HEADER RIBOSOME/ANTIBIOTIC 04-FEB-14 4OX9
TITLE CRYSTAL STRUCTURE OF THE AMINOGLYCOSIDE RESISTANCE METHYLTRANSFERASE
TITLE 2 NPMA BOUND TO THE 30S RIBOSOMAL SUBUNIT
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: 16S RRNA (ADENINE(1408)-N(1))-METHYLTRANSFERASE;
COMPND 68 CHAIN: Y;
COMPND 69 SYNONYM: 16S RRNA M1A1408 METHYLTRANSFERASE;
COMPND 70 EC: 2.1.1.180;
COMPND 71 ENGINEERED: YES
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: 300852;
SOURCE 7 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 8 MOL_ID: 3;
SOURCE 9 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 10 ORGANISM_TAXID: 300852;
SOURCE 11 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 12 MOL_ID: 4;
SOURCE 13 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 14 ORGANISM_TAXID: 300852;
SOURCE 15 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 16 MOL_ID: 5;
SOURCE 17 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 18 ORGANISM_TAXID: 300852;
SOURCE 19 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 20 MOL_ID: 6;
SOURCE 21 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 22 ORGANISM_TAXID: 300852;
SOURCE 23 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 24 MOL_ID: 7;
SOURCE 25 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 26 ORGANISM_TAXID: 300852;
SOURCE 27 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 28 MOL_ID: 8;
SOURCE 29 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 30 ORGANISM_TAXID: 300852;
SOURCE 31 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 32 MOL_ID: 9;
SOURCE 33 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 34 ORGANISM_TAXID: 300852;
SOURCE 35 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 36 MOL_ID: 10;
SOURCE 37 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 38 ORGANISM_TAXID: 300852;
SOURCE 39 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 40 MOL_ID: 11;
SOURCE 41 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 42 ORGANISM_TAXID: 300852;
SOURCE 43 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 44 MOL_ID: 12;
SOURCE 45 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 46 ORGANISM_TAXID: 300852;
SOURCE 47 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 48 MOL_ID: 13;
SOURCE 49 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 50 ORGANISM_TAXID: 300852;
SOURCE 51 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 52 MOL_ID: 14;
SOURCE 53 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 54 ORGANISM_TAXID: 300852;
SOURCE 55 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 56 MOL_ID: 15;
SOURCE 57 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 58 ORGANISM_TAXID: 300852;
SOURCE 59 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 60 MOL_ID: 16;
SOURCE 61 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 62 ORGANISM_TAXID: 300852;
SOURCE 63 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 64 MOL_ID: 17;
SOURCE 65 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 66 ORGANISM_TAXID: 300852;
SOURCE 67 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 68 MOL_ID: 18;
SOURCE 69 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 70 ORGANISM_TAXID: 300852;
SOURCE 71 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 72 MOL_ID: 19;
SOURCE 73 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 74 ORGANISM_TAXID: 300852;
SOURCE 75 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 76 MOL_ID: 20;
SOURCE 77 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 78 ORGANISM_TAXID: 300852;
SOURCE 79 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 80 MOL_ID: 21;
SOURCE 81 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 82 ORGANISM_TAXID: 300852;
SOURCE 83 STRAIN: HB8 / ATCC 27634 / DSM 579;
SOURCE 84 MOL_ID: 22;
SOURCE 85 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 86 ORGANISM_TAXID: 562;
SOURCE 87 GENE: NPMA;
SOURCE 88 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 89 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN BIOSYNTHESIS, RIBOSOME, RNA, 30S, 16S, RIBOSOMAL SUBUNIT,
KEYWDS 2 AMINOGLYCOSIDE, A1408, METHYLTRANSFERASE, RIBOSOME-ANTIBIOTIC
KEYWDS 3 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.A.DUNKLE,G.L.CONN,C.M.DUNHAM
REVDAT 6 27-SEP-23 4OX9 1 REMARK LINK
REVDAT 5 30-SEP-15 4OX9 1 REMARK
REVDAT 4 01-OCT-14 4OX9 1 JRNL
REVDAT 3 21-MAY-14 4OX9 1 REMARK
REVDAT 2 30-APR-14 4OX9 1 JRNL
REVDAT 1 09-APR-14 4OX9 0
JRNL AUTH J.A.DUNKLE,K.VINAL,P.M.DESAI,N.ZELINSKAYA,M.SAVIC,D.M.WEST,
JRNL AUTH 2 G.L.CONN,C.M.DUNHAM
JRNL TITL MOLECULAR RECOGNITION AND MODIFICATION OF THE 30S RIBOSOME
JRNL TITL 2 BY THE AMINOGLYCOSIDE-RESISTANCE METHYLTRANSFERASE NPMA.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 111 6275 2014
JRNL REFN ESSN 1091-6490
JRNL PMID 24717845
JRNL DOI 10.1073/PNAS.1402789111
REMARK 2
REMARK 2 RESOLUTION. 3.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 141742
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 7034
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 49.7188 - 11.7676 0.99 4755 268 0.2366 0.2517
REMARK 3 2 11.7676 - 9.3606 1.00 4642 235 0.2118 0.2065
REMARK 3 3 9.3606 - 8.1833 1.00 4564 261 0.2157 0.2353
REMARK 3 4 8.1833 - 7.4378 1.00 4571 217 0.2034 0.2487
REMARK 3 5 7.4378 - 6.9062 1.00 4546 254 0.2025 0.2276
REMARK 3 6 6.9062 - 6.5000 1.00 4517 238 0.2032 0.2374
REMARK 3 7 6.5000 - 6.1751 1.00 4540 226 0.2168 0.2451
REMARK 3 8 6.1751 - 5.9067 1.00 4514 216 0.2100 0.2613
REMARK 3 9 5.9067 - 5.6797 1.00 4511 243 0.2095 0.2433
REMARK 3 10 5.6797 - 5.4839 1.00 4513 232 0.2183 0.2568
REMARK 3 11 5.4839 - 5.3126 0.99 4470 226 0.2175 0.2549
REMARK 3 12 5.3126 - 5.1609 1.00 4496 230 0.2207 0.2448
REMARK 3 13 5.1609 - 5.0252 1.00 4507 221 0.2254 0.2344
REMARK 3 14 5.0252 - 4.9027 1.00 4454 247 0.2309 0.2640
REMARK 3 15 4.9027 - 4.7914 1.00 4505 223 0.2351 0.2759
REMARK 3 16 4.7914 - 4.6895 1.00 4481 218 0.2418 0.2413
REMARK 3 17 4.6895 - 4.5957 1.00 4483 225 0.2399 0.2570
REMARK 3 18 4.5957 - 4.5091 1.00 4489 225 0.2429 0.2698
REMARK 3 19 4.5091 - 4.4286 1.00 4433 258 0.2454 0.2674
REMARK 3 20 4.4286 - 4.3536 1.00 4452 259 0.2553 0.2858
REMARK 3 21 4.3536 - 4.2834 1.00 4466 241 0.2569 0.3038
REMARK 3 22 4.2834 - 4.2175 1.00 4453 223 0.2638 0.2932
REMARK 3 23 4.2175 - 4.1555 1.00 4474 221 0.2738 0.3105
REMARK 3 24 4.1555 - 4.0970 1.00 4459 243 0.2812 0.3263
REMARK 3 25 4.0970 - 4.0417 1.00 4408 258 0.3014 0.3225
REMARK 3 26 4.0417 - 3.9892 1.00 4455 261 0.2959 0.3105
REMARK 3 27 3.9892 - 3.9394 1.00 4459 200 0.2941 0.3300
REMARK 3 28 3.9394 - 3.8919 0.99 4397 250 0.3257 0.3308
REMARK 3 29 3.8919 - 3.8467 1.00 4431 222 0.3138 0.3182
REMARK 3 30 3.8467 - 3.8035 0.95 4263 193 0.3208 0.3165
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.450
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.090
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 80.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 57747
REMARK 3 ANGLE : 1.292 85452
REMARK 3 CHIRALITY : 0.106 10693
REMARK 3 PLANARITY : 0.015 5212
REMARK 3 DIHEDRAL : 17.371 26595
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4OX9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-14.
REMARK 100 THE DEPOSITION ID IS D_1000200141.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-JUN-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 142385
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 8.890
REMARK 200 R MERGE (I) : 0.12000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.2200
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 1.43800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.430
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1J5E
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.98
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.55
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% MPD, 0.2 M KCL , 75 MM NH4CL, 15
REMARK 280 MM MGCL2 , 0.1M MES, PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K. 14% MPD, 0.2 M KCL , 75 MM NH4CL, 15 MM MGCL2 ,
REMARK 280 0.1M MES, PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
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 88.30500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 201.76000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 201.76000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 44.15250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 201.76000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 201.76000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 132.45750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 201.76000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 201.76000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 44.15250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 201.76000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 201.76000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 132.45750
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 88.30500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 22-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 91910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 286050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -768.0 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, Y
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 1535
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 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 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 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 MET M 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 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 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 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 LYS V 26
REMARK 465 LYS V 27
REMARK 465 MET Y -2
REMARK 465 GLY Y -1
REMARK 465 SER Y 0
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG J 79 CB CG CD NE CZ NH1 NH2
REMARK 470 THR J 100 OG1 CG2
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 35 O SER L 118 1.88
REMARK 500 O LEU L 27 N GLY L 29 1.94
REMARK 500 O4 U A 652 O2' G A 752 2.09
REMARK 500 OP1 G A 254 O LYS Q 67 2.10
REMARK 500 O2' G A 1405 O2' A A 1518 2.13
REMARK 500 OP1 G A 521 O GLU L 73 2.13
REMARK 500 O2' G A 1405 O4' A A 1519 2.13
REMARK 500 N1 G A 942 O2 U A 1341 2.13
REMARK 500 OP1 C A 19 OG SER E 125 2.19
REMARK 500 OG1 THR Y 109 N6 SFG Y 301 2.19
REMARK 500 O TYR Q 95 N SER Q 97 2.19
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 669 O3' G A 670 P 0.072
REMARK 500 VAL E 69 C PRO E 70 N 0.214
REMARK 500 ILE E 101 C ALA E 102 N 0.244
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 C2' - C3' - O3' ANGL. DEV. = 10.2 DEGREES
REMARK 500 A A 60 C2' - C3' - O3' ANGL. DEV. = 12.4 DEGREES
REMARK 500 G A 115 C2' - C3' - O3' ANGL. DEV. = 10.3 DEGREES
REMARK 500 G A 115 N9 - C1' - C2' ANGL. DEV. = 9.0 DEGREES
REMARK 500 A A 197 N9 - C1' - C2' ANGL. DEV. = 10.2 DEGREES
REMARK 500 A A 243 C2' - C3' - O3' ANGL. DEV. = 16.6 DEGREES
REMARK 500 G A 266 C2' - C3' - O3' ANGL. DEV. = 12.4 DEGREES
REMARK 500 C A 366 C2' - C3' - O3' ANGL. DEV. = 13.1 DEGREES
REMARK 500 C A 372 C2' - C3' - O3' ANGL. DEV. = 10.2 DEGREES
REMARK 500 A A 460 N9 - C1' - C2' ANGL. DEV. = 8.0 DEGREES
REMARK 500 A A 509 C2' - C3' - O3' ANGL. DEV. = 10.1 DEGREES
REMARK 500 A A 559 C2' - C3' - O3' ANGL. DEV. = 15.9 DEGREES
REMARK 500 G A 575 C2' - C3' - O3' ANGL. DEV. = 12.8 DEGREES
REMARK 500 U A 603 C3' - O3' - P ANGL. DEV. = 7.4 DEGREES
REMARK 500 A A 687 C2' - C3' - O3' ANGL. DEV. = 12.8 DEGREES
REMARK 500 A A 792 C2' - C3' - O3' ANGL. DEV. = 11.6 DEGREES
REMARK 500 A A1067 C2' - C3' - O3' ANGL. DEV. = 10.6 DEGREES
REMARK 500 A A1299 N9 - C1' - C2' ANGL. DEV. = 11.2 DEGREES
REMARK 500 G A1405 C3' - O3' - P ANGL. DEV. = -11.5 DEGREES
REMARK 500 U A1406 O5' - P - OP2 ANGL. DEV. = -10.3 DEGREES
REMARK 500 C A1409 C6 - N1 - C2 ANGL. DEV. = -2.8 DEGREES
REMARK 500 G A1410 N3 - C4 - C5 ANGL. DEV. = -4.2 DEGREES
REMARK 500 G A1410 C4 - C5 - C6 ANGL. DEV. = 3.9 DEGREES
REMARK 500 G A1410 C8 - N9 - C4 ANGL. DEV. = -2.4 DEGREES
REMARK 500 G A1410 N3 - C4 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 G A1410 C6 - C5 - N7 ANGL. DEV. = -4.7 DEGREES
REMARK 500 G A1410 C4 - N9 - C1' ANGL. DEV. = 10.2 DEGREES
REMARK 500 C A1411 O3' - P - OP2 ANGL. DEV. = 8.6 DEGREES
REMARK 500 U A1498 C2' - C3' - O3' ANGL. DEV. = 17.6 DEGREES
REMARK 500 A A1502 N9 - C1' - C2' ANGL. DEV. = 8.6 DEGREES
REMARK 500 G A1505 C2' - C3' - O3' ANGL. DEV. = 10.8 DEGREES
REMARK 500 CYS D 12 CA - CB - SG ANGL. DEV. = 8.3 DEGREES
REMARK 500 GLY S 54 N - CA - C ANGL. DEV. = -15.1 DEGREES
REMARK 500 LEU Y 155 CA - CB - CG ANGL. DEV. = 16.6 DEGREES
REMARK 500 LEU Y 155 N - CA - C ANGL. DEV. = 16.9 DEGREES
REMARK 500 PRO Y 156 C - N - CA ANGL. DEV. = 17.0 DEGREES
REMARK 500 PRO Y 156 C - N - CD ANGL. DEV. = -14.8 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 -138.91 177.19
REMARK 500 GLU B 9 162.16 112.80
REMARK 500 LEU B 10 -49.69 -144.91
REMARK 500 LEU B 11 46.76 -72.84
REMARK 500 VAL B 15 -81.11 -157.76
REMARK 500 HIS B 16 -99.79 -41.12
REMARK 500 PHE B 17 -158.86 34.36
REMARK 500 GLU B 20 126.67 59.62
REMARK 500 ARG B 21 -95.62 -56.01
REMARK 500 LYS B 22 92.16 -167.12
REMARK 500 ARG B 23 -2.03 -161.15
REMARK 500 TRP B 24 -142.93 2.35
REMARK 500 PRO B 26 -31.09 -29.42
REMARK 500 ALA B 34 169.05 169.74
REMARK 500 ASP B 60 -77.83 -30.39
REMARK 500 ALA B 62 -72.19 -56.96
REMARK 500 LYS B 74 148.40 -39.63
REMARK 500 MET B 83 -78.48 -45.68
REMARK 500 GLN B 95 -91.28 -82.96
REMARK 500 TRP B 97 92.14 -57.14
REMARK 500 ILE B 108 -6.50 -59.62
REMARK 500 PHE B 122 42.23 -95.41
REMARK 500 ALA B 123 13.21 -176.82
REMARK 500 SER B 124 -164.38 -115.68
REMARK 500 GLU B 126 2.70 -57.33
REMARK 500 ILE B 127 -73.68 -48.88
REMARK 500 ARG B 130 156.51 69.06
REMARK 500 GLN B 135 2.13 -63.70
REMARK 500 LEU B 155 105.25 -37.11
REMARK 500 ALA B 161 177.65 179.72
REMARK 500 VAL B 165 -95.46 -85.31
REMARK 500 GLU B 170 33.69 -94.19
REMARK 500 PRO B 183 150.52 -44.98
REMARK 500 ASP B 189 -157.60 -111.05
REMARK 500 ASN B 204 101.80 -34.20
REMARK 500 ALA B 207 114.44 73.14
REMARK 500 LEU B 213 -72.60 -57.09
REMARK 500 VAL B 229 55.33 34.91
REMARK 500 PRO B 232 153.85 -30.31
REMARK 500 ASN C 3 -159.14 -121.67
REMARK 500 LYS C 4 127.41 52.45
REMARK 500 LEU C 12 -38.11 -37.70
REMARK 500 ILE C 14 -161.02 -125.22
REMARK 500 THR C 15 53.29 2.76
REMARK 500 ARG C 16 115.89 157.79
REMARK 500 ALA C 24 -175.20 170.90
REMARK 500 LYS C 26 -81.84 28.13
REMARK 500 TYR C 29 -54.18 -18.97
REMARK 500 ILE C 39 -75.77 -52.73
REMARK 500 GLU C 46 -79.56 -102.07
REMARK 500
REMARK 500 THIS ENTRY HAS 324 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 GLU Y 147 ALA Y 148 -30.96
REMARK 500 LEU Y 157 LEU Y 158 -38.85
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 12 0.07 SIDE CHAIN
REMARK 500 A A 197 0.11 SIDE CHAIN
REMARK 500 U A 203 0.09 SIDE CHAIN
REMARK 500 G A 220 0.05 SIDE CHAIN
REMARK 500 G A 231 0.05 SIDE CHAIN
REMARK 500 U A 249 0.06 SIDE CHAIN
REMARK 500 A A 250 0.06 SIDE CHAIN
REMARK 500 G A 251 0.07 SIDE CHAIN
REMARK 500 G A 254 0.06 SIDE CHAIN
REMARK 500 G A 266 0.06 SIDE CHAIN
REMARK 500 A A 274 0.06 SIDE CHAIN
REMARK 500 C A 290 0.07 SIDE CHAIN
REMARK 500 G A 297 0.06 SIDE CHAIN
REMARK 500 G A 305 0.05 SIDE CHAIN
REMARK 500 G A 380 0.07 SIDE CHAIN
REMARK 500 G A 413 0.05 SIDE CHAIN
REMARK 500 G A 481 0.07 SIDE CHAIN
REMARK 500 A A 573 0.06 SIDE CHAIN
REMARK 500 G A 575 0.06 SIDE CHAIN
REMARK 500 U A 603 0.07 SIDE CHAIN
REMARK 500 G A 727 0.07 SIDE CHAIN
REMARK 500 C A 879 0.07 SIDE CHAIN
REMARK 500 G A 898 0.07 SIDE CHAIN
REMARK 500 U A 982 0.07 SIDE CHAIN
REMARK 500 G A1048 0.06 SIDE CHAIN
REMARK 500 U A1073 0.07 SIDE CHAIN
REMARK 500 G A1079 0.06 SIDE CHAIN
REMARK 500 U A1085 0.09 SIDE CHAIN
REMARK 500 A A1092 0.06 SIDE CHAIN
REMARK 500 A A1130 0.05 SIDE CHAIN
REMARK 500 G A1139 0.05 SIDE CHAIN
REMARK 500 U A1281 0.10 SIDE CHAIN
REMARK 500 A A1289 0.06 SIDE CHAIN
REMARK 500 G A1293 0.05 SIDE CHAIN
REMARK 500 A A1299 0.06 SIDE CHAIN
REMARK 500 U A1301 0.08 SIDE CHAIN
REMARK 500 G A1305 0.05 SIDE CHAIN
REMARK 500 A A1340 0.05 SIDE CHAIN
REMARK 500 A A1360 0.05 SIDE CHAIN
REMARK 500 U A1506 0.07 SIDE CHAIN
REMARK 500 G A1525 0.05 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 A1609 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 11 O6
REMARK 620 2 U A 12 O4 74.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1613 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U A 14 O4
REMARK 620 2 U A 17 OP2 78.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1638 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 48 OP2
REMARK 620 2 G A 115 OP1 136.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1608 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 58 O3'
REMARK 620 2 A A 59 OP1 54.8
REMARK 620 3 U A 387 OP1 125.6 78.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1701 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 116 OP2
REMARK 620 2 G A 117 OP2 94.7
REMARK 620 3 G A 289 OP2 80.3 152.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1601 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 258 O6
REMARK 620 2 G A 266 OP2 101.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1670 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 299 O6
REMARK 620 2 G A 558 OP1 125.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1704 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 372 O2
REMARK 620 2 G A 376 O6 102.2
REMARK 620 3 U A 387 O4 69.7 82.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1633 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 509 OP2
REMARK 620 2 A A 509 O3' 67.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1672 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U A 516 O4
REMARK 620 2 A A 533 OP1 111.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1673 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 572 OP2
REMARK 620 2 A A 573 OP2 89.7
REMARK 620 3 A A 574 OP2 165.2 82.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1607 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 592 O6
REMARK 620 2 G A 593 O6 92.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1639 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 596 OP2
REMARK 620 2 G A 597 OP2 68.6
REMARK 620 3 U A 598 O4 151.3 93.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1655 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 635 O6
REMARK 620 2 U A 636 O4 73.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1610 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 665 O3'
REMARK 620 2 G A 666 OP1 64.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1600 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 703 O6
REMARK 620 2 C A1452 O2' 42.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1622 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 749 OP2
REMARK 620 2 G A 750 OP2 76.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1710 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 782 OP1
REMARK 620 2 A A 794 OP1 167.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1659 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 944 OP1
REMARK 620 2 G A 945 OP2 89.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1660 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 964 OP1
REMARK 620 2 U A1199 OP1 85.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1661 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 980 OP2
REMARK 620 2 U A 981 O4 77.9
REMARK 620 3 U A 982 O2 147.3 82.7
REMARK 620 4 G A1222 O6 133.0 76.5 65.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1663 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A1054 OP1
REMARK 620 2 C A1054 OP2 59.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1664 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A1054 O5'
REMARK 620 2 U A1196 O3' 115.1
REMARK 620 3 G A1197 OP1 91.5 57.4
REMARK 620 4 G A1198 OP2 108.9 102.1 60.9
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1681 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A1067 O3'
REMARK 620 2 G A1068 OP1 60.6
REMARK 620 3 G A1094 OP1 79.5 113.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1682 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U A1095 OP2
REMARK 620 2 G A1108 O6 75.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1691 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A1499 OP2
REMARK 620 2 A A1500 OP2 98.2
REMARK 620 3 G A1505 OP2 150.5 98.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 301 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 166 OD1
REMARK 620 2 ASP B 166 OD2 50.7
REMARK 620 3 ASP B 205 OD2 58.0 93.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 301 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 9 SG
REMARK 620 2 CYS D 12 SG 111.9
REMARK 620 3 CYS D 26 SG 126.6 112.4
REMARK 620 4 CYS D 31 SG 131.6 82.6 82.4
REMARK 620 N 1 2 3
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 98.6
REMARK 620 3 CYS N 40 SG 108.5 103.2
REMARK 620 4 CYS N 43 SG 125.1 120.0 99.5
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 MG A 1600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1603
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1606
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1607
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1608
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1609
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1610
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1611
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1613
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1614
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1615
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1616
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1617
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1629
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1631
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1632
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1633
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1634
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1636
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1637
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1638
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1639
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1640
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1641
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1642
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1643
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1644
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1645
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1646
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1647
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1648
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1651
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1655
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1657
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1659
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1660
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1663
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1664
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1665
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1667
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1668
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1669
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1670
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1674
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1675
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1676
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1677
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1678
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1679
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1680
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1682
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1683
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1685
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1686
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1689
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1691
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1692
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1695
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1696
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1697
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1698
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1699
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1706
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1707
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1710
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1712
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1713
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1715
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1716
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN N 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG N 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SFG Y 301
DBREF 4OX9 A 0 1535 GB 155076 M26923.1 646 2158
DBREF 4OX9 B 1 256 UNP P80371 RS2_THET8 1 256
DBREF 4OX9 C 1 239 UNP P80372 RS3_THET8 1 239
DBREF 4OX9 D 2 209 UNP P80373 RS4_THET8 2 209
DBREF 4OX9 E 2 162 UNP Q5SHQ5 RS5_THET8 2 162
DBREF 4OX9 F 1 101 UNP Q5SLP8 RS6_THET8 1 101
DBREF 4OX9 G 2 156 UNP P17291 RS7_THET8 2 156
DBREF 4OX9 H 1 138 UNP Q5SHQ2 RS8_THET8 1 138
DBREF 4OX9 I 1 128 UNP P80374 RS9_THET8 1 128
DBREF 4OX9 J 2 105 UNP Q5SHN7 RS10_THET8 2 105
DBREF 4OX9 K 1 129 UNP P80376 RS11_THET8 1 129
DBREF 4OX9 L 4 134 UNP Q5SHN3 RS12_THET8 1 131
DBREF 4OX9 M 1 126 UNP P80377 RS13_THET8 1 126
DBREF 4OX9 N 2 61 UNP Q5SHQ1 RS14Z_THET8 2 61
DBREF 4OX9 O 2 89 UNP Q5SJ76 RS15_THET8 2 89
DBREF 4OX9 P 1 88 UNP Q5SJH3 RS16_THET8 1 88
DBREF 4OX9 Q 2 105 UNP Q5SHP7 RS17_THET8 2 105
DBREF 4OX9 R 1 88 UNP Q5SLQ0 RS18_THET8 1 88
DBREF 4OX9 S 2 93 UNP Q5SHP2 RS19_THET8 2 93
DBREF 4OX9 T 1 106 UNP P80380 RS20_THET8 1 106
DBREF 4OX9 V 2 27 UNP Q5SIH3 RSHX_THET8 2 27
DBREF 4OX9 Y 1 219 UNP A8C927 NPMA_ECOLX 1 219
SEQRES 1 A 1513 U U U G U U G G A G A G U
SEQRES 2 A 1513 U U G A U C C U G G C U C
SEQRES 3 A 1513 A G G G U G A A C G C U G
SEQRES 4 A 1513 G C G G C G U G C C U A A
SEQRES 5 A 1513 G A C A U G C A A G U C G
SEQRES 6 A 1513 U G C G G G C C G C G G G
SEQRES 7 A 1513 G U U U U A C U C C G U G
SEQRES 8 A 1513 G U C A G C G G C G G A C
SEQRES 9 A 1513 G G G U G A G U A A C G C
SEQRES 10 A 1513 G U G G G U G A C C U A C
SEQRES 11 A 1513 C C G G A A G A G G G G G
SEQRES 12 A 1513 A C A A C C C G G G G A A
SEQRES 13 A 1513 A C U C G G G C U A A U C
SEQRES 14 A 1513 C C C C A U G U G G A C C
SEQRES 15 A 1513 C G C C C C U U G G G G U
SEQRES 16 A 1513 G U G U C C A A A G G G C
SEQRES 17 A 1513 U U U G C C C G C U U C C
SEQRES 18 A 1513 G G A U G G G C C C G C G
SEQRES 19 A 1513 U C C C A U C A G C U A G
SEQRES 20 A 1513 U U G G U G G G G U A A U
SEQRES 21 A 1513 G G C C C A C C A A G G C
SEQRES 22 A 1513 G A C G A C G G G U A G C
SEQRES 23 A 1513 C G G U C U G A G A G G A
SEQRES 24 A 1513 U G G C C G G C C A C A G
SEQRES 25 A 1513 G G G C A C U G A G A C A
SEQRES 26 A 1513 C G G G C C C C A C U C C
SEQRES 27 A 1513 U A C G G G A G G C A G C
SEQRES 28 A 1513 A G U U A G G A A U C U U
SEQRES 29 A 1513 C C G C A A U G G G C G C
SEQRES 30 A 1513 A A G C C U G A C G G A G
SEQRES 31 A 1513 C G A C G C C G C U U G G
SEQRES 32 A 1513 A G G A A G A A G C C C U
SEQRES 33 A 1513 U C G G G G U G U A A A C
SEQRES 34 A 1513 U C C U G A A C C C G G G
SEQRES 35 A 1513 A C G A A A C C C C C G A
SEQRES 36 A 1513 C G A G G G G A C U G A C
SEQRES 37 A 1513 G G U A C C G G G G U A A
SEQRES 38 A 1513 U A G C G C C G G C C A A
SEQRES 39 A 1513 C U C C G U G C C A G C A
SEQRES 40 A 1513 G C C G C G G U A A U A C
SEQRES 41 A 1513 G G A G G G C G C G A G C
SEQRES 42 A 1513 G U U A C C C G G A U U C
SEQRES 43 A 1513 A C U G G G C G U A A A G
SEQRES 44 A 1513 G G C G U G U A G G C G G
SEQRES 45 A 1513 C C U G G G G C G U C C C
SEQRES 46 A 1513 A U G U G A A A G A C C A
SEQRES 47 A 1513 C G G C U C A A C C G U G
SEQRES 48 A 1513 G G G G A G C G U G G G A
SEQRES 49 A 1513 U A C G C U C A G G C U A
SEQRES 50 A 1513 G A C G G U G G G A G A G
SEQRES 51 A 1513 G G U G G U G G A A U U C
SEQRES 52 A 1513 C C G G A G U A G C G G U
SEQRES 53 A 1513 G A A A U G C G C A G A U
SEQRES 54 A 1513 A C C G G G A G G A A C G
SEQRES 55 A 1513 C C G A U G G C G A A G G
SEQRES 56 A 1513 C A G C C A C C U G G U C
SEQRES 57 A 1513 C A C C C G U G A C G C U
SEQRES 58 A 1513 G A G G C G C G A A A G C
SEQRES 59 A 1513 G U G G G G A G C A A A C
SEQRES 60 A 1513 C G G A U U A G A U A C C
SEQRES 61 A 1513 C G G G U A G U C C A C G
SEQRES 62 A 1513 C C C U A A A C G A U G C
SEQRES 63 A 1513 G C G C U A G G U C U C U
SEQRES 64 A 1513 G G G U C U C C U G G G G
SEQRES 65 A 1513 G C C G A A G C U A A C G
SEQRES 66 A 1513 C G U U A A G C G C G C C
SEQRES 67 A 1513 G C C U G G G G A G U A C
SEQRES 68 A 1513 G G C C G C A A G G C U G
SEQRES 69 A 1513 A A A C U C A A A G G A A
SEQRES 70 A 1513 U U G A C G G G G G C C C
SEQRES 71 A 1513 G C A C A A G C G G U G G
SEQRES 72 A 1513 A G C A U G U G G U U U A
SEQRES 73 A 1513 A U U C G A A G C A A C G
SEQRES 74 A 1513 C G A A G A A C C U U A C
SEQRES 75 A 1513 C A G G C C U U G A C A U
SEQRES 76 A 1513 G C U A G G G A A C C C G
SEQRES 77 A 1513 G G U G A A A G C C U G G
SEQRES 78 A 1513 G G U G C C C C G C G A G
SEQRES 79 A 1513 G G G A G C C C U A G C A
SEQRES 80 A 1513 C A G G U G C U G C A U G
SEQRES 81 A 1513 G C C G U C G U C A G C U
SEQRES 82 A 1513 C G U G C C G U G A G G U
SEQRES 83 A 1513 G U U G G G U U A A G U C
SEQRES 84 A 1513 C C G C A A C G A G C G C
SEQRES 85 A 1513 A A C C C C C G C C G U U
SEQRES 86 A 1513 A G U U G C C A G C G G U
SEQRES 87 A 1513 U C G G C C G G G C A C U
SEQRES 88 A 1513 C U A A C G G G A C U G C
SEQRES 89 A 1513 C C G C G A A A G C G G G
SEQRES 90 A 1513 A G G A A G G A G G G G A
SEQRES 91 A 1513 C G A C G U C U G G U C A
SEQRES 92 A 1513 G C A U G G C C C U U A C
SEQRES 93 A 1513 G G C C U G G G C G A C A
SEQRES 94 A 1513 C A C G U G C U A C A A U
SEQRES 95 A 1513 G C C C A C U A C A A A G
SEQRES 96 A 1513 C G A U G C C A C C C G G
SEQRES 97 A 1513 C A A C G G G G A G C U A
SEQRES 98 A 1513 A U C G C A A A A A G G U
SEQRES 99 A 1513 G G G C C C A G U U C G G
SEQRES 100 A 1513 A U U G G G G U C U G C A
SEQRES 101 A 1513 A C C C G A C C C C A U G
SEQRES 102 A 1513 A A G C C G G A A U C G C
SEQRES 103 A 1513 U A G U A A U C G C G G A
SEQRES 104 A 1513 U C A G C C A U G C C G C
SEQRES 105 A 1513 G G U G A A U A C G U U C
SEQRES 106 A 1513 C C G G G C C U U G U A C
SEQRES 107 A 1513 A C A C C G C C C G U C A
SEQRES 108 A 1513 C G C C A U G G G A G C G
SEQRES 109 A 1513 G G C U C U A C C C G A A
SEQRES 110 A 1513 G U C G C C G G G A G C C
SEQRES 111 A 1513 U A C G G G C A G G C G C
SEQRES 112 A 1513 C G A G G G U A G G G C C
SEQRES 113 A 1513 C G U G A C U G G G G C G
SEQRES 114 A 1513 A A G U C G U A A C A A G
SEQRES 115 A 1513 G U A G C U G U A C C G G
SEQRES 116 A 1513 A A G G U G C G G C U G G
SEQRES 117 A 1513 A U C A C
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 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 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 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 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 131 MET PRO THR ILE ASN GLN LEU VAL ARG LYS GLY ARG GLU
SEQRES 2 L 131 LYS VAL ARG LYS LYS SER LYS VAL PRO ALA LEU LYS GLY
SEQRES 3 L 131 ALA PRO PHE ARG ARG GLY VAL CYS THR VAL VAL ARG THR
SEQRES 4 L 131 VAL THR PRO LYS LYS PRO ASN SER ALA LEU ARG LYS VAL
SEQRES 5 L 131 ALA LYS VAL ARG LEU THR SER GLY TYR GLU VAL THR ALA
SEQRES 6 L 131 TYR ILE PRO GLY GLU GLY HIS ASN LEU GLN GLU HIS SER
SEQRES 7 L 131 VAL VAL LEU ILE ARG GLY GLY ARG VAL LYS ASP LEU PRO
SEQRES 8 L 131 GLY VAL ARG TYR HIS ILE VAL ARG GLY VAL TYR ASP ALA
SEQRES 9 L 131 ALA GLY VAL LYS ASP ARG LYS LYS SER ARG SER LYS TYR
SEQRES 10 L 131 GLY THR LYS LYS PRO LYS GLU ALA ALA LYS THR ALA ALA
SEQRES 11 L 131 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 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 LYS TYR LYS LEU
SEQRES 5 Q 104 GLY ASP VAL VAL GLU ILE ILE GLU SER ARG PRO ILE SER
SEQRES 6 Q 104 LYS ARG LYS ARG PHE ARG VAL LEU ARG LEU VAL GLU SER
SEQRES 7 Q 104 GLY ARG MET ASP LEU VAL GLU LYS TYR LEU ILE ARG ARG
SEQRES 8 Q 104 GLN ASN TYR GLU SER LEU SER LYS ARG GLY GLY LYS 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 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 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 26 GLY LYS GLY ASP ARG ARG THR ARG ARG GLY LYS ILE TRP
SEQRES 2 V 26 ARG GLY THR TYR GLY LYS TYR ARG PRO ARG LYS LYS LYS
SEQRES 1 Y 222 MET GLY SER MET LEU ILE LEU LYS GLY THR LYS THR VAL
SEQRES 2 Y 222 ASP LEU SER LYS ASP GLU LEU THR GLU ILE ILE GLY GLN
SEQRES 3 Y 222 PHE ASP ARG VAL HIS ILE ASP LEU GLY THR GLY ASP GLY
SEQRES 4 Y 222 ARG ASN ILE TYR LYS LEU ALA ILE ASN ASP GLN ASN THR
SEQRES 5 Y 222 PHE TYR ILE GLY ILE ASP PRO VAL LYS GLU ASN LEU PHE
SEQRES 6 Y 222 ASP ILE SER LYS LYS ILE ILE LYS LYS PRO SER LYS GLY
SEQRES 7 Y 222 GLY LEU SER ASN VAL VAL PHE VAL ILE ALA ALA ALA GLU
SEQRES 8 Y 222 SER LEU PRO PHE GLU LEU LYS ASN ILE ALA ASP SER ILE
SEQRES 9 Y 222 SER ILE LEU PHE PRO TRP GLY THR LEU LEU GLU TYR VAL
SEQRES 10 Y 222 ILE LYS PRO ASN ARG ASP ILE LEU SER ASN VAL ALA ASP
SEQRES 11 Y 222 LEU ALA LYS LYS GLU ALA HIS PHE GLU PHE VAL THR THR
SEQRES 12 Y 222 TYR SER ASP SER TYR GLU GLU ALA GLU ILE LYS LYS ARG
SEQRES 13 Y 222 GLY LEU PRO LEU LEU SER LYS ALA TYR PHE LEU SER GLU
SEQRES 14 Y 222 GLN TYR LYS ALA GLU LEU SER ASN SER GLY PHE ARG ILE
SEQRES 15 Y 222 ASP ASP VAL LYS GLU LEU ASP ASN GLU TYR VAL LYS GLN
SEQRES 16 Y 222 PHE ASN SER LEU TRP ALA LYS ARG LEU ALA PHE GLY ARG
SEQRES 17 Y 222 LYS ARG SER PHE PHE ARG VAL SER GLY HIS VAL SER LYS
SEQRES 18 Y 222 HIS
HET MG A1600 1
HET MG A1601 1
HET MG A1602 1
HET MG A1603 1
HET MG A1604 1
HET MG A1605 1
HET MG A1606 1
HET MG A1607 1
HET MG A1608 1
HET MG A1609 1
HET MG A1610 1
HET MG A1611 1
HET MG A1612 1
HET MG A1613 1
HET MG A1614 1
HET MG A1615 1
HET MG A1616 1
HET MG A1617 1
HET MG A1618 1
HET MG A1619 1
HET MG A1620 1
HET MG A1621 1
HET MG A1622 1
HET MG A1623 1
HET MG A1624 1
HET MG A1625 1
HET MG A1626 1
HET MG A1627 1
HET MG A1628 1
HET MG A1629 1
HET MG A1630 1
HET MG A1631 1
HET MG A1632 1
HET MG A1633 1
HET MG A1634 1
HET MG A1635 1
HET MG A1636 1
HET MG A1637 1
HET MG A1638 1
HET MG A1639 1
HET MG A1640 1
HET MG A1641 1
HET MG A1642 1
HET MG A1643 1
HET MG A1644 1
HET MG A1645 1
HET MG A1646 1
HET MG A1647 1
HET MG A1648 1
HET MG A1649 1
HET MG A1650 1
HET MG A1651 1
HET MG A1652 1
HET MG A1653 1
HET MG A1654 1
HET MG A1655 1
HET MG A1656 1
HET MG A1657 1
HET MG A1658 1
HET MG A1659 1
HET MG A1660 1
HET MG A1661 1
HET MG A1662 1
HET MG A1663 1
HET MG A1664 1
HET MG A1665 1
HET MG A1666 1
HET MG A1667 1
HET MG A1668 1
HET MG A1669 1
HET MG A1670 1
HET MG A1671 1
HET MG A1672 1
HET MG A1673 1
HET MG A1674 1
HET MG A1675 1
HET MG A1676 1
HET MG A1677 1
HET MG A1678 1
HET MG A1679 1
HET MG A1680 1
HET MG A1681 1
HET MG A1682 1
HET MG A1683 1
HET MG A1684 1
HET MG A1685 1
HET MG A1686 1
HET MG A1687 1
HET MG A1688 1
HET MG A1689 1
HET MG A1690 1
HET MG A1691 1
HET MG A1692 1
HET MG A1693 1
HET MG A1694 1
HET MG A1695 1
HET MG A1696 1
HET MG A1697 1
HET MG A1698 1
HET MG A1699 1
HET MG A1700 1
HET MG A1701 1
HET MG A1702 1
HET MG A1703 1
HET MG A1704 1
HET MG A1705 1
HET MG A1706 1
HET MG A1707 1
HET MG A1708 1
HET MG A1709 1
HET MG A1710 1
HET MG A1711 1
HET MG A1712 1
HET MG A1713 1
HET MG A1714 1
HET MG A1715 1
HET MG A1716 1
HET MG B 301 1
HET ZN D 301 1
HET MG E 201 1
HET ZN N 101 1
HET MG N 102 1
HET SFG Y 301 27
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
HETNAM SFG SINEFUNGIN
HETSYN SFG ADENOSYL-ORNITHINE
FORMUL 23 MG 120(MG 2+)
FORMUL 41 ZN 2(ZN 2+)
FORMUL 45 SFG C15 H23 N7 O5
HELIX 1 AA1 LEU B 11 VAL B 15 5 5
HELIX 2 AA2 ASN B 25 ARG B 30 5 6
HELIX 3 AA3 ASP B 43 MET B 63 1 21
HELIX 4 AA4 LYS B 74 ARG B 87 1 14
HELIX 5 AA5 ASN B 104 PHE B 122 1 19
HELIX 6 AA6 ALA B 123 SER B 124 5 2
HELIX 7 AA7 PRO B 125 GLU B 129 5 5
HELIX 8 AA8 LYS B 133 LEU B 149 1 17
HELIX 9 AA9 GLU B 170 LEU B 180 1 11
HELIX 10 AB1 ASP B 193 VAL B 197 5 5
HELIX 11 AB2 ALA B 207 ALA B 225 1 19
HELIX 12 AB3 SER B 235 GLN B 240 5 6
HELIX 13 AB4 HIS C 6 LEU C 12 1 7
HELIX 14 AB5 GLN C 28 LEU C 47 1 20
HELIX 15 AB6 LYS C 72 GLY C 78 1 7
HELIX 16 AB7 GLU C 82 LYS C 93 1 12
HELIX 17 AB8 ASN C 108 LEU C 111 5 4
HELIX 18 AB9 SER C 112 ARG C 127 1 16
HELIX 19 AC1 ALA C 129 GLU C 143 1 15
HELIX 20 AC2 ARG C 156 ALA C 160 5 5
HELIX 21 AC3 VAL D 8 GLU D 15 1 8
HELIX 22 AC4 SER D 52 TYR D 68 1 17
HELIX 23 AC5 SER D 71 LYS D 85 1 15
HELIX 24 AC6 VAL D 88 SER D 99 1 12
HELIX 25 AC7 ARG D 100 LEU D 108 1 9
HELIX 26 AC8 SER D 113 HIS D 123 1 11
HELIX 27 AC9 ALA D 149 ASN D 154 1 6
HELIX 28 AD1 LEU D 155 MET D 165 1 11
HELIX 29 AD2 ASP D 190 LEU D 194 5 5
HELIX 30 AD3 ASN D 199 TYR D 207 1 9
HELIX 31 AD4 GLU E 50 ARG E 64 1 15
HELIX 32 AD5 GLY E 103 ALA E 113 1 11
HELIX 33 AD6 ASN E 127 LEU E 142 1 16
HELIX 34 AD7 THR E 144 ARG E 152 1 9
HELIX 35 AD8 ASP F 15 TYR F 33 1 19
HELIX 36 AD9 PRO F 68 ARG F 82 1 15
HELIX 37 AE1 ASP G 20 MET G 31 1 12
HELIX 38 AE2 LYS G 35 LYS G 53 1 19
HELIX 39 AE3 GLU G 57 LYS G 70 1 14
HELIX 40 AE4 SER G 92 ASN G 109 1 18
HELIX 41 AE5 ARG G 115 GLY G 130 1 16
HELIX 42 AE6 GLY G 132 ALA G 145 1 14
HELIX 43 AE7 ALA G 150 ARG G 155 5 6
HELIX 44 AE8 ASP H 4 VAL H 19 1 16
HELIX 45 AE9 SER H 29 GLU H 42 1 14
HELIX 46 AF1 ARG H 102 LEU H 107 5 6
HELIX 47 AF2 ASP H 121 LEU H 127 1 7
HELIX 48 AF3 ASP I 32 PHE I 37 1 6
HELIX 49 AF4 ARG I 42 ALA I 46 5 5
HELIX 50 AF5 LEU I 47 VAL I 53 1 7
HELIX 51 AF6 GLY I 69 ASN I 89 1 21
HELIX 52 AF7 TYR I 92 LYS I 97 1 6
HELIX 53 AF8 ALA J 18 ARG J 28 1 11
HELIX 54 AF9 LYS J 80 LEU J 85 1 6
HELIX 55 AG1 THR K 57 TYR K 75 1 19
HELIX 56 AG2 ARG K 91 GLY K 102 1 12
HELIX 57 AG3 LYS K 122 ARG K 126 5 5
HELIX 58 AG4 THR L 6 LYS L 13 1 8
HELIX 59 AG5 ARG M 14 TYR M 21 1 8
HELIX 60 AG6 GLY M 26 THR M 37 1 12
HELIX 61 AG7 ARG M 44 LEU M 48 5 5
HELIX 62 AG8 ALA M 51 ASN M 62 1 12
HELIX 63 AG9 LEU M 66 ILE M 84 1 19
HELIX 64 AH1 CYS M 86 ARG M 94 1 9
HELIX 65 AH2 ALA M 107 GLY M 112 1 6
HELIX 66 AH3 ARG N 3 ILE N 7 5 5
HELIX 67 AH4 GLU N 8 ARG N 12 5 5
HELIX 68 AH5 PHE N 16 ALA N 20 5 5
HELIX 69 AH6 ARG N 29 VAL N 33 5 5
HELIX 70 AH7 CYS N 40 GLY N 51 1 12
HELIX 71 AH8 THR O 4 ALA O 16 1 13
HELIX 72 AH9 SER O 24 LEU O 43 1 20
HELIX 73 AI1 ASP O 49 ASP O 74 1 26
HELIX 74 AI2 ASP O 74 GLY O 86 1 13
HELIX 75 AI3 ASP P 52 SER P 61 1 10
HELIX 76 AI4 THR P 67 ALA P 77 1 11
HELIX 77 AI5 ARG Q 81 GLU Q 96 1 16
HELIX 78 AI6 ASN R 36 LYS R 41 1 6
HELIX 79 AI7 ARG R 42 LEU R 44 5 3
HELIX 80 AI8 PRO R 52 GLY R 57 1 6
HELIX 81 AI9 SER R 59 LEU R 76 1 18
HELIX 82 AJ1 LEU S 15 LEU S 20 1 6
HELIX 83 AJ2 LEU S 20 LYS S 25 1 6
HELIX 84 AJ3 VAL S 41 VAL S 45 5 5
HELIX 85 AJ4 THR S 63 VAL S 67 5 5
HELIX 86 AJ5 LYS S 70 ALA S 75 5 6
HELIX 87 AJ6 LEU T 13 GLU T 46 1 34
HELIX 88 AJ7 LYS T 48 ALA T 67 1 20
HELIX 89 AJ8 LYS T 74 LEU T 92 1 19
HELIX 90 AJ9 THR V 8 ARG V 15 1 8
HELIX 91 AK1 SER Y 13 GLY Y 22 1 10
HELIX 92 AK2 GLY Y 36 ASP Y 46 1 11
HELIX 93 AK3 VAL Y 57 ASN Y 60 5 4
HELIX 94 AK4 LEU Y 61 ILE Y 69 1 9
HELIX 95 AK5 LYS Y 71 GLY Y 75 5 5
HELIX 96 AK6 ALA Y 86 LEU Y 90 5 5
HELIX 97 AK7 PRO Y 91 LYS Y 95 5 5
HELIX 98 AK8 TRP Y 107 LYS Y 116 1 10
HELIX 99 AK9 ASN Y 118 ASP Y 127 1 10
HELIX 100 AL1 ASP Y 143 GLU Y 147 5 5
HELIX 101 AL2 ALA Y 148 GLY Y 154 1 7
HELIX 102 AL3 SER Y 159 SER Y 165 1 7
HELIX 103 AL4 SER Y 165 GLY Y 176 1 12
HELIX 104 AL5 ASP Y 186 LYS Y 191 1 6
HELIX 105 AL6 GLN Y 192 ASN Y 194 5 3
HELIX 106 AL7 TRP Y 197 PHE Y 203 1 7
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 41 N ALA B 34
SHEET 1 AA2 5 TYR B 92 VAL B 93 0
SHEET 2 AA2 5 LEU B 69 VAL B 71 1 N PHE B 70 O VAL B 93
SHEET 3 AA2 5 ILE B 162 VAL B 164 1 O PHE B 163 N VAL B 71
SHEET 4 AA2 5 VAL B 184 ALA B 188 1 O ILE B 185 N ILE B 162
SHEET 5 AA2 5 TYR B 199 PRO B 202 1 O ILE B 201 N ALA B 186
SHEET 1 AA3 3 LEU C 52 ASP C 56 0
SHEET 2 AA3 3 THR C 67 VAL C 70 -1 O HIS C 69 N ARG C 54
SHEET 3 AA3 3 ASN C 102 GLU C 105 1 O GLN C 104 N VAL C 70
SHEET 1 AA4 4 ALA C 169 GLN C 170 0
SHEET 2 AA4 4 GLY C 148 VAL C 153 -1 N ALA C 149 O GLN C 170
SHEET 3 AA4 4 VAL C 198 PHE C 203 -1 O PHE C 203 N GLY C 148
SHEET 4 AA4 4 ILE C 182 ALA C 187 -1 N GLY C 185 O ALA C 200
SHEET 1 AA5 2 LEU D 176 ASP D 177 0
SHEET 2 AA5 2 LYS D 182 GLY D 183 -1 O LYS D 182 N ASP D 177
SHEET 1 AA6 4 GLU E 7 ARG E 14 0
SHEET 2 AA6 4 PHE E 28 GLY E 35 -1 O GLY E 35 N GLU E 7
SHEET 3 AA6 4 ARG E 40 ALA E 48 -1 O GLY E 44 N VAL E 32
SHEET 4 AA6 4 MET E 66 GLU E 68 -1 O VAL E 67 N VAL E 41
SHEET 1 AA7 2 MET E 19 GLN E 20 0
SHEET 2 AA7 2 GLY E 23 ARG E 24 -1 O GLY E 23 N GLN E 20
SHEET 1 AA8 4 ILE E 80 PHE E 84 0
SHEET 2 AA8 4 SER E 87 PRO E 93 -1 O SER E 87 N PHE E 84
SHEET 3 AA8 4 ILE E 118 GLY E 124 -1 O LEU E 123 N LYS E 88
SHEET 4 AA8 4 VAL E 100 ILE E 101 1 N ILE E 101 O ILE E 118
SHEET 1 AA9 4 LYS F 39 ILE F 52 0
SHEET 2 AA9 4 ASP F 55 GLN F 64 -1 O PHE F 60 N GLY F 44
SHEET 3 AA9 4 ARG F 2 LEU F 10 -1 N VAL F 6 O TYR F 63
SHEET 4 AA9 4 GLU F 66 MET F 67 -1 O MET F 67 N ARG F 2
SHEET 1 AB1 4 LYS F 39 ILE F 52 0
SHEET 2 AB1 4 ASP F 55 GLN F 64 -1 O PHE F 60 N GLY F 44
SHEET 3 AB1 4 ARG F 2 LEU F 10 -1 N VAL F 6 O TYR F 63
SHEET 4 AB1 4 VAL F 85 LYS F 92 -1 O ARG F 86 N VAL F 9
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 76 0
SHEET 2 AB3 2 VAL G 87 GLU G 90 -1 O VAL G 87 N ARG G 76
SHEET 1 AB4 3 ASP H 25 PRO H 27 0
SHEET 2 AB4 3 LYS H 56 TYR H 62 -1 O LEU H 59 N VAL H 26
SHEET 3 AB4 3 GLY H 47 VAL H 53 -1 N GLU H 49 O ARG H 60
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 GLY H 117 N THR H 114
SHEET 1 AB7 4 TYR I 4 GLY I 6 0
SHEET 2 AB7 4 VAL I 14 LEU I 19 -1 O VAL I 17 N GLY I 6
SHEET 3 AB7 4 ALA I 61 ARG I 66 -1 O THR I 64 N ARG I 16
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 ARG J 70 0
SHEET 2 AB8 3 ARG J 5 GLY J 10 -1 N GLY J 10 O HIS J 68
SHEET 3 AB8 3 VAL J 94 LYS J 99 -1 O LYS J 99 N ARG J 5
SHEET 1 AB9 3 ARG J 46 THR J 48 0
SHEET 2 AB9 3 HIS J 62 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 ILE K 29 THR K 33 -1 N ILE K 32 O ILE K 40
SHEET 3 AC1 6 SER K 16 HIS K 22 -1 N ARG K 18 O THR K 33
SHEET 4 AC1 6 SER K 79 ARG K 85 1 O ASP K 81 N ALA K 19
SHEET 5 AC1 6 GLN K 104 ASP K 110 1 O LYS K 106 N VAL K 80
SHEET 6 AC1 6 LEU R 85 VAL R 86 -1 O LEU R 85 N ASP K 110
SHEET 1 AC2 4 THR L 42 VAL L 43 0
SHEET 2 AC2 4 ARG L 53 LEU L 60 -1 O ARG L 53 N VAL L 43
SHEET 3 AC2 4 ARG L 33 VAL L 39 -1 N VAL L 36 O ARG L 59
SHEET 4 AC2 4 VAL L 82 ILE L 85 -1 O ILE L 85 N ARG L 33
SHEET 1 AC3 4 THR L 42 VAL L 43 0
SHEET 2 AC3 4 ARG L 53 LEU L 60 -1 O ARG L 53 N VAL L 43
SHEET 3 AC3 4 GLU L 65 TYR L 69 -1 O VAL L 66 N VAL L 58
SHEET 4 AC3 4 TYR L 98 HIS L 99 1 O TYR L 98 N TYR L 69
SHEET 1 AC4 4 GLU P 34 LYS P 35 0
SHEET 2 AC4 4 VAL P 20 ASP P 23 -1 N VAL P 21 O GLU P 34
SHEET 3 AC4 4 VAL P 2 ARG P 5 -1 N ARG P 5 O VAL P 20
SHEET 4 AC4 4 GLN P 65 PRO P 66 1 O GLN P 65 N VAL P 2
SHEET 1 AC5 2 TYR P 38 TYR P 39 0
SHEET 2 AC5 2 LEU P 49 LYS P 50 -1 O LYS P 50 N TYR P 38
SHEET 1 AC6 6 VAL Q 5 SER Q 12 0
SHEET 2 AC6 6 THR Q 18 PRO Q 28 -1 O LEU Q 22 N VAL Q 9
SHEET 3 AC6 6 VAL Q 35 HIS Q 45 -1 O TYR Q 42 N VAL Q 21
SHEET 4 AC6 6 PHE Q 71 GLU Q 78 1 O PHE Q 71 N HIS Q 45
SHEET 5 AC6 6 VAL Q 56 GLU Q 61 -1 N VAL Q 56 O VAL Q 77
SHEET 6 AC6 6 VAL Q 5 SER Q 12 -1 N LEU Q 6 O ILE Q 59
SHEET 1 AC7 2 THR S 48 TYR S 52 0
SHEET 2 AC7 2 HIS S 57 TYR S 61 -1 O VAL S 58 N VAL S 51
SHEET 1 AC8 2 LEU Y 2 LYS Y 5 0
SHEET 2 AC8 2 LYS Y 8 ASP Y 11 -1 O LYS Y 8 N LYS Y 5
SHEET 1 AC9 7 VAL Y 80 ILE Y 84 0
SHEET 2 AC9 7 THR Y 49 ASP Y 55 1 N GLY Y 53 O VAL Y 83
SHEET 3 AC9 7 ARG Y 26 LEU Y 31 1 N HIS Y 28 O PHE Y 50
SHEET 4 AC9 7 ALA Y 98 LEU Y 104 1 O SER Y 102 N LEU Y 31
SHEET 5 AC9 7 ALA Y 129 THR Y 139 1 O HIS Y 134 N ILE Y 101
SHEET 6 AC9 7 PHE Y 209 VAL Y 216 -1 O VAL Y 212 N PHE Y 137
SHEET 7 AC9 7 PHE Y 177 LEU Y 185 -1 N ARG Y 178 O HIS Y 215
LINK OP2 A A 8 MG MG A1695 1555 1555 2.97
LINK O6 G A 11 MG MG A1609 1555 1555 2.74
LINK O4 U A 12 MG MG A1609 1555 1555 2.53
LINK O4 U A 14 MG MG A1613 1555 1555 2.65
LINK OP2 U A 17 MG MG A1613 1555 1555 2.82
LINK OP1 G A 21 MG MG A1637 1555 1555 2.23
LINK OP2 C A 48 MG MG A1638 1555 1555 2.15
LINK OP2 A A 53 MG MG A1679 1555 1555 2.34
LINK O3' C A 58 MG MG A1608 1555 1555 2.47
LINK OP1 A A 59 MG MG A1608 1555 1555 2.89
LINK OP2 G A 111 MG MG A1707 1555 1555 2.38
LINK OP1 G A 115 MG MG A1638 1555 1555 2.15
LINK OP2 A A 116 MG MG A1701 1555 1555 2.68
LINK OP2 G A 117 MG MG A1701 1555 1555 1.89
LINK OP2 A A 195 MG MG A1699 1555 1555 2.50
LINK O6 G A 258 MG MG A1601 1555 1555 2.57
LINK OP2 G A 266 MG MG A1601 1555 1555 2.69
LINK OP2 G A 289 MG MG A1701 1555 1555 2.28
LINK OP1 G A 299 MG MG A1614 1555 1555 2.35
LINK O6 G A 299 MG MG A1670 1555 1555 1.88
LINK O4 U A 304 MG MG A1702 1555 1555 2.87
LINK OP2 C A 352 MG MG A1703 1555 1555 2.31
LINK O2 C A 372 MG MG A1704 1555 1555 2.53
LINK O6 G A 376 MG MG A1704 1555 1555 2.62
LINK OP1 U A 387 MG MG A1608 1555 1555 2.35
LINK O4 U A 387 MG MG A1704 1555 1555 2.62
LINK OP1 C A 504 MG MG A1706 1555 1555 2.48
LINK OP2 A A 509 MG MG A1633 1555 1555 2.34
LINK O3' A A 509 MG MG A1633 1555 1555 2.71
LINK O4 U A 516 MG MG A1672 1555 1555 2.23
LINK OP1 A A 533 MG MG A1672 1555 1555 2.53
LINK OP1 G A 558 MG MG A1670 1555 1555 2.25
LINK OP2 U A 560 MG MG A1634 1555 1555 2.68
LINK OP1 A A 572 MG MG A1636 1555 1555 2.46
LINK OP2 A A 572 MG MG A1673 1555 1555 2.49
LINK OP2 A A 573 MG MG A1673 1555 1555 2.17
LINK OP2 A A 574 MG MG A1673 1555 1555 2.15
LINK OP1 G A 576 MG MG A1615 1555 1555 2.70
LINK OP1 C A 578 MG MG A1629 1555 1555 2.45
LINK OP2 G A 588 MG MG A1657 1555 1555 2.28
LINK O6 G A 592 MG MG A1607 1555 1555 2.54
LINK O6 G A 593 MG MG A1607 1555 1555 2.28
LINK OP2 C A 596 MG MG A1639 1555 1555 2.66
LINK OP2 G A 597 MG MG A1639 1555 1555 2.55
LINK O4 U A 598 MG MG A1639 1555 1555 2.54
LINK OP2 A A 608 MG MG A1676 1555 1555 2.62
LINK O6 G A 635 MG MG A1655 1555 1555 2.66
LINK O4 U A 636 MG MG A1655 1555 1555 2.61
LINK O6 G A 637 MG MG A1644 1555 1555 2.93
LINK O3' A A 665 MG MG A1610 1555 1555 2.24
LINK OP1 G A 666 MG MG A1610 1555 1555 2.43
LINK O6 G A 703 MG MG A1600 1555 1555 2.52
LINK OP2 C A 749 MG MG A1622 1555 1555 2.30
LINK OP2 G A 750 MG MG A1622 1555 1555 2.47
LINK OP2 A A 766 MG MG A1624 1555 1555 2.34
LINK OP2 A A 768 MG MG A1625 1555 1555 2.49
LINK OP1 A A 777 MG MG A1628 1555 1555 2.21
LINK OP1 A A 782 MG MG A1710 1555 1555 2.79
LINK OP1 A A 794 MG MG A1710 1555 1555 2.67
LINK OP2 A A 860 MG MG A1643 1555 1555 2.25
LINK O6 G A 888 MG MG A1677 1555 1555 2.78
LINK O6 G A 895 MG MG A1678 1555 1555 2.94
LINK O6 G A 925 MG MG A1689 1555 1555 2.50
LINK OP1 C A 934 MG MG A1648 1555 1555 2.46
LINK OP2 A A 937 MG MG A1647 1555 1555 2.48
LINK OP1 G A 944 MG MG A1659 1555 1555 2.17
LINK OP2 G A 945 MG MG A1659 1555 1555 2.29
LINK OP1 A A 964 MG MG A1660 1555 1555 2.25
LINK OP2 C A 980 MG MG A1661 1555 1555 2.55
LINK O4 U A 981 MG MG A1661 1555 1555 2.48
LINK O2 U A 982 MG MG A1661 1555 1555 2.86
LINK OP1 C A1054 MG MG A1663 1555 1555 2.36
LINK OP2 C A1054 MG MG A1663 1555 1555 2.77
LINK O5' C A1054 MG MG A1664 1555 1555 2.71
LINK O3' A A1067 MG MG A1681 1555 1555 2.46
LINK OP1 G A1068 MG MG A1681 1555 1555 2.54
LINK OP1 U A1083 MG MG A1683 1555 1555 2.22
LINK OP1 G A1094 MG MG A1681 1555 1555 2.15
LINK OP2 U A1095 MG MG A1682 1555 1555 2.27
LINK O6 G A1108 MG MG A1682 1555 1555 2.52
LINK OP2 A A1110 MG MG A1680 1555 1555 2.25
LINK O3' U A1196 MG MG A1664 1555 1555 2.75
LINK OP1 G A1197 MG MG A1664 1555 1555 2.32
LINK OP2 G A1198 MG MG A1664 1555 1555 2.53
LINK OP1 U A1199 MG MG A1660 1555 1555 2.19
LINK O6 G A1222 MG MG A1661 1555 1555 2.38
LINK OP1 G A1224 MG MG A1685 1555 1555 2.01
LINK O6 G A1266 MG MG A1686 1555 1555 2.80
LINK OP2 G A1304 MG MG A1715 1555 1555 2.37
LINK O6 G A1370 MG MG A1651 1555 1555 2.49
LINK O6 G A1432 MG MG A1617 1555 1555 2.22
LINK O2' C A1452 MG MG A1600 1555 3545 2.51
LINK O6 G A1469 MG MG A1667 1555 1555 2.82
LINK OP2 A A1499 MG MG A1691 1555 1555 2.60
LINK OP2 A A1500 MG MG A1691 1555 1555 1.90
LINK OP2 G A1505 MG MG A1691 1555 1555 2.58
LINK OP2 G A1517 MG MG A1619 1555 1555 1.93
LINK MG MG A1665 OG1 THR T 35 1555 1555 2.27
LINK OD1 ASP B 166 MG MG B 301 1555 1555 2.69
LINK OD2 ASP B 166 MG MG B 301 1555 1555 2.37
LINK OD2 ASP B 205 MG MG B 301 1555 1555 2.38
LINK SG CYS D 9 ZN ZN D 301 1555 1555 2.56
LINK SG CYS D 12 ZN ZN D 301 1555 1555 2.86
LINK SG CYS D 26 ZN ZN D 301 1555 1555 2.67
LINK SG CYS D 31 ZN ZN D 301 1555 1555 2.28
LINK SG CYS N 24 ZN ZN N 101 1555 1555 2.40
LINK SG CYS N 27 ZN ZN N 101 1555 1555 2.02
LINK SG CYS N 40 ZN ZN N 101 1555 1555 2.44
LINK SG CYS N 43 ZN ZN N 101 1555 1555 2.21
CISPEP 1 LYS Y 116 PRO Y 117 0 -7.71
CISPEP 2 TYR Y 141 SER Y 142 0 -13.60
SITE 1 AC1 2 G A 703 C A1452
SITE 1 AC2 3 G A 257 G A 258 G A 266
SITE 1 AC3 1 G A 577
SITE 1 AC4 2 G A 581 G A 758
SITE 1 AC5 3 G A 592 G A 593 U A 646
SITE 1 AC6 3 C A 58 A A 59 U A 387
SITE 1 AC7 4 G A 11 U A 12 G A 21 G A 22
SITE 1 AC8 2 A A 665 G A 666
SITE 1 AC9 1 G A 115
SITE 1 AD1 2 U A 14 U A 17
SITE 1 AD2 2 G A 297 G A 299
SITE 1 AD3 2 G A 575 G A 576
SITE 1 AD4 2 A A 583 G A 584
SITE 1 AD5 1 G A1432
SITE 1 AD6 2 G A1517 ARG Y 37
SITE 1 AD7 1 G A 377
SITE 1 AD8 1 G A 438
SITE 1 AD9 2 C A 749 G A 750
SITE 1 AE1 2 A A 766 C A 812
SITE 1 AE2 1 A A 768
SITE 1 AE3 1 G A 774
SITE 1 AE4 1 A A 777
SITE 1 AE5 2 G A 576 C A 578
SITE 1 AE6 1 G A 362
SITE 1 AE7 2 A A 453 C A 454
SITE 1 AE8 2 A A 509 A A 510
SITE 1 AE9 1 U A 560
SITE 1 AF1 1 A A 572
SITE 1 AF2 1 G A 21
SITE 1 AF3 3 C A 48 U A 114 G A 115
SITE 1 AF4 4 G A 595 C A 596 G A 597 U A 598
SITE 1 AF5 2 G A 837 G A 838
SITE 1 AF6 2 G A 858 G A 869
SITE 1 AF7 1 G A 570
SITE 1 AF8 1 A A 860
SITE 1 AF9 2 G A 637 G A 638
SITE 1 AG1 3 G A 885 G A 886 U A 911
SITE 1 AG2 1 G A1385
SITE 1 AG3 2 A A 937 A A 938
SITE 1 AG4 2 C A 934 U A1345
SITE 1 AG5 2 G A1370 G A1371
SITE 1 AG6 3 A A 602 G A 635 U A 636
SITE 1 AG7 1 G A 588
SITE 1 AG8 2 G A 944 G A 945
SITE 1 AG9 2 A A 964 U A1199
SITE 1 AH1 6 C A 979 C A 980 U A 981 U A 982
SITE 2 AH1 6 G A1221 G A1222
SITE 1 AH2 3 G A1053 C A1054 G A1197
SITE 1 AH3 4 C A1054 U A1196 G A1197 G A1198
SITE 1 AH4 3 G A1441 G A1455 THR T 35
SITE 1 AH5 1 G A1469
SITE 1 AH6 1 A A 915
SITE 1 AH7 1 G A 301
SITE 1 AH8 4 G A 299 G A 558 U A 560 G A 566
SITE 1 AH9 1 G A 324
SITE 1 AI1 4 U A 516 G A 517 A A 532 A A 533
SITE 1 AI2 3 A A 572 A A 573 A A 574
SITE 1 AI3 2 G A 649 G A 650
SITE 1 AI4 2 G A 595 U A 641
SITE 1 AI5 2 A A 608 G A 610
SITE 1 AI6 1 G A 888
SITE 1 AI7 1 G A 895
SITE 1 AI8 2 A A 53 A A 353
SITE 1 AI9 2 A A1110 C A1189
SITE 1 AJ1 4 A A1067 G A1068 G A1094 G A1387
SITE 1 AJ2 2 U A1095 G A1108
SITE 1 AJ3 1 U A1083
SITE 1 AJ4 1 G A1224
SITE 1 AJ5 1 G A1266
SITE 1 AJ6 5 C A 924 G A 925 U A1390 U A1391
SITE 2 AJ6 5 G A1392
SITE 1 AJ7 4 A A1499 A A1500 G A1504 G A1505
SITE 1 AJ8 2 G A 64 A A 101
SITE 1 AJ9 2 A A 8 A A 298
SITE 1 AK1 2 A A 535 C A 536
SITE 1 AK2 2 G A 148 A A 172
SITE 1 AK3 1 G A 168
SITE 1 AK4 1 A A 195
SITE 1 AK5 3 A A 116 G A 117 G A 289
SITE 1 AK6 3 G A 293 U A 304 G A 305
SITE 1 AK7 2 C A 330 C A 352
SITE 1 AK8 4 C A 372 U A 375 G A 376 U A 387
SITE 1 AK9 2 G A 410 A A 431
SITE 1 AL1 2 C A 504 G A 505
SITE 1 AL2 1 G A 111
SITE 1 AL3 2 A A 782 A A 794
SITE 1 AL4 2 U A 133 U A 229
SITE 1 AL5 5 G A1057 G A1058 C A1059 G A1198
SITE 2 AL5 5 U A1199
SITE 1 AL6 2 C A1303 G A1304
SITE 1 AL7 1 G A1520
SITE 1 AL8 3 ASP B 166 ASP B 191 ASP B 205
SITE 1 AL9 5 CYS D 9 CYS D 12 LEU D 19 CYS D 26
SITE 2 AL9 5 CYS D 31
SITE 1 AM1 2 U A 863 GLU E 83
SITE 1 AM2 4 CYS N 24 CYS N 27 CYS N 40 CYS N 43
SITE 1 AM3 2 C A 980 ALA N 20
SITE 1 AM4 16 A A1408 C A1484 U A1485 GLY Y 32
SITE 2 AM4 16 THR Y 33 GLY Y 34 ASP Y 55 PRO Y 56
SITE 3 AM4 16 ALA Y 87 GLU Y 88 LEU Y 104 PHE Y 105
SITE 4 AM4 16 THR Y 109 LEU Y 110 LEU Y 196 TRP Y 197
CRYST1 403.520 403.520 176.610 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 0.002478 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002478 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005662 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
