 465 LYS V 27
REMARK 465 MET W 0
REMARK 465 MET X 2
REMARK 465 SER X 171
REMARK 465 ALA X 172
REMARK 465 G Y 1
REMARK 465 C Y 2
REMARK 465 U Y 3
REMARK 465 C Y 4
REMARK 465 U Y 5
REMARK 465 U Y 6
REMARK 465 U Y 7
REMARK 465 U Y 8
REMARK 465 A Y 9
REMARK 465 A Y 10
REMARK 465 C Y 11
REMARK 465 A Y 12
REMARK 465 A Y 13
REMARK 465 U Y 14
REMARK 465 U Y 15
REMARK 465 U Y 16
REMARK 465 A Y 17
REMARK 465 U Y 18
REMARK 465 C Y 19
REMARK 465 A Y 33
REMARK 465 A Y 34
REMARK 465 A Y 35
REMARK 465 U Y 40
REMARK 465 C Y 41
REMARK 465 A Y 42
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 U A 5 P OP1 OP2
REMARK 470 G A 567 P OP1 OP2
REMARK 470 A A 914 P OP1 OP2
REMARK 470 C A1397 P OP1 OP2
REMARK 470 THR J 100 OG1 CG2
REMARK 470 ARG S 81 CG CD NE CZ NH1 NH2
REMARK 470 LYS X 79 CG CD CE NZ
REMARK 470 LYS X 81 CG CD CE NZ
REMARK 470 ARG X 82 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 SG CYS D 31 ZN ZN D 300 1.54
REMARK 500 O4 U A 1358 N1 A A 1363A 1.75
REMARK 500 N3 U A 1345 N6 A A 1375 1.87
REMARK 500 O ALA C 92 O THR C 95 1.87
REMARK 500 O4 U A 827 N1 A A 872 1.91
REMARK 500 CE2 TYR I 5 OG1 THR I 7 1.95
REMARK 500 P U A 1257 NZ LYS C 27 2.04
REMARK 500 N3 U A 1358 N6 A A 1363A 2.05
REMARK 500 CG PRO E 93 NH2 ARG H 105 2.05
REMARK 500 OH TYR I 5 OG1 THR I 7 2.05
REMARK 500 NH1 ARG C 30 O ARG N 35 2.06
REMARK 500 N3 U A 827 N6 A A 872 2.13
REMARK 500 O TRP P 59 CG2 VAL P 62 2.14
REMARK 500 O2 C A 999 O2 C A 1043 2.18
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 266 C2' - C3' - O3' ANGL. DEV. = 12.8 DEGREES
REMARK 500 A A 687 C2' - C3' - O3' ANGL. DEV. = 9.9 DEGREES
REMARK 500 C A1145 C2' - C3' - O3' ANGL. DEV. = 13.0 DEGREES
REMARK 500 G A1190 C2' - C3' - O3' ANGL. DEV. = 11.3 DEGREES
REMARK 500 U A1301 C2' - C3' - O3' ANGL. DEV. = 10.3 DEGREES
REMARK 500 U A1498 C2' - C3' - O3' ANGL. DEV. = 11.4 DEGREES
REMARK 500 LEU B 221 CA - CB - CG ANGL. DEV. = 14.4 DEGREES
REMARK 500 LEU C 34 CA - CB - CG ANGL. DEV. = 15.1 DEGREES
REMARK 500 ALA C 65 CB - CA - C ANGL. DEV. = -22.3 DEGREES
REMARK 500 ALA C 65 N - CA - C ANGL. DEV. = -20.2 DEGREES
REMARK 500 VAL C 66 N - CA - C ANGL. DEV. = -23.5 DEGREES
REMARK 500 LEU C 91 CA - CB - CG ANGL. DEV. = 14.8 DEGREES
REMARK 500 LEU E 12 CA - CB - CG ANGL. DEV. = 14.9 DEGREES
REMARK 500 ARG E 15 CB - CA - C ANGL. DEV. = -24.8 DEGREES
REMARK 500 ARG E 15 N - CA - C ANGL. DEV. = -23.6 DEGREES
REMARK 500 LEU F 75 CA - CB - CG ANGL. DEV. = 14.0 DEGREES
REMARK 500 GLU J 61 N - CA - CB ANGL. DEV. = -15.0 DEGREES
REMARK 500 LEU M 81 CA - CB - CG ANGL. DEV. = 18.7 DEGREES
REMARK 500 LEU N 44 CA - CB - CG ANGL. DEV. = 16.8 DEGREES
REMARK 500 ARG W 23 N - CA - C ANGL. DEV. = -31.8 DEGREES
REMARK 500 U Z 47 C2' - C3' - O3' 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 LYS B 8 -117.20 -132.64
REMARK 500 GLU B 9 94.80 68.09
REMARK 500 LEU B 11 43.14 -96.22
REMARK 500 GLU B 12 47.93 -77.27
REMARK 500 HIS B 16 -80.80 -85.78
REMARK 500 PHE B 17 -118.32 17.28
REMARK 500 GLU B 20 135.76 64.15
REMARK 500 ARG B 21 -102.27 -66.92
REMARK 500 TRP B 24 -164.99 38.35
REMARK 500 ALA B 29 -18.62 -48.09
REMARK 500 ALA B 34 -162.16 -162.60
REMARK 500 GLN B 78 3.10 -64.85
REMARK 500 ASP B 79 -30.53 -133.70
REMARK 500 GLN B 95 -82.72 -67.13
REMARK 500 ASN B 104 58.76 -108.14
REMARK 500 PRO B 125 6.72 -59.36
REMARK 500 ARG B 130 179.69 68.12
REMARK 500 PRO B 167 38.31 -86.37
REMARK 500 LEU B 180 31.04 -99.65
REMARK 500 ASN B 204 99.36 -39.99
REMARK 500 ASP B 206 -156.61 -109.70
REMARK 500 ALA B 207 107.99 56.88
REMARK 500 VAL B 229 100.98 60.07
REMARK 500 GLU B 231 152.29 -47.39
REMARK 500 SER B 233 129.94 -33.02
REMARK 500 SER B 235 33.35 -79.61
REMARK 500 TYR B 236 41.32 -108.64
REMARK 500 VAL B 239 77.72 -105.04
REMARK 500 ASN C 3 -151.93 -88.93
REMARK 500 LYS C 4 98.08 62.47
REMARK 500 ILE C 14 -107.82 -93.53
REMARK 500 ALA C 53 -62.91 -103.10
REMARK 500 ALA C 61 105.64 52.57
REMARK 500 ASN C 108 105.83 65.95
REMARK 500 ARG C 126 4.05 -66.61
REMARK 500 SER C 154 -116.33 -76.50
REMARK 500 ARG C 156 70.78 70.90
REMARK 500 ARG C 164 -158.99 -104.56
REMARK 500 TRP C 167 -117.71 -118.50
REMARK 500 ALA C 168 125.42 69.52
REMARK 500 VAL C 173 74.55 -116.18
REMARK 500 THR C 177 94.43 -67.13
REMARK 500 ARG C 179 -1.53 -176.51
REMARK 500 GLU C 206 -166.22 -77.06
REMARK 500 ILE D 5 109.89 61.77
REMARK 500 TYR D 20 61.18 -105.75
REMARK 500 ARG D 25 -47.90 65.49
REMARK 500 CYS D 26 4.92 -62.56
REMARK 500 PRO D 29 57.73 -68.61
REMARK 500 LYS D 30 -2.65 -151.04
REMARK 500
REMARK 500 THIS ENTRY HAS 188 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 HIS B 16 PHE B 17 -149.65
REMARK 500 ASP X 53 PRO X 54 -142.08
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 N 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS N 24 SG
REMARK 620 2 CYS N 27 SG 96.2
REMARK 620 3 CYS N 40 SG 108.0 126.5
REMARK 620 4 CYS N 43 SG 106.7 110.2 107.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 300
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN N 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG W 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residues 5MU Z 54 and PSU Z 55
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: EMD-4077 RELATED DB: EMDB
REMARK 900 STRUCTURE OF BACTERIAL 30S-IF1-IF3-MRNA-TRNA TRANSLATION PRE-
REMARK 900 INITIATION COMPLEX(STATE-2B)
DBREF1 5LMR A 0 1544 GB AP008226.1
DBREF2 5LMR A 55771382 131300 132821
DBREF 5LMR B 1 256 UNP P80371 RS2_THET8 1 256
DBREF 5LMR C 1 239 UNP P80372 RS3_THET8 1 239
DBREF 5LMR D 1 209 UNP P80373 RS4_THET8 1 209
DBREF 5LMR E 1 162 UNP Q5SHQ5 RS5_THET8 1 162
DBREF 5LMR F 1 101 UNP Q5SLP8 RS6_THET8 1 101
DBREF 5LMR G 1 156 UNP P17291 RS7_THET8 1 156
DBREF 5LMR H 1 138 UNP Q5SHQ2 RS8_THET8 1 138
DBREF 5LMR I 1 128 UNP P80374 RS9_THET8 1 128
DBREF 5LMR J 1 105 UNP Q5SHN7 RS10_THET8 1 105
DBREF 5LMR K 1 129 UNP P80376 RS11_THET8 1 129
DBREF 5LMR L 4 135 UNP Q5SHN3 RS12_THET8 1 132
DBREF 5LMR M 1 126 UNP P80377 RS13_THET8 1 126
DBREF 5LMR N 1 61 UNP Q5SHQ1 RS14Z_THET8 1 61
DBREF 5LMR O 1 89 UNP Q5SJ76 RS15_THET8 1 89
DBREF 5LMR P 1 88 UNP Q5SJH3 RS16_THET8 1 88
DBREF 5LMR Q 1 105 UNP Q5SHP7 RS17_THET8 1 105
DBREF 5LMR R 1 88 UNP Q5SLQ0 RS18_THET8 1 88
DBREF 5LMR S 1 93 UNP Q5SHP2 RS19_THET8 1 93
DBREF 5LMR T 1 106 UNP P80380 RS20_THET8 1 106
DBREF 5LMR V 1 27 UNP Q5SIH3 RSHX_THET8 1 27
DBREF 5LMR W 0 71 UNP Q5SHR1 IF1_THET8 1 72
DBREF 5LMR X 2 172 UNP Q5SKU2 IF3_THET8 1 171
DBREF 5LMR Y 1 42 PDB 5LMR 5LMR 1 42
DBREF 5LMR Z 1 76 PDB 5LMR 5LMR 1 76
SEQRES 1 A 1522 U U U G U U G G A G A G U
SEQRES 2 A 1522 U U G A U C C U G G C U C
SEQRES 3 A 1522 A G G G U G A A C G C U G
SEQRES 4 A 1522 G C G G C G U G C C U A A
SEQRES 5 A 1522 G A C A U G C A A G U C G
SEQRES 6 A 1522 U G C G G G C C G C G G G
SEQRES 7 A 1522 G U U U U A C U C C G U G
SEQRES 8 A 1522 G U C A G C G G C G G A C
SEQRES 9 A 1522 G G G U G A G U A A C G C
SEQRES 10 A 1522 G U G G G U G A C C U A C
SEQRES 11 A 1522 C C G G A A G A G G G G G
SEQRES 12 A 1522 A C A A C C C G G G G A A
SEQRES 13 A 1522 A C U C G G G C U A A U C
SEQRES 14 A 1522 C C C C A U G U G G A C C
SEQRES 15 A 1522 C G C C C C U U G G G G U
SEQRES 16 A 1522 G U G U C C A A A G G G C
SEQRES 17 A 1522 U U U G C C C G C U U C C
SEQRES 18 A 1522 G G A U G G G C C C G C G
SEQRES 19 A 1522 U C C C A U C A G C U A G
SEQRES 20 A 1522 U U G G U G G G G U A A U
SEQRES 21 A 1522 G G C C C A C C A A G G C
SEQRES 22 A 1522 G A C G A C G G G U A G C
SEQRES 23 A 1522 C G G U C U G A G A G G A
SEQRES 24 A 1522 U G G C C G G C C A C A G
SEQRES 25 A 1522 G G G C A C U G A G A C A
SEQRES 26 A 1522 C G G G C C C C A C U C C
SEQRES 27 A 1522 U A C G G G A G G C A G C
SEQRES 28 A 1522 A G U U A G G A A U C U U
SEQRES 29 A 1522 C C G C A A U G G G C G C
SEQRES 30 A 1522 A A G C C U G A C G G A G
SEQRES 31 A 1522 C G A C G C C G C U U G G
SEQRES 32 A 1522 A G G A A G A A G C C C U
SEQRES 33 A 1522 U C G G G G U G U A A A C
SEQRES 34 A 1522 U C C U G A A C C C G G G
SEQRES 35 A 1522 A C G A A A C C C C C G A
SEQRES 36 A 1522 C G A G G G G A C U G A C
SEQRES 37 A 1522 G G U A C C G G G G U A A
SEQRES 38 A 1522 U A G C G C C G G C C A A
SEQRES 39 A 1522 C U C C G U G C C A G C A
SEQRES 40 A 1522 G C C G C G G U A A U A C
SEQRES 41 A 1522 G G A G G G C G C G A G C
SEQRES 42 A 1522 G U U A C C C G G A U U C
SEQRES 43 A 1522 A C U G G G C G U A A A G
SEQRES 44 A 1522 G G C G U G U A G G C G G
SEQRES 45 A 1522 C C U G G G G C G U C C C
SEQRES 46 A 1522 A U G U G A A A G A C C A
SEQRES 47 A 1522 C G G C U C A A C C G U G
SEQRES 48 A 1522 G G G G A G C G U G G G A
SEQRES 49 A 1522 U A C G C U C A G G C U A
SEQRES 50 A 1522 G A C G G U G G G A G A G
SEQRES 51 A 1522 G G U G G U G G A A U U C
SEQRES 52 A 1522 C C G G A G U A G C G G U
SEQRES 53 A 1522 G A A A U G C G C A G A U
SEQRES 54 A 1522 A C C G G G A G G A A C G
SEQRES 55 A 1522 C C G A U G G C G A A G G
SEQRES 56 A 1522 C A G C C A C C U G G U C
SEQRES 57 A 1522 C A C C C G U G A C G C U
SEQRES 58 A 1522 G A G G C G C G A A A G C
SEQRES 59 A 1522 G U G G G G A G C A A A C
SEQRES 60 A 1522 C G G A U U A G A U A C C
SEQRES 61 A 1522 C G G G U A G U C C A C G
SEQRES 62 A 1522 C C C U A A A C G A U G C
SEQRES 63 A 1522 G C G C U A G G U C U C U
SEQRES 64 A 1522 G G G U C U C C U G G G G
SEQRES 65 A 1522 G C C G A A G C U A A C G
SEQRES 66 A 1522 C G U U A A G C G C G C C
SEQRES 67 A 1522 G C C U G G G G A G U A C
SEQRES 68 A 1522 G G C C G C A A G G C U G
SEQRES 69 A 1522 A A A C U C A A A G G A A
SEQRES 70 A 1522 U U G A C G G G G G C C C
SEQRES 71 A 1522 G C A C A A G C G G U G G
SEQRES 72 A 1522 A G C A U G U G G U U U A
SEQRES 73 A 1522 A U U C G A A G C A A C G
SEQRES 74 A 1522 C G A A G A A C C U U A C
SEQRES 75 A 1522 C A G G C C U U G A C A U
SEQRES 76 A 1522 G C U A G G G A A C C C G
SEQRES 77 A 1522 G G U G A A A G C C U G G
SEQRES 78 A 1522 G G U G C C C C G C G A G
SEQRES 79 A 1522 G G G A G C C C U A G C A
SEQRES 80 A 1522 C A G G U G C U G C A U G
SEQRES 81 A 1522 G C C G U C G U C A G C U
SEQRES 82 A 1522 C G U G C C G U G A G G U
SEQRES 83 A 1522 G U U G G G U U A A G U C
SEQRES 84 A 1522 C C G C A A C G A G C G C
SEQRES 85 A 1522 A A C C C C C G C C G U U
SEQRES 86 A 1522 A G U U G C C A G C G G U
SEQRES 87 A 1522 U C G G C C G G G C A C U
SEQRES 88 A 1522 C U A A C G G G A C U G C
SEQRES 89 A 1522 C C G C G A A A G C G G G
SEQRES 90 A 1522 A G G A A G G A G G G G A
SEQRES 91 A 1522 C G A C G U C U G G U C A
SEQRES 92 A 1522 G C A U G G C C C U U A C
SEQRES 93 A 1522 G G C C U G G G C G A C A
SEQRES 94 A 1522 C A C G U G C U A C A A U
SEQRES 95 A 1522 G C C C A C U A C A A A G
SEQRES 96 A 1522 C G A U G C C A C C C G G
SEQRES 97 A 1522 C A A C G G G G A G C U A
SEQRES 98 A 1522 A U C G C A A A A A G G U
SEQRES 99 A 1522 G G G C C C A G U U C G G
SEQRES 100 A 1522 A U U G G G G U C U G C A
SEQRES 101 A 1522 A C C C G A C C C C A U G
SEQRES 102 A 1522 A A G C C G G A A U C G C
SEQRES 103 A 1522 U A G U A A U C G C G G A
SEQRES 104 A 1522 U C A G C C A U G C C G C
SEQRES 105 A 1522 G G U G A A U A C G U U C
SEQRES 106 A 1522 C C G G G C C U U G U A C
SEQRES 107 A 1522 A C A C C G C C C G U C A
SEQRES 108 A 1522 C G C C A U G G G A G C G
SEQRES 109 A 1522 G G C U C U A C C C G A A
SEQRES 110 A 1522 G U C G C C G G G A G C C
SEQRES 111 A 1522 U A C G G G C A G G C G C
SEQRES 112 A 1522 C G A G G G U A G G G C C
SEQRES 113 A 1522 C G U G A C U G G G G C G
SEQRES 114 A 1522 A A G U C G U A A C A A G
SEQRES 115 A 1522 G U A G C U G U A C C G G
SEQRES 116 A 1522 A A G G U G C G G C U G G
SEQRES 117 A 1522 A U C A C C U C C U U U C
SEQRES 118 A 1522 U
SEQRES 1 B 256 MET PRO VAL GLU ILE THR VAL LYS GLU LEU LEU GLU ALA
SEQRES 2 B 256 GLY VAL HIS PHE GLY HIS GLU ARG LYS ARG TRP ASN PRO
SEQRES 3 B 256 LYS PHE ALA ARG TYR ILE TYR ALA GLU ARG ASN GLY ILE
SEQRES 4 B 256 HIS ILE ILE ASP LEU GLN LYS THR MET GLU GLU LEU GLU
SEQRES 5 B 256 ARG THR PHE ARG PHE ILE GLU ASP LEU ALA MET ARG GLY
SEQRES 6 B 256 GLY THR ILE LEU PHE VAL GLY THR LYS LYS GLN ALA GLN
SEQRES 7 B 256 ASP ILE VAL ARG MET GLU ALA GLU ARG ALA GLY MET PRO
SEQRES 8 B 256 TYR VAL ASN GLN ARG TRP LEU GLY GLY MET LEU THR ASN
SEQRES 9 B 256 PHE LYS THR ILE SER GLN ARG VAL HIS ARG LEU GLU GLU
SEQRES 10 B 256 LEU GLU ALA LEU PHE ALA SER PRO GLU ILE GLU GLU ARG
SEQRES 11 B 256 PRO LYS LYS GLU GLN VAL ARG LEU LYS HIS GLU LEU GLU
SEQRES 12 B 256 ARG LEU GLN LYS TYR LEU SER GLY PHE ARG LEU LEU LYS
SEQRES 13 B 256 ARG LEU PRO ASP ALA ILE PHE VAL VAL ASP PRO THR LYS
SEQRES 14 B 256 GLU ALA ILE ALA VAL ARG GLU ALA ARG LYS LEU PHE ILE
SEQRES 15 B 256 PRO VAL ILE ALA LEU ALA ASP THR ASP SER ASP PRO ASP
SEQRES 16 B 256 LEU VAL ASP TYR ILE ILE PRO GLY ASN ASP ASP ALA ILE
SEQRES 17 B 256 ARG SER ILE GLN LEU ILE LEU SER ARG ALA VAL ASP LEU
SEQRES 18 B 256 ILE ILE GLN ALA ARG GLY GLY VAL VAL GLU PRO SER PRO
SEQRES 19 B 256 SER TYR ALA LEU VAL GLN GLU ALA GLU ALA THR GLU THR
SEQRES 20 B 256 PRO GLU GLY GLU SER GLU VAL GLU ALA
SEQRES 1 C 239 MET GLY ASN LYS ILE HIS PRO ILE GLY PHE ARG LEU GLY
SEQRES 2 C 239 ILE THR ARG ASP TRP GLU SER ARG TRP TYR ALA GLY LYS
SEQRES 3 C 239 LYS GLN TYR ARG HIS LEU LEU LEU GLU ASP GLN ARG ILE
SEQRES 4 C 239 ARG GLY LEU LEU GLU LYS GLU LEU TYR SER ALA GLY LEU
SEQRES 5 C 239 ALA ARG VAL ASP ILE GLU ARG ALA ALA ASP ASN VAL ALA
SEQRES 6 C 239 VAL THR VAL HIS VAL ALA LYS PRO GLY VAL VAL ILE GLY
SEQRES 7 C 239 ARG GLY GLY GLU ARG ILE ARG VAL LEU ARG GLU GLU LEU
SEQRES 8 C 239 ALA LYS LEU THR GLY LYS ASN VAL ALA LEU ASN VAL GLN
SEQRES 9 C 239 GLU VAL GLN ASN PRO ASN LEU SER ALA PRO LEU VAL ALA
SEQRES 10 C 239 GLN ARG VAL ALA GLU GLN ILE GLU ARG ARG PHE ALA VAL
SEQRES 11 C 239 ARG ARG ALA ILE LYS GLN ALA VAL GLN ARG VAL MET GLU
SEQRES 12 C 239 SER GLY ALA LYS GLY ALA LYS VAL ILE VAL SER GLY ARG
SEQRES 13 C 239 ILE GLY GLY ALA GLU GLN ALA ARG THR GLU TRP ALA ALA
SEQRES 14 C 239 GLN GLY ARG VAL PRO LEU HIS THR LEU ARG ALA ASN ILE
SEQRES 15 C 239 ASP TYR GLY PHE ALA LEU ALA ARG THR THR TYR GLY VAL
SEQRES 16 C 239 LEU GLY VAL LYS ALA TYR ILE PHE LEU GLY GLU VAL ILE
SEQRES 17 C 239 GLY GLY GLN LYS PRO LYS ALA ARG PRO GLU LEU PRO LYS
SEQRES 18 C 239 ALA GLU GLU ARG PRO ARG ARG ARG ARG PRO ALA VAL ARG
SEQRES 19 C 239 VAL LYS LYS GLU GLU
SEQRES 1 D 209 MET GLY ARG TYR ILE GLY PRO VAL CYS ARG LEU CYS ARG
SEQRES 2 D 209 ARG GLU GLY VAL LYS LEU TYR LEU LYS GLY GLU ARG CYS
SEQRES 3 D 209 TYR SER PRO LYS CYS ALA MET GLU ARG ARG PRO TYR PRO
SEQRES 4 D 209 PRO GLY GLN HIS GLY GLN LYS ARG ALA ARG ARG PRO SER
SEQRES 5 D 209 ASP TYR ALA VAL ARG LEU ARG GLU LYS GLN LYS LEU ARG
SEQRES 6 D 209 ARG ILE TYR GLY ILE SER GLU ARG GLN PHE ARG ASN LEU
SEQRES 7 D 209 PHE GLU GLU ALA SER LYS LYS LYS GLY VAL THR GLY SER
SEQRES 8 D 209 VAL PHE LEU GLY LEU LEU GLU SER ARG LEU ASP ASN VAL
SEQRES 9 D 209 VAL TYR ARG LEU GLY PHE ALA VAL SER ARG ARG GLN ALA
SEQRES 10 D 209 ARG GLN LEU VAL ARG HIS GLY HIS ILE THR VAL ASN GLY
SEQRES 11 D 209 ARG ARG VAL ASP LEU PRO SER TYR ARG VAL ARG PRO GLY
SEQRES 12 D 209 ASP GLU ILE ALA VAL ALA GLU LYS SER ARG ASN LEU GLU
SEQRES 13 D 209 LEU ILE ARG GLN ASN LEU GLU ALA MET LYS GLY ARG LYS
SEQRES 14 D 209 VAL GLY PRO TRP LEU SER LEU ASP VAL GLU GLY MET LYS
SEQRES 15 D 209 GLY LYS PHE LEU ARG LEU PRO ASP ARG GLU ASP LEU ALA
SEQRES 16 D 209 LEU PRO VAL ASN GLU GLN LEU VAL ILE GLU PHE TYR SER
SEQRES 17 D 209 ARG
SEQRES 1 E 162 MET PRO GLU THR ASP PHE GLU GLU LYS MET ILE LEU ILE
SEQRES 2 E 162 ARG ARG THR ALA ARG MET GLN ALA GLY GLY ARG ARG PHE
SEQRES 3 E 162 ARG PHE GLY ALA LEU VAL VAL VAL GLY ASP ARG GLN GLY
SEQRES 4 E 162 ARG VAL GLY LEU GLY PHE GLY LYS ALA PRO GLU VAL PRO
SEQRES 5 E 162 LEU ALA VAL GLN LYS ALA GLY TYR TYR ALA ARG ARG ASN
SEQRES 6 E 162 MET VAL GLU VAL PRO LEU GLN ASN GLY THR ILE PRO HIS
SEQRES 7 E 162 GLU ILE GLU VAL GLU PHE GLY ALA SER LYS ILE VAL LEU
SEQRES 8 E 162 LYS PRO ALA ALA PRO GLY THR GLY VAL ILE ALA GLY ALA
SEQRES 9 E 162 VAL PRO ARG ALA ILE LEU GLU LEU ALA GLY VAL THR ASP
SEQRES 10 E 162 ILE LEU THR LYS GLU LEU GLY SER ARG ASN PRO ILE ASN
SEQRES 11 E 162 ILE ALA TYR ALA THR MET GLU ALA LEU ARG GLN LEU ARG
SEQRES 12 E 162 THR LYS ALA ASP VAL GLU ARG LEU ARG LYS GLY GLU ALA
SEQRES 13 E 162 HIS 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 156 MET ALA ARG ARG ARG ARG ALA GLU VAL ARG GLN LEU GLN
SEQRES 2 G 156 PRO ASP LEU VAL TYR GLY ASP VAL LEU VAL THR ALA PHE
SEQRES 3 G 156 ILE ASN LYS ILE MET ARG ASP GLY LYS LYS ASN LEU ALA
SEQRES 4 G 156 ALA ARG ILE PHE TYR ASP ALA CYS LYS ILE ILE GLN GLU
SEQRES 5 G 156 LYS THR GLY GLN GLU PRO LEU LYS VAL PHE LYS GLN ALA
SEQRES 6 G 156 VAL GLU ASN VAL LYS PRO ARG MET GLU VAL ARG SER ARG
SEQRES 7 G 156 ARG VAL GLY GLY ALA ASN TYR GLN VAL PRO MET GLU VAL
SEQRES 8 G 156 SER PRO ARG ARG GLN GLN SER LEU ALA LEU ARG TRP LEU
SEQRES 9 G 156 VAL GLN ALA ALA ASN GLN ARG PRO GLU ARG ARG ALA ALA
SEQRES 10 G 156 VAL ARG ILE ALA HIS GLU LEU MET ASP ALA ALA GLU GLY
SEQRES 11 G 156 LYS GLY GLY ALA VAL LYS LYS LYS GLU ASP VAL GLU ARG
SEQRES 12 G 156 MET 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 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 HIS 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 105 MET PRO LYS ILE ARG ILE LYS LEU ARG GLY PHE ASP HIS
SEQRES 2 J 105 LYS THR LEU ASP ALA SER ALA GLN LYS ILE VAL GLU ALA
SEQRES 3 J 105 ALA ARG ARG SER GLY ALA GLN VAL SER GLY PRO ILE PRO
SEQRES 4 J 105 LEU PRO THR ARG VAL ARG ARG PHE THR VAL ILE ARG GLY
SEQRES 5 J 105 PRO PHE LYS HIS LYS ASP SER ARG GLU HIS PHE GLU LEU
SEQRES 6 J 105 ARG THR HIS ASN ARG LEU VAL ASP ILE ILE ASN PRO ASN
SEQRES 7 J 105 ARG LYS THR ILE GLU GLN LEU MET THR LEU ASP LEU PRO
SEQRES 8 J 105 THR GLY VAL GLU ILE GLU ILE LYS THR VAL GLY GLY GLY
SEQRES 9 J 105 ARG
SEQRES 1 K 129 MET ALA LYS LYS PRO SER LYS LYS LYS VAL LYS ARG GLN
SEQRES 2 K 129 VAL ALA SER GLY ARG ALA TYR ILE HIS ALA SER TYR ASN
SEQRES 3 K 129 ASN THR ILE VAL THR ILE THR ASP PRO ASP GLY ASN PRO
SEQRES 4 K 129 ILE THR TRP SER SER GLY GLY VAL ILE GLY TYR LYS GLY
SEQRES 5 K 129 SER ARG LYS GLY THR PRO TYR ALA ALA GLN LEU ALA ALA
SEQRES 6 K 129 LEU ASP ALA ALA LYS LYS ALA MET ALA TYR GLY MET GLN
SEQRES 7 K 129 SER VAL ASP VAL ILE VAL ARG GLY THR GLY ALA GLY ARG
SEQRES 8 K 129 GLU GLN ALA ILE ARG ALA LEU GLN ALA SER GLY LEU GLN
SEQRES 9 K 129 VAL LYS SER ILE VAL ASP ASP THR PRO VAL PRO HIS ASN
SEQRES 10 K 129 GLY CYS ARG PRO LYS LYS LYS PHE ARG LYS ALA SER
SEQRES 1 L 132 MET PRO THR ILE ASN GLN LEU VAL ARG LYS GLY ARG GLU
SEQRES 2 L 132 LYS VAL ARG LYS LYS SER LYS VAL PRO ALA LEU LYS GLY
SEQRES 3 L 132 ALA PRO PHE ARG ARG GLY VAL CYS THR VAL VAL ARG THR
SEQRES 4 L 132 VAL THR PRO LYS LYS PRO ASN SER ALA LEU ARG LYS VAL
SEQRES 5 L 132 ALA LYS VAL ARG LEU THR SER GLY TYR GLU VAL THR ALA
SEQRES 6 L 132 TYR ILE PRO GLY GLU GLY HIS ASN LEU GLN GLU HIS SER
SEQRES 7 L 132 VAL VAL LEU ILE ARG GLY GLY ARG VAL LYS ASP LEU PRO
SEQRES 8 L 132 GLY VAL ARG TYR HIS ILE VAL ARG GLY VAL TYR ASP ALA
SEQRES 9 L 132 ALA GLY VAL LYS ASP ARG LYS LYS SER ARG SER LYS TYR
SEQRES 10 L 132 GLY THR LYS LYS PRO LYS GLU ALA ALA LYS THR ALA ALA
SEQRES 11 L 132 LYS LYS
SEQRES 1 M 126 MET ALA ARG ILE ALA GLY VAL GLU ILE PRO ARG ASN LYS
SEQRES 2 M 126 ARG VAL ASP VAL ALA LEU THR TYR ILE TYR GLY ILE GLY
SEQRES 3 M 126 LYS ALA ARG ALA LYS GLU ALA LEU GLU LYS THR GLY ILE
SEQRES 4 M 126 ASN PRO ALA THR ARG VAL LYS ASP LEU THR GLU ALA GLU
SEQRES 5 M 126 VAL VAL ARG LEU ARG GLU TYR VAL GLU ASN THR TRP LYS
SEQRES 6 M 126 LEU GLU GLY GLU LEU ARG ALA GLU VAL ALA ALA ASN ILE
SEQRES 7 M 126 LYS ARG LEU MET ASP ILE GLY CYS TYR ARG GLY LEU ARG
SEQRES 8 M 126 HIS ARG ARG GLY LEU PRO VAL ARG GLY GLN ARG THR ARG
SEQRES 9 M 126 THR ASN ALA ARG THR ARG LYS GLY PRO ARG LYS THR VAL
SEQRES 10 M 126 ALA GLY LYS LYS LYS ALA PRO ARG LYS
SEQRES 1 N 61 MET ALA ARG LYS ALA LEU ILE GLU LYS ALA LYS ARG THR
SEQRES 2 N 61 PRO LYS PHE LYS VAL ARG ALA TYR THR ARG CYS VAL ARG
SEQRES 3 N 61 CYS GLY ARG ALA ARG SER VAL TYR ARG PHE PHE GLY LEU
SEQRES 4 N 61 CYS ARG ILE CYS LEU ARG GLU LEU ALA HIS LYS GLY GLN
SEQRES 5 N 61 LEU PRO GLY VAL ARG LYS ALA SER TRP
SEQRES 1 O 89 MET PRO ILE THR LYS GLU GLU LYS GLN LYS VAL ILE GLN
SEQRES 2 O 89 GLU PHE ALA ARG PHE PRO GLY ASP THR GLY SER THR GLU
SEQRES 3 O 89 VAL GLN VAL ALA LEU LEU THR LEU ARG ILE ASN ARG LEU
SEQRES 4 O 89 SER GLU HIS LEU LYS VAL HIS LYS LYS ASP HIS HIS SER
SEQRES 5 O 89 HIS ARG GLY LEU LEU MET MET VAL GLY GLN ARG ARG ARG
SEQRES 6 O 89 LEU LEU ARG TYR LEU GLN ARG GLU ASP PRO GLU ARG TYR
SEQRES 7 O 89 ARG 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 105 MET PRO LYS LYS VAL LEU THR GLY VAL VAL VAL SER ASP
SEQRES 2 Q 105 LYS MET GLN LYS THR VAL THR VAL LEU VAL GLU ARG GLN
SEQRES 3 Q 105 PHE PRO HIS PRO LEU TYR GLY LYS VAL ILE LYS ARG SER
SEQRES 4 Q 105 LYS LYS TYR LEU ALA HIS ASP PRO GLU GLU LYS TYR LYS
SEQRES 5 Q 105 LEU GLY ASP VAL VAL GLU ILE ILE GLU SER ARG PRO ILE
SEQRES 6 Q 105 SER LYS ARG LYS ARG PHE ARG VAL LEU ARG LEU VAL GLU
SEQRES 7 Q 105 SER GLY ARG MET ASP LEU VAL GLU LYS TYR LEU ILE ARG
SEQRES 8 Q 105 ARG GLN ASN TYR GLU SER LEU SER LYS ARG GLY GLY LYS
SEQRES 9 Q 105 ALA
SEQRES 1 R 88 MET SER THR LYS ASN ALA LYS PRO LYS LYS GLU ALA GLN
SEQRES 2 R 88 ARG ARG PRO SER ARG LYS ALA LYS VAL LYS ALA THR LEU
SEQRES 3 R 88 GLY GLU PHE ASP LEU ARG ASP TYR ARG ASN VAL GLU VAL
SEQRES 4 R 88 LEU LYS ARG PHE LEU SER GLU THR GLY LYS ILE LEU PRO
SEQRES 5 R 88 ARG ARG ARG THR GLY LEU SER ALA LYS GLU GLN ARG ILE
SEQRES 6 R 88 LEU ALA LYS THR ILE LYS ARG ALA ARG ILE LEU GLY LEU
SEQRES 7 R 88 LEU PRO PHE THR GLU LYS LEU VAL ARG LYS
SEQRES 1 S 93 MET PRO ARG SER LEU LYS LYS GLY VAL PHE VAL ASP ASP
SEQRES 2 S 93 HIS LEU LEU GLU LYS VAL LEU GLU LEU ASN ALA LYS GLY
SEQRES 3 S 93 GLU LYS ARG LEU ILE LYS THR TRP SER ARG ARG SER THR
SEQRES 4 S 93 ILE VAL PRO GLU MET VAL GLY HIS THR ILE ALA VAL TYR
SEQRES 5 S 93 ASN GLY LYS GLN HIS VAL PRO VAL TYR ILE THR GLU ASN
SEQRES 6 S 93 MET VAL GLY HIS LYS LEU GLY GLU PHE ALA PRO THR ARG
SEQRES 7 S 93 THR TYR ARG GLY HIS GLY LYS GLU ALA LYS ALA THR LYS
SEQRES 8 S 93 LYS LYS
SEQRES 1 T 106 MET ALA GLN LYS LYS PRO LYS ARG ASN LEU SER ALA LEU
SEQRES 2 T 106 LYS ARG HIS ARG GLN SER LEU LYS ARG ARG LEU ARG ASN
SEQRES 3 T 106 LYS ALA LYS LYS SER ALA ILE LYS THR LEU SER LYS LYS
SEQRES 4 T 106 ALA ILE GLN LEU ALA GLN GLU GLY LYS ALA GLU GLU ALA
SEQRES 5 T 106 LEU LYS ILE MET ARG LYS ALA GLU SER LEU ILE ASP LYS
SEQRES 6 T 106 ALA ALA LYS GLY SER THR LEU HIS LYS ASN ALA ALA ALA
SEQRES 7 T 106 ARG ARG LYS SER ARG LEU MET ARG LYS VAL ARG GLN LEU
SEQRES 8 T 106 LEU GLU ALA ALA GLY ALA PRO LEU ILE GLY GLY GLY LEU
SEQRES 9 T 106 SER ALA
SEQRES 1 V 27 MET GLY LYS GLY ASP ARG ARG THR ARG ARG GLY LYS ILE
SEQRES 2 V 27 TRP ARG GLY THR TYR GLY LYS TYR ARG PRO ARG LYS LYS
SEQRES 3 V 27 LYS
SEQRES 1 W 72 MET ALA LYS GLU LYS ASP THR ILE ARG THR GLU GLY VAL
SEQRES 2 W 72 VAL THR GLU ALA LEU PRO ASN ALA THR PHE ARG VAL LYS
SEQRES 3 W 72 LEU ASP SER GLY PRO GLU ILE LEU ALA TYR ILE SER GLY
SEQRES 4 W 72 LYS MET ARG MET HIS TYR ILE ARG ILE LEU PRO GLY ASP
SEQRES 5 W 72 ARG VAL VAL VAL GLU ILE THR PRO TYR ASP PRO THR ARG
SEQRES 6 W 72 GLY ARG ILE VAL TYR ARG LYS
SEQRES 1 X 171 MET LYS GLU TYR LEU THR ASN GLU ARG ILE ARG ALA LYS
SEQRES 2 X 171 GLN VAL ARG VAL VAL GLY PRO ASP GLY LYS GLN LEU GLY
SEQRES 3 X 171 ILE MET ASP THR ARG GLU ALA LEU ARG LEU ALA GLN GLU
SEQRES 4 X 171 MET ASP LEU ASP LEU VAL LEU VAL GLY PRO ASN ALA ASP
SEQRES 5 X 171 PRO PRO VAL ALA ARG ILE MET ASP TYR SER LYS TRP ARG
SEQRES 6 X 171 TYR GLU GLN GLN MET ALA GLU LYS GLU ALA ARG LYS LYS
SEQRES 7 X 171 ALA LYS ARG THR GLU VAL LYS SER ILE LYS PHE ARG VAL
SEQRES 8 X 171 LYS ILE ASP GLU HIS ASP TYR GLN THR LYS LEU GLY HIS
SEQRES 9 X 171 ILE LYS ARG PHE LEU GLN GLU GLY HIS LYS VAL LYS VAL
SEQRES 10 X 171 THR ILE MET PHE ARG GLY ARG GLU VAL ALA HIS PRO GLU
SEQRES 11 X 171 LEU GLY GLU ARG ILE LEU ASN ARG VAL THR GLU ASP LEU
SEQRES 12 X 171 LYS ASP LEU ALA VAL VAL GLU MET LYS PRO GLU MET LEU
SEQRES 13 X 171 GLY ARG ASP MET ASN MET LEU LEU ALA PRO VAL LYS VAL
SEQRES 14 X 171 SER ALA
SEQRES 1 Y 42 G C U C U U U U A A C A A
SEQRES 2 Y 42 U U U A U C A G G C A A G
SEQRES 3 Y 42 G A G G U A A A A A U G U
SEQRES 4 Y 42 U C A
SEQRES 1 Z 77 C G C G G G G 4SU G G A G C
SEQRES 2 Z 77 A G C C U G G U A G C U C
SEQRES 3 Z 77 G U C G G G OMC U C A U A A
SEQRES 4 Z 77 C C C G A A G G7M U C G U C
SEQRES 5 Z 77 G G 5MU PSU C A A A U C C G G
SEQRES 6 Z 77 C C C C C G C A A C C A
HET 4SU Z 8 20
HET OMC Z 32 21
HET G7M Z 46 24
HET 5MU Z 54 21
HET PSU Z 55 20
HET ZN D 300 1
HET ZN N 101 1
HET MG W 101 1
HET MG Z 101 1
HETNAM 4SU 4-THIOURIDINE-5'-MONOPHOSPHATE
HETNAM OMC O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE
HETNAM G7M N7-METHYL-GUANOSINE-5'-MONOPHOSPHATE
HETNAM 5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE
HETNAM PSU PSEUDOURIDINE-5'-MONOPHOSPHATE
HETNAM ZN ZINC ION
HETNAM MG MAGNESIUM ION
FORMUL 25 4SU C9 H13 N2 O8 P S
FORMUL 25 OMC C10 H16 N3 O8 P
FORMUL 25 G7M C11 H17 N5 O8 P 1+
FORMUL 25 5MU C10 H15 N2 O9 P
FORMUL 25 PSU C9 H13 N2 O9 P
FORMUL 26 ZN 2(ZN 2+)
FORMUL 28 MG 2(MG 2+)
HELIX 1 AA1 ASN B 25 ARG B 30 5 6
HELIX 2 AA2 ASP B 43 GLY B 65 1 23
HELIX 3 AA3 ASP B 79 ALA B 88 1 10
HELIX 4 AA4 ASN B 104 LEU B 121 1 18
HELIX 5 AA5 PRO B 131 GLN B 146 1 16
HELIX 6 AA6 GLY B 151 LEU B 155 5 5
HELIX 7 AA7 GLU B 170 LEU B 180 1 11
HELIX 8 AA8 ALA B 207 GLY B 227 1 21
HELIX 9 AA9 HIS C 6 LEU C 12 1 7
HELIX 10 AB1 GLN C 28 LEU C 47 1 20
HELIX 11 AB2 LYS C 72 GLY C 78 1 7
HELIX 12 AB3 GLU C 82 THR C 95 1 14
HELIX 13 AB4 SER C 112 ARG C 126 1 15
HELIX 14 AB5 ALA C 129 GLY C 145 1 17
HELIX 15 AB6 VAL D 8 GLY D 16 1 9
HELIX 16 AB7 SER D 52 GLY D 69 1 18
HELIX 17 AB8 SER D 71 LYS D 85 1 15
HELIX 18 AB9 VAL D 88 ARG D 100 1 13
HELIX 19 AC1 ARG D 100 LEU D 108 1 9
HELIX 20 AC2 SER D 113 HIS D 123 1 11
HELIX 21 AC3 LEU D 155 MET D 165 1 11
HELIX 22 AC4 ASN D 199 SER D 208 1 10
HELIX 23 AC5 GLU E 50 ASN E 65 1 16
HELIX 24 AC6 GLY E 103 GLY E 114 1 12
HELIX 25 AC7 ASN E 127 LEU E 142 1 16
HELIX 26 AC8 THR E 144 ARG E 152 1 9
HELIX 27 AC9 ASP F 15 TYR F 33 1 19
HELIX 28 AD1 PRO F 68 ASP F 70 5 3
HELIX 29 AD2 ARG F 71 ARG F 82 1 12
HELIX 30 AD3 ASP G 20 MET G 31 1 12
HELIX 31 AD4 LYS G 35 THR G 54 1 20
HELIX 32 AD5 GLU G 57 LYS G 70 1 14
HELIX 33 AD6 SER G 92 ARG G 111 1 20
HELIX 34 AD7 ARG G 115 GLY G 130 1 16
HELIX 35 AD8 GLY G 132 ASN G 148 1 17
HELIX 36 AD9 ARG G 149 ALA G 152 5 4
HELIX 37 AE1 ASP H 4 TYR H 20 1 17
HELIX 38 AE2 SER H 29 GLY H 43 1 15
HELIX 39 AE3 GLY H 96 ILE H 100 5 5
HELIX 40 AE4 ASP H 121 LEU H 127 1 7
HELIX 41 AE5 ASP I 32 PHE I 37 1 6
HELIX 42 AE6 VAL I 41 ALA I 46 5 6
HELIX 43 AE7 LEU I 47 VAL I 53 1 7
HELIX 44 AE8 GLY I 69 ASN I 89 1 21
HELIX 45 AE9 TYR I 92 LYS I 97 1 6
HELIX 46 AF1 LEU J 16 ARG J 29 1 14
HELIX 47 AF2 GLY K 52 GLY K 56 5 5
HELIX 48 AF3 THR K 57 TYR K 75 1 19
HELIX 49 AF4 ARG K 91 SER K 101 1 11
HELIX 50 AF5 THR L 6 GLY L 14 1 9
HELIX 51 AF6 SER L 116 TYR L 120 5 5
HELIX 52 AF7 ARG M 14 TYR M 21 1 8
HELIX 53 AF8 GLY M 26 GLY M 38 1 13
HELIX 54 AF9 THR M 49 ASN M 62 1 14
HELIX 55 AG1 LEU M 66 ASP M 83 1 18
HELIX 56 AG2 CYS M 86 GLY M 95 1 10
HELIX 57 AG3 ALA M 107 GLY M 112 1 6
HELIX 58 AG4 PHE N 16 ALA N 20 5 5
HELIX 59 AG5 ARG N 41 GLY N 51 1 11
HELIX 60 AG6 THR O 4 ALA O 16 1 13
HELIX 61 AG7 SER O 24 HIS O 46 1 23
HELIX 62 AG8 ASP O 49 ASP O 74 1 26
HELIX 63 AG9 ASP O 74 GLY O 86 1 13
HELIX 64 AH1 ASP P 52 GLY P 63 1 12
HELIX 65 AH2 THR P 67 GLY P 78 1 12
HELIX 66 AH3 ARG Q 81 LEU Q 98 1 18
HELIX 67 AH4 ASN R 36 LYS R 41 1 6
HELIX 68 AH5 PRO R 52 GLY R 57 1 6
HELIX 69 AH6 SER R 59 GLY R 77 1 19
HELIX 70 AH7 ASP S 12 LEU S 20 1 9
HELIX 71 AH8 LEU S 71 ALA S 75 5 5
HELIX 72 AH9 ALA T 12 GLY T 47 1 36
HELIX 73 AI1 ALA T 49 SER T 70 1 22
HELIX 74 AI2 ASN T 75 GLU T 93 1 19
HELIX 75 AI3 THR V 8 GLY V 16 1 9
HELIX 76 AI4 SER W 37 HIS W 43 1 7
HELIX 77 AI5 THR X 31 ASP X 42 1 12
HELIX 78 AI6 ASP X 61 LYS X 79 1 19
HELIX 79 AI7 ASP X 95 GLY X 113 1 19
HELIX 80 AI8 VAL X 127 LEU X 144 1 18
SHEET 1 AA1 2 ILE B 32 ARG B 36 0
SHEET 2 AA1 2 ILE B 39 ILE B 42 -1 O ILE B 39 N ARG B 36
SHEET 1 AA2 5 TYR B 92 VAL B 93 0
SHEET 2 AA2 5 ILE B 68 VAL B 71 1 N PHE B 70 O VAL B 93
SHEET 3 AA2 5 ALA B 161 VAL B 164 1 O PHE B 163 N LEU B 69
SHEET 4 AA2 5 VAL B 184 ALA B 186 1 O ILE B 185 N VAL B 164
SHEET 5 AA2 5 TYR B 199 ILE B 200 1 O TYR B 199 N ALA B 186
SHEET 1 AA3 3 LEU C 52 ARG C 59 0
SHEET 2 AA3 3 VAL C 64 VAL C 70 -1 O ALA C 65 N GLU C 58
SHEET 3 AA3 3 ASN C 102 GLU C 105 1 O GLN C 104 N VAL C 68
SHEET 1 AA4 4 ALA C 169 GLY C 171 0
SHEET 2 AA4 4 GLY C 148 VAL C 153 -1 N ALA C 149 O GLN C 170
SHEET 3 AA4 4 GLY C 194 PHE C 203 -1 O LYS C 199 N ILE C 152
SHEET 4 AA4 4 ILE C 182 THR C 191 -1 N ASP C 183 O ILE C 202
SHEET 1 AA5 3 ARG D 131 ARG D 132 0
SHEET 2 AA5 3 ILE D 126 VAL D 128 -1 N VAL D 128 O ARG D 131
SHEET 3 AA5 3 ILE D 146 VAL D 148 -1 O ALA D 147 N THR D 127
SHEET 1 AA6 2 LEU D 174 ASP D 177 0
SHEET 2 AA6 2 LYS D 182 PHE D 185 -1 O LYS D 184 N SER D 175
SHEET 1 AA7 4 GLU E 7 ARG E 14 0
SHEET 2 AA7 4 GLY E 29 GLY E 35 -1 O VAL E 33 N LYS E 9
SHEET 3 AA7 4 ARG E 40 LYS E 47 -1 O GLY E 44 N VAL E 32
SHEET 4 AA7 4 MET E 66 GLU E 68 -1 O VAL E 67 N VAL E 41
SHEET 1 AA8 2 ARG E 18 MET E 19 0
SHEET 2 AA8 2 ARG E 24 ARG E 25 -1 O ARG E 25 N ARG E 18
SHEET 1 AA9 4 ILE E 80 PHE E 84 0
SHEET 2 AA9 4 SER E 87 PRO E 93 -1 O LEU E 91 N ILE E 80
SHEET 3 AA9 4 ILE E 118 GLY E 124 -1 O LYS E 121 N VAL E 90
SHEET 4 AA9 4 VAL E 100 ILE E 101 1 N ILE E 101 O ILE E 118
SHEET 1 AB1 4 ARG F 36 ILE F 52 0
SHEET 2 AB1 4 ASP F 55 MET F 67 -1 O GLN F 64 N LYS F 39
SHEET 3 AB1 4 ARG F 2 LEU F 10 -1 N TYR F 4 O VAL F 65
SHEET 4 AB1 4 VAL F 85 LYS F 92 -1 O VAL F 91 N GLU F 5
SHEET 1 AB2 2 LEU F 98 ALA F 99 0
SHEET 2 AB2 2 PHE R 29 ASP R 30 -1 O PHE R 29 N ALA F 99
SHEET 1 AB3 2 MET G 73 ARG G 79 0
SHEET 2 AB3 2 ASN G 84 GLU G 90 -1 O VAL G 87 N ARG G 76
SHEET 1 AB4 3 SER H 23 PRO H 27 0
SHEET 2 AB4 3 PRO H 57 TYR H 62 -1 O LEU H 59 N VAL H 26
SHEET 3 AB4 3 GLY H 47 ASP H 52 -1 N GLY H 47 O TYR H 62
SHEET 1 AB5 3 HIS H 82 ARG H 85 0
SHEET 2 AB5 3 GLY H 131 TRP H 138 -1 O TRP H 138 N HIS H 82
SHEET 3 AB5 3 TYR H 94 VAL H 95 -1 N VAL H 95 O GLY H 131
SHEET 1 AB6 4 HIS H 82 ARG H 85 0
SHEET 2 AB6 4 GLY H 131 TRP H 138 -1 O TRP H 138 N HIS H 82
SHEET 3 AB6 4 ILE H 109 THR H 114 -1 N ILE H 109 O VAL H 137
SHEET 4 AB6 4 GLY H 117 THR H 120 -1 O LEU H 119 N LEU H 112
SHEET 1 AB7 4 TYR I 4 ARG I 10 0
SHEET 2 AB7 4 ALA I 13 PRO I 21 -1 O ALA I 15 N GLY I 8
SHEET 3 AB7 4 PHE I 59 ARG I 66 -1 O ARG I 66 N VAL I 14
SHEET 4 AB7 4 VAL I 26 VAL I 28 1 N THR I 27 O ILE I 63
SHEET 1 AB8 3 HIS J 68 ILE J 74 0
SHEET 2 AB8 3 ILE J 4 GLY J 10 -1 N LEU J 8 O ARG J 70
SHEET 3 AB8 3 VAL J 94 LYS J 99 -1 O LYS J 99 N ARG J 5
SHEET 1 AB9 3 PHE J 47 ILE J 50 0
SHEET 2 AB9 3 ARG J 60 GLU J 64 -1 O PHE J 63 N PHE J 47
SHEET 3 AB9 3 ARG N 57 LYS N 58 -1 O ARG N 57 N GLU J 64
SHEET 1 AC1 6 PRO K 39 SER K 44 0
SHEET 2 AC1 6 THR K 28 THR K 33 -1 N VAL K 30 O SER K 43
SHEET 3 AC1 6 SER K 16 ALA K 23 -1 N HIS K 22 O ILE K 29
SHEET 4 AC1 6 SER K 79 ARG K 85 1 O ILE K 83 N ILE K 21
SHEET 5 AC1 6 GLN K 104 ASP K 110 1 O VAL K 109 N VAL K 82
SHEET 6 AC1 6 LEU R 85 VAL R 86 -1 O LEU R 85 N ASP K 110
SHEET 1 AC2 5 VAL L 82 ILE L 85 0
SHEET 2 AC2 5 ARG L 33 VAL L 43 -1 N GLY L 35 O VAL L 83
SHEET 3 AC2 5 ARG L 53 LEU L 60 -1 O ARG L 59 N VAL L 36
SHEET 4 AC2 5 GLU L 65 TYR L 69 -1 O ALA L 68 N ALA L 56
SHEET 5 AC2 5 VAL L 96 HIS L 99 1 O TYR L 98 N TYR L 69
SHEET 1 AC3 2 VAL N 33 TYR N 34 0
SHEET 2 AC3 2 LEU N 39 CYS N 40 -1 O LEU N 39 N TYR N 34
SHEET 1 AC4 5 LEU P 49 VAL P 51 0
SHEET 2 AC4 5 GLU P 34 TYR P 39 -1 N TYR P 38 O LYS P 50
SHEET 3 AC4 5 TYR P 17 ASP P 23 -1 N TYR P 17 O TYR P 39
SHEET 4 AC4 5 VAL P 2 ARG P 5 -1 N LYS P 3 O THR P 22
SHEET 5 AC4 5 GLN P 65 PRO P 66 1 O GLN P 65 N VAL P 2
SHEET 1 AC5 6 VAL Q 5 MET Q 15 0
SHEET 2 AC5 6 THR Q 18 PRO Q 28 -1 O THR Q 20 N VAL Q 11
SHEET 3 AC5 6 VAL Q 35 HIS Q 45 -1 O ARG Q 38 N ARG Q 25
SHEET 4 AC5 6 LYS Q 69 GLU Q 78 1 O PHE Q 71 N HIS Q 45
SHEET 5 AC5 6 VAL Q 56 SER Q 66 -1 N VAL Q 56 O VAL Q 77
SHEET 6 AC5 6 VAL Q 5 MET Q 15 -1 N LEU Q 6 O ILE Q 59
SHEET 1 AC6 3 ILE S 31 THR S 33 0
SHEET 2 AC6 3 THR S 48 TYR S 52 1 O ALA S 50 N THR S 33
SHEET 3 AC6 3 HIS S 57 TYR S 61 -1 O VAL S 58 N VAL S 51
SHEET 1 AC7 6 ILE W 7 LEU W 17 0
SHEET 2 AC7 6 THR W 21 LEU W 26 -1 O LYS W 25 N VAL W 12
SHEET 3 AC7 6 LEU W 33 ILE W 36 -1 O ALA W 34 N PHE W 22
SHEET 4 AC7 6 ARG W 64 TYR W 69 1 O GLY W 65 N LEU W 33
SHEET 5 AC7 6 ARG W 52 ILE W 57 -1 N VAL W 54 O VAL W 68
SHEET 6 AC7 6 ILE W 7 LEU W 17 -1 N THR W 9 O VAL W 55
SHEET 1 AC8 4 GLN X 25 ASP X 30 0
SHEET 2 AC8 4 GLN X 15 VAL X 19 -1 N VAL X 18 O GLY X 27
SHEET 3 AC8 4 VAL X 56 MET X 60 1 O ALA X 57 N ARG X 17
SHEET 4 AC8 4 ASP X 44 GLY X 49 -1 N ASP X 44 O MET X 60
SHEET 1 AC9 4 VAL X 85 PHE X 90 0
SHEET 2 AC9 4 LYS X 115 MET X 121 1 O LYS X 115 N LYS X 86
SHEET 3 AC9 4 ASP X 160 PRO X 167 -1 O LEU X 165 N VAL X 116
SHEET 4 AC9 4 ALA X 148 MET X 156 -1 N VAL X 149 O ALA X 166
SSBOND 1 CYS D 26 CYS D 31 1555 1555 2.89
LINK OP2 U A1257 NZ LYS C 27 1555 1555 1.43
LINK SG CYS D 9 ZN ZN D 300 1555 1555 2.44
LINK SG CYS N 24 ZN ZN N 101 1555 1555 2.64
LINK SG CYS N 27 ZN ZN N 101 1555 1555 2.33
LINK SG CYS N 40 ZN ZN N 101 1555 1555 2.08
LINK SG CYS N 43 ZN ZN N 101 1555 1555 2.49
LINK O3' G Z 7 P 4SU Z 8 1555 1555 1.62
LINK O3' 4SU Z 8 P G Z 9 1555 1555 1.62
LINK O3' G Z 31 P OMC Z 32 1555 1555 1.60
LINK O3' OMC Z 32 P U Z 33 1555 1555 1.61
LINK O3' G Z 45 P G7M Z 46 1555 1555 1.61
LINK O3' G7M Z 46 P U Z 47 1555 1555 1.61
LINK O3' G Z 53 P 5MU Z 54 1555 1555 1.61
LINK O3' 5MU Z 54 P PSU Z 55 1555 1555 1.62
LINK O3' PSU Z 55 P C Z 56 1555 1555 1.62
SITE 1 AC1 4 CYS D 9 LEU D 19 CYS D 26 CYS D 31
SITE 1 AC2 4 CYS N 24 CYS N 27 CYS N 40 CYS N 43
SITE 1 AC3 1 THR W 6
SITE 1 AC4 6 G Z 18 G Z 53 C Z 56 A Z 57
SITE 2 AC4 6 A Z 58 C Z 61
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
(ATOM LINES ARE NOT SHOWN.)
END