HEADER RIBOSOME 27-FEB-15 4YHH
TITLE CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS
TITLE 2 THERMOPHILUS IN COMPLEX WITH TIGECYCLINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 16S RIBOSOMAL RNA;
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
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
KEYWDS PROTEIN SYNTHESIS, RIBOSOME, ANTIBIOTIC
EXPDTA X-RAY DIFFRACTION
AUTHOR A.SCHEDLBAUER,T.KAMINISHI,B.OCHOA-LIZARRALDE,N.DHIMOLE,S.ZHOU,
AUTHOR 2 J.P.LOPEZ-ALONSO,S.R.CONNELL,P.FUCINI
REVDAT 4 10-JAN-24 4YHH 1 LINK
REVDAT 3 03-FEB-16 4YHH 1 COMPND SOURCE DBREF
REVDAT 2 22-APR-15 4YHH 1 JRNL
REVDAT 1 08-APR-15 4YHH 0
JRNL AUTH A.SCHEDLBAUER,T.KAMINISHI,B.OCHOA-LIZARRALDE,N.DHIMOLE,
JRNL AUTH 2 S.ZHOU,J.P.LOPEZ-ALONSO,S.R.CONNELL,P.FUCINI
JRNL TITL STRUCTURAL CHARACTERIZATION OF AN ALTERNATIVE MODE OF
JRNL TITL 2 TIGECYCLINE BINDING TO THE BACTERIAL RIBOSOME.
JRNL REF ANTIMICROB.AGENTS CHEMOTHER. V. 59 2849 2015
JRNL REFN ESSN 1098-6596
JRNL PMID 25753625
JRNL DOI 10.1128/AAC.04895-14
REMARK 2
REMARK 2 RESOLUTION. 3.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.3_928
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) : 3.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.72
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 87.5
REMARK 3 NUMBER OF REFLECTIONS : 171310
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.231
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.287
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030
REMARK 3 FREE R VALUE TEST SET COUNT : 8610
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 0.0000 - 3.4000 0.00 0 0 0.0000 0.0000
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.23
REMARK 3 B_SOL : 103.2
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.670
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 42.540
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 212.9
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 23.34670
REMARK 3 B22 (A**2) : 23.34670
REMARK 3 B33 (A**2) : -46.69340
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 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 : 0.010 55817
REMARK 3 ANGLE : 1.308 82825
REMARK 3 CHIRALITY : 0.079 10389
REMARK 3 PLANARITY : 0.007 4926
REMARK 3 DIHEDRAL : 17.963 25854
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: RESNAME T1C
REMARK 3 ORIGIN FOR THE GROUP (A): 306.8429 179.1150 33.1229
REMARK 3 T TENSOR
REMARK 3 T11: 1.9183 T22: 1.5514
REMARK 3 T33: 2.1625 T12: -0.1497
REMARK 3 T13: -0.4486 T23: 0.2090
REMARK 3 L TENSOR
REMARK 3 L11: 1.3031 L22: 0.3919
REMARK 3 L33: 1.8463 L12: -0.4700
REMARK 3 L13: -1.1933 L23: 0.8409
REMARK 3 S TENSOR
REMARK 3 S11: 1.8393 S12: -4.1656 S13: 1.2648
REMARK 3 S21: 4.7462 S22: 1.3751 S23: 1.1035
REMARK 3 S31: -0.5711 S32: 4.7190 S33: 0.1129
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 4YHH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-FEB-15.
REMARK 100 THE DEPOSITION ID IS D_1000207234.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS JULY 4, 2012
REMARK 200 DATA SCALING SOFTWARE : XSCALE JULY 4, 2012
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 192315
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
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 (%) : 96.7
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.16200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 4.4500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 6.99500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 2ZM6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 73.88
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES-KOH, MGCL2, NH4CL, BETA
REMARK 280 -MERCAPTOETHANOL, MPD, SPERMIDINE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 85.86500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 204.79500
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 204.79500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 42.93250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 204.79500
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 204.79500
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 128.79750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 204.79500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 204.79500
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 42.93250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 204.79500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 204.79500
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 128.79750
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 85.86500
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 21-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 94420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 277370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -824.0 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
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 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 OP1 A A 559 NH2 ARG E 126 1.92
REMARK 500 O2 C A 501 O2' C A 549 1.98
REMARK 500 O GLY B 100 N LEU B 102 2.00
REMARK 500 N2 G A 947 O2 U A 1235 2.03
REMARK 500 OP1 G A 426 OH TYR D 38 2.04
REMARK 500 O ARG D 25 OG SER D 28 2.06
REMARK 500 O2' G A 667 OD1 ASP O 49 2.06
REMARK 500 O ARG H 14 OG1 THR H 17 2.06
REMARK 500 OP2 A A 1256 NZ LYS C 26 2.06
REMARK 500 O2' A A 533 OP2 A A 535 2.07
REMARK 500 O2 C A 620 OG SER D 137 2.07
REMARK 500 N2 G A 42 O2 C A 401 2.09
REMARK 500 O2' A A 959 O2' C A 984 2.10
REMARK 500 O2' A A 978 N3 C A 1322 2.11
REMARK 500 O THR O 33 ND2 ASN O 37 2.11
REMARK 500 NH1 ARG C 40 O VAL C 55 2.11
REMARK 500 OP1 C A 689 OG SER K 44 2.12
REMARK 500 O ARG E 152 N GLY E 154 2.12
REMARK 500 O2' G A 1417 N6 A A 1483 2.12
REMARK 500 O THR H 17 N TYR H 20 2.13
REMARK 500 O ASP E 36 N GLN E 38 2.13
REMARK 500 O GLU B 4 NH1 ARG B 217 2.13
REMARK 500 O6 G A 594 N4 C A 645 2.14
REMARK 500 O2' U A 17 O2' G A 1079 2.14
REMARK 500 NZ LYS M 79 OD2 ASP M 83 2.15
REMARK 500 OH TYR D 68 OE2 GLU D 98 2.16
REMARK 500 O2 C A 770 N4 C A 899 2.16
REMARK 500 OG1 THR H 114 N GLY H 117 2.17
REMARK 500 OP1 A A 1503 O2' A A 1531 2.17
REMARK 500 O2' G A 396 OP1 C A 398 2.17
REMARK 500 O2' G A 869 N7 A A 872 2.17
REMARK 500 O LEU R 76 N LEU R 78 2.18
REMARK 500 O GLY R 48 NH2 ARG R 74 2.18
REMARK 500 OP1 C A 545 NZ LYS D 61 2.18
REMARK 500 O GLY L 74 NH1 ARG L 102 2.18
REMARK 500 OP1 G A 581 NH2 ARG O 65 2.18
REMARK 500 O THR H 17 N VAL H 19 2.18
REMARK 500 OE2 GLU C 35 NH2 ARG C 59 2.19
REMARK 500 O2' G A 481 N4 C A 483 2.19
REMARK 500 O2' A A 975 OG SER N 32 2.19
REMARK 500 OE2 GLU F 42 OH TYR F 59 2.19
REMARK 500 N3 A A 938 O2' U A 1376 2.19
REMARK 500 OP2 G A 316 O2' G A 351 2.19
REMARK 500 OP1 C A 1326 NZ LYS V 12 2.19
REMARK 500 O2' C A 110 O ARG P 25 2.19
REMARK 500 O TYR M 59 OG1 THR M 63 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 G A 410 N9 G A 410 C4 0.050
REMARK 500 A A 728 N9 A A 728 C4 0.038
REMARK 500 G A 758 C5 G A 758 N7 -0.043
REMARK 500 CYS D 12 CB CYS D 12 SG 0.132
REMARK 500 GLU H 123 CG GLU H 123 CD 0.092
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 A A 8 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 U A 17 C6 - N1 - C2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 C A 18 C6 - N1 - C2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 C A 18 N3 - C4 - C5 ANGL. DEV. = -2.9 DEGREES
REMARK 500 C A 19 N3 - C2 - O2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 U A 37 C5 - C6 - N1 ANGL. DEV. = 4.3 DEGREES
REMARK 500 C A 40 C6 - N1 - C2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 C A 40 N3 - C2 - O2 ANGL. DEV. = -4.4 DEGREES
REMARK 500 C A 40 C2 - N1 - C1' ANGL. DEV. = 6.9 DEGREES
REMARK 500 G A 46 C8 - N9 - C4 ANGL. DEV. = -2.4 DEGREES
REMARK 500 C A 73 C6 - N1 - C2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 C A 99 C6 - N1 - C2 ANGL. DEV. = -2.7 DEGREES
REMARK 500 C A 110 C6 - N1 - C2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 C A 110 N3 - C2 - O2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 C A 110 C2 - N1 - C1' ANGL. DEV. = 9.2 DEGREES
REMARK 500 G A 115 N9 - C4 - C5 ANGL. DEV. = -2.5 DEGREES
REMARK 500 G A 124 N3 - C4 - C5 ANGL. DEV. = -3.7 DEGREES
REMARK 500 G A 124 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 C A 150 C6 - N1 - C2 ANGL. DEV. = -2.8 DEGREES
REMARK 500 C A 174 C6 - N1 - C2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 C A 177 N1 - C2 - O2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 C A 224 C6 - N1 - C2 ANGL. DEV. = -2.6 DEGREES
REMARK 500 C A 237 C6 - N1 - C2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 C A 241 C6 - N1 - C2 ANGL. DEV. = 2.9 DEGREES
REMARK 500 C A 242 C2 - N1 - C1' ANGL. DEV. = -7.5 DEGREES
REMARK 500 G A 278 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 U A 294 C6 - N1 - C2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 U A 294 C5 - C6 - N1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 C A 295 C6 - N1 - C2 ANGL. DEV. = -2.8 DEGREES
REMARK 500 C A 295 C5 - C6 - N1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 C A 295 N3 - C4 - N4 ANGL. DEV. = 4.4 DEGREES
REMARK 500 U A 296 N3 - C4 - C5 ANGL. DEV. = -3.6 DEGREES
REMARK 500 A A 298 N1 - C2 - N3 ANGL. DEV. = 3.3 DEGREES
REMARK 500 A A 298 C4 - C5 - C6 ANGL. DEV. = 4.3 DEGREES
REMARK 500 A A 298 N7 - C8 - N9 ANGL. DEV. = 3.3 DEGREES
REMARK 500 A A 298 C8 - N9 - C4 ANGL. DEV. = -3.1 DEGREES
REMARK 500 A A 298 C6 - C5 - N7 ANGL. DEV. = -4.3 DEGREES
REMARK 500 A A 300 N1 - C6 - N6 ANGL. DEV. = -3.8 DEGREES
REMARK 500 C A 311 N1 - C2 - O2 ANGL. DEV. = 5.1 DEGREES
REMARK 500 C A 311 N3 - C2 - O2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 U A 323 C5 - C6 - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 C A 328 C2 - N1 - C1' ANGL. DEV. = -6.8 DEGREES
REMARK 500 C A 355 C6 - N1 - C2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 C A 366 C6 - N1 - C2 ANGL. DEV. = -2.9 DEGREES
REMARK 500 C A 366 N3 - C4 - C5 ANGL. DEV. = -2.9 DEGREES
REMARK 500 C A 366 C4 - C5 - C6 ANGL. DEV. = 3.4 DEGREES
REMARK 500 C A 366 C5 - C4 - N4 ANGL. DEV. = 4.5 DEGREES
REMARK 500 C A 372 C6 - N1 - C2 ANGL. DEV. = 2.6 DEGREES
REMARK 500 A A 373 C8 - N9 - C4 ANGL. DEV. = 3.1 DEGREES
REMARK 500 C A 385 C6 - N1 - C2 ANGL. DEV. = -2.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 356 ANGLE DEVIATIONS.
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 PHE B 17 83.52 -60.72
REMARK 500 HIS B 19 -166.11 -115.63
REMARK 500 GLU B 20 -176.86 -65.95
REMARK 500 ALA B 29 -98.98 -29.68
REMARK 500 ARG B 30 -31.84 -11.97
REMARK 500 TYR B 33 -67.63 -99.55
REMARK 500 ALA B 34 -153.06 -168.83
REMARK 500 ARG B 36 85.72 -69.58
REMARK 500 ASN B 37 49.88 90.12
REMARK 500 GLU B 52 -78.46 -50.91
REMARK 500 LYS B 75 -11.26 -39.72
REMARK 500 GLN B 78 -90.76 -7.23
REMARK 500 ASP B 79 11.13 -65.55
REMARK 500 ARG B 82 -91.52 -36.96
REMARK 500 MET B 83 6.00 -60.11
REMARK 500 GLN B 95 -73.36 -70.93
REMARK 500 MET B 101 7.81 -19.78
REMARK 500 LEU B 102 -56.44 -150.91
REMARK 500 ASN B 104 23.41 154.67
REMARK 500 LYS B 147 -80.18 -61.87
REMARK 500 SER B 150 7.45 -51.93
REMARK 500 ALA B 161 132.64 -171.53
REMARK 500 ASP B 166 87.76 108.62
REMARK 500 PRO B 167 27.39 -77.32
REMARK 500 GLU B 170 54.50 -103.12
REMARK 500 GLU B 176 -70.26 -75.96
REMARK 500 ALA B 177 -0.52 -49.99
REMARK 500 PHE B 181 56.67 -28.56
REMARK 500 ASP B 189 -144.67 -84.28
REMARK 500 ASP B 191 41.22 -82.38
REMARK 500 LEU B 196 18.04 -67.67
REMARK 500 ILE B 208 10.73 -65.25
REMARK 500 SER B 216 7.92 -61.41
REMARK 500 LEU B 221 20.03 -74.83
REMARK 500 ILE B 222 -64.60 -99.77
REMARK 500 LEU C 12 84.25 -36.90
REMARK 500 ILE C 14 -40.33 -133.31
REMARK 500 THR C 15 33.27 -159.06
REMARK 500 ARG C 16 -153.66 -149.36
REMARK 500 TRP C 22 -149.40 -109.94
REMARK 500 ALA C 24 152.34 175.75
REMARK 500 GLU C 44 -80.44 -58.20
REMARK 500 LYS C 45 -41.47 -21.48
REMARK 500 LEU C 47 7.59 -48.10
REMARK 500 ALA C 53 -97.39 -108.45
REMARK 500 ILE C 57 49.80 -145.13
REMARK 500 ALA C 60 -163.07 -114.66
REMARK 500 ALA C 61 93.83 -60.91
REMARK 500 VAL C 66 94.17 -65.99
REMARK 500 LYS C 97 -161.75 -168.16
REMARK 500
REMARK 500 THIS ENTRY HAS 336 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 SER D 28 PRO D 29 143.31
REMARK 500 CYS D 31 ALA D 32 -135.88
REMARK 500 ARG F 2 ARG F 3 -148.42
REMARK 500 ARG F 46 ARG F 47 149.68
REMARK 500 LYS L 126 GLU L 127 -146.80
REMARK 500 TYR Q 32 GLY Q 33 148.86
REMARK 500 LYS Q 100 ARG Q 101 147.59
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 A1635 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 299 O6
REMARK 620 2 G A 558 OP1 157.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1621 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 307 OP2
REMARK 620 2 C A 308 OP2 103.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1628 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 450 OP1
REMARK 620 2 A A 452 OP2 57.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1630 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 506 OP1
REMARK 620 2 A A 509 OP2 129.0
REMARK 620 3 A A 510 OP2 149.3 80.4
REMARK 620 N 1 2
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 A A 572 OP2
REMARK 620 2 A A 573 OP2 69.5
REMARK 620 3 A A 574 OP2 137.6 68.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1643 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 596 OP2
REMARK 620 2 G A 597 OP2 69.9
REMARK 620 3 U A 598 O4 155.2 85.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1645 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 610 OP1
REMARK 620 2 G A 625 OP2 70.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1656 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 749 OP2
REMARK 620 2 G A 750 OP2 60.3
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 C A 934 OP1
REMARK 620 2 C A 934 O5' 53.1
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 937 OP2
REMARK 620 2 G A 939 O6 131.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1675 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A 964 OP1
REMARK 620 2 U A1199 OP1 57.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1702 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A 966 OP1
REMARK 620 2 T1C A1601 O21 136.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1690 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A 979 OP1
REMARK 620 2 C A 980 OP2 128.9
REMARK 620 3 G A1221 O6 146.5 83.6
REMARK 620 4 G A1222 O6 71.8 112.4 106.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1677 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A1054 OP2
REMARK 620 2 G A1197 OP2 76.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1688 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A1054 OP1
REMARK 620 2 G A1197 OP1 71.0
REMARK 620 3 G A1198 OP2 75.8 70.1
REMARK 620 4 T1C A1601 O12 142.7 71.8 89.6
REMARK 620 5 T1C A1601 O11 116.4 96.6 158.8 70.1
REMARK 620 N 1 2 3 4
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 G A1068 OP1
REMARK 620 2 G A1094 OP1 59.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1679 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C A1069 OP2
REMARK 620 2 U A1085 O2 142.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1683 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U A1095 OP2
REMARK 620 2 G A1108 O6 65.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1694 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A1238 OP2
REMARK 620 2 A A1238 O5' 51.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1703 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G A1304 OP2
REMARK 620 2 ASP V 5 OD2 125.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1699 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U A1498 O3'
REMARK 620 2 A A1499 OP2 52.2
REMARK 620 3 A A1500 OP2 99.4 50.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1700 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A A1500 OP1
REMARK 620 2 G A1504 OP1 138.5
REMARK 620 3 G A1505 OP1 59.3 141.6
REMARK 620 4 G A1508 OP1 55.4 112.3 104.6
REMARK 620 N 1 2 3
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 26 SG 88.5
REMARK 620 3 CYS D 31 SG 42.5 46.6
REMARK 620 N 1 2
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 80.9
REMARK 620 3 CYS N 40 SG 137.0 121.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue T1C A 1601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1602
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 1605
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1606
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 1618
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1619
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1620
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1621
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1622
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1623
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1624
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1625
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1626
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1627
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1628
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1629
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1630
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1631
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1632
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1633
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1634
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1635
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1636
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1637
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1638
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1639
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1640
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1641
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1643
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1644
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1645
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1646
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1647
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1648
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1649
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1650
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1651
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1652
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1655
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1656
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1658
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1659
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1660
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1661
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1662
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1663
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1665
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1667
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1668
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1669
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1671
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1672
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1673
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1674
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1675
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1676
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1677
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1678
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1679
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1680
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1681
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1682
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1683
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1684
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1685
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1688
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1689
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1690
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1691
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1692
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1693
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1694
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1695
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1696
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1697
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1699
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN D 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN N 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZM6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL SUBUNIT FROM THERMUS
REMARK 900 THERMOPHILUS
DBREF1 4YHH A 3 1532 GB AP008226.1
DBREF2 4YHH A 55771382 131303 132809
DBREF 4YHH B 3 228 UNP P80371 RS2_THET8 3 228
DBREF 4YHH C 2 207 UNP P80372 RS3_THET8 2 207
DBREF 4YHH D 2 209 UNP P80373 RS4_THET8 2 209
DBREF 4YHH E 5 161 UNP Q5SHQ5 RS5_THET8 5 161
DBREF 4YHH F 1 101 UNP Q5SLP8 RS6_THET8 1 101
DBREF 4YHH G 2 156 UNP P17291 RS7_THET8 2 156
DBREF 4YHH H 1 138 UNP Q5SHQ2 RS8_THET8 1 138
DBREF 4YHH I 2 128 UNP P80374 RS9_THET8 2 128
DBREF 4YHH J 3 101 UNP Q5SHN7 RS10_THET8 3 101
DBREF 4YHH K 11 125 UNP P80376 RS11_THET8 11 125
DBREF 4YHH L 5 128 UNP Q5SHN3 RS12_THET8 2 125
DBREF 4YHH M 2 120 UNP P80377 RS13_THET8 2 120
DBREF 4YHH N 2 61 UNP Q5SHQ1 RS14Z_THET8 2 61
DBREF 4YHH O 2 89 UNP Q5SJ76 RS15_THET8 2 89
DBREF 4YHH P 1 85 UNP Q5SJH3 RS16_THET8 1 85
DBREF 4YHH Q 2 105 UNP Q5SHP7 RS17_THET8 2 105
DBREF 4YHH R 16 88 UNP Q5SLQ0 RS18_THET8 16 88
DBREF 4YHH S 2 84 UNP Q5SHP2 RS19_THET8 2 84
DBREF 4YHH T 8 106 UNP P80380 RS20_THET8 8 106
DBREF 4YHH V 2 25 UNP Q5SIH3 RSHX_THET8 2 25
SEQRES 1 A 1507 G U U G G A G A G U U U G
SEQRES 2 A 1507 A U C C U G G C U C A G G
SEQRES 3 A 1507 G U G A A C G C U G G C G
SEQRES 4 A 1507 G C G U G C C U A A G A C
SEQRES 5 A 1507 A U G C A A G U C G U G C
SEQRES 6 A 1507 G G G C C G C G G G G U U
SEQRES 7 A 1507 U U A C U C C G U G G U C
SEQRES 8 A 1507 A G C G G C G G A C G G G
SEQRES 9 A 1507 U G A G U A A C G C G U G
SEQRES 10 A 1507 G G U G A C C U A C C C G
SEQRES 11 A 1507 G A A G A G G G G G A C A
SEQRES 12 A 1507 A C C C G G G G A A A C U
SEQRES 13 A 1507 C G G G C U A A U C C C C
SEQRES 14 A 1507 C A U G U G G A C C C G C
SEQRES 15 A 1507 C C C U U G G G G U G U G
SEQRES 16 A 1507 U C C A A A G G G C U U U
SEQRES 17 A 1507 G C C C G C U U C C G G A
SEQRES 18 A 1507 U G G G C C C G C G U C C
SEQRES 19 A 1507 C A U C A G C U A G U U G
SEQRES 20 A 1507 G U G G G G U A A U G G C
SEQRES 21 A 1507 C C A C C A A G G C G A C
SEQRES 22 A 1507 G A C G G G U A G C C G G
SEQRES 23 A 1507 U C U G A G A G G A U G G
SEQRES 24 A 1507 C C G G C C A C A G G G G
SEQRES 25 A 1507 C A C U G A G A C A C G G
SEQRES 26 A 1507 G C C C C A C U C C U A C
SEQRES 27 A 1507 G G G A G G C A G C A G U
SEQRES 28 A 1507 U A G G A A U C U U C C G
SEQRES 29 A 1507 C A A U G G G C G C A A G
SEQRES 30 A 1507 C C U G A C G G A G C G A
SEQRES 31 A 1507 C G C C G C U U G G A G G
SEQRES 32 A 1507 A A G A A G C C C U U C G
SEQRES 33 A 1507 G G G U G U A A A C U C C
SEQRES 34 A 1507 U G A A C C C G G G A C G
SEQRES 35 A 1507 A A A C C C C C G A C G A
SEQRES 36 A 1507 G G G G A C U G A C G G U
SEQRES 37 A 1507 A C C G G G G U A A U A G
SEQRES 38 A 1507 C G C C G G C C A A C U C
SEQRES 39 A 1507 C G U G C C A G C A G C C
SEQRES 40 A 1507 G C G G U A A U A C G G A
SEQRES 41 A 1507 G G G C G C G A G C G U U
SEQRES 42 A 1507 A C C C G G A U U C A C U
SEQRES 43 A 1507 G G G C G U A A A G G G C
SEQRES 44 A 1507 G U G U A G G C G G C C U
SEQRES 45 A 1507 G G G G C G U C C C A U G
SEQRES 46 A 1507 U G A A A G A C C A C G G
SEQRES 47 A 1507 C U C A A C C G U G G G G
SEQRES 48 A 1507 G A G C G U G G G A U A C
SEQRES 49 A 1507 G C U C A G G C U A G A C
SEQRES 50 A 1507 G G U G G G A G A G G G U
SEQRES 51 A 1507 G G U G G A A U U C C C G
SEQRES 52 A 1507 G A G U A G C G G U G A A
SEQRES 53 A 1507 A U G C G C A G A U A C C
SEQRES 54 A 1507 G G G A G G A A C G C C G
SEQRES 55 A 1507 A U G G C G A A G G C A G
SEQRES 56 A 1507 C C A C C U G G U C C A C
SEQRES 57 A 1507 C C G U G A C G C U G A G
SEQRES 58 A 1507 G C G C G A A A G C G U G
SEQRES 59 A 1507 G G G A G C A A A C C G G
SEQRES 60 A 1507 A U U A G A U A C C C G G
SEQRES 61 A 1507 G U A G U C C A C G C C C
SEQRES 62 A 1507 U A A A C G A U G C G C G
SEQRES 63 A 1507 C U A G G U C U C U G G G
SEQRES 64 A 1507 U C U C C U G G G G G C C
SEQRES 65 A 1507 G A A G C U A A C G C G U
SEQRES 66 A 1507 U A A G C G C G C C G C C
SEQRES 67 A 1507 U G G G G A G U A C G G C
SEQRES 68 A 1507 C G C A A G G C U G A A A
SEQRES 69 A 1507 C U C A A A G G A A U U G
SEQRES 70 A 1507 A C G G G G G C C C G C A
SEQRES 71 A 1507 C A A G C G G U G G A G C
SEQRES 72 A 1507 A U G U G G U U U A A U U
SEQRES 73 A 1507 C G A A G C A A C G C G A
SEQRES 74 A 1507 A G A A C C U U A C C A G
SEQRES 75 A 1507 G C C U U G A C A U G C U
SEQRES 76 A 1507 A G G G A A C C C G G G U
SEQRES 77 A 1507 G A A A G C C U G G G G U
SEQRES 78 A 1507 G C C C C G C G A G G G G
SEQRES 79 A 1507 A G C C C U A G C A C A G
SEQRES 80 A 1507 G U G C U G C A U G G C C
SEQRES 81 A 1507 G U C G U C A G C U C G U
SEQRES 82 A 1507 G C C G U G A G G U G U U
SEQRES 83 A 1507 G G G U U A A G U C C C G
SEQRES 84 A 1507 C A A C G A G C G C A A C
SEQRES 85 A 1507 C C C C G C C G U U A G U
SEQRES 86 A 1507 U G C C A G C G G U U C G
SEQRES 87 A 1507 G C C G G G C A C U C U A
SEQRES 88 A 1507 A C G G G A C U G C C C G
SEQRES 89 A 1507 C G A A A G C G G G A G G
SEQRES 90 A 1507 A A G G A G G G G A C G A
SEQRES 91 A 1507 C G U C U G G U C A G C A
SEQRES 92 A 1507 U G G C C C U U A C G G C
SEQRES 93 A 1507 C U G G G C G A C A C A C
SEQRES 94 A 1507 G U G C U A C A A U G C C
SEQRES 95 A 1507 C A C U A C A A A G C G A
SEQRES 96 A 1507 U G C C A C C C G G C A A
SEQRES 97 A 1507 C G G G G A G C U A A U C
SEQRES 98 A 1507 G C A A A A A G G U G G G
SEQRES 99 A 1507 C C C A G U U C G G A U U
SEQRES 100 A 1507 G G G G U C U G C A A C C
SEQRES 101 A 1507 C G A C C C C A U G A A G
SEQRES 102 A 1507 C C G G A A U C G C U A G
SEQRES 103 A 1507 U A A U C G C G G A U C A
SEQRES 104 A 1507 G C C A U G C C G C G G U
SEQRES 105 A 1507 G A A U A C G U U C C C G
SEQRES 106 A 1507 G G C C U U G U A C A C A
SEQRES 107 A 1507 C C G C C C G U C A C G C
SEQRES 108 A 1507 C A U G G G A G C G G G C
SEQRES 109 A 1507 U C U A C C C G A A G U C
SEQRES 110 A 1507 G C C G G G A G C C U A C
SEQRES 111 A 1507 G G G C A G G C G C C G A
SEQRES 112 A 1507 G G G U A G G G C C C G U
SEQRES 113 A 1507 G A C U G G G G C G A A G
SEQRES 114 A 1507 U C G U A A C A A G G U A
SEQRES 115 A 1507 G C U G U A C C G G A A G
SEQRES 116 A 1507 G U G C G G C U G G A U
SEQRES 1 B 226 VAL GLU ILE THR VAL LYS GLU LEU LEU GLU ALA GLY VAL
SEQRES 2 B 226 HIS PHE GLY HIS GLU ARG LYS ARG TRP ASN PRO LYS PHE
SEQRES 3 B 226 ALA ARG TYR ILE TYR ALA GLU ARG ASN GLY ILE HIS ILE
SEQRES 4 B 226 ILE ASP LEU GLN LYS THR MET GLU GLU LEU GLU ARG THR
SEQRES 5 B 226 PHE ARG PHE ILE GLU ASP LEU ALA MET ARG GLY GLY THR
SEQRES 6 B 226 ILE LEU PHE VAL GLY THR LYS LYS GLN ALA GLN ASP ILE
SEQRES 7 B 226 VAL ARG MET GLU ALA GLU ARG ALA GLY MET PRO TYR VAL
SEQRES 8 B 226 ASN GLN ARG TRP LEU GLY GLY MET LEU THR ASN PHE LYS
SEQRES 9 B 226 THR ILE SER GLN ARG VAL HIS ARG LEU GLU GLU LEU GLU
SEQRES 10 B 226 ALA LEU PHE ALA SER PRO GLU ILE GLU GLU ARG PRO LYS
SEQRES 11 B 226 LYS GLU GLN VAL ARG LEU LYS HIS GLU LEU GLU ARG LEU
SEQRES 12 B 226 GLN LYS TYR LEU SER GLY PHE ARG LEU LEU LYS ARG LEU
SEQRES 13 B 226 PRO ASP ALA ILE PHE VAL VAL ASP PRO THR LYS GLU ALA
SEQRES 14 B 226 ILE ALA VAL ARG GLU ALA ARG LYS LEU PHE ILE PRO VAL
SEQRES 15 B 226 ILE ALA LEU ALA ASP THR ASP SER ASP PRO ASP LEU VAL
SEQRES 16 B 226 ASP TYR ILE ILE PRO GLY ASN ASP ASP ALA ILE ARG SER
SEQRES 17 B 226 ILE GLN LEU ILE LEU SER ARG ALA VAL ASP LEU ILE ILE
SEQRES 18 B 226 GLN ALA ARG GLY GLY
SEQRES 1 C 206 GLY ASN LYS ILE HIS PRO ILE GLY PHE ARG LEU GLY ILE
SEQRES 2 C 206 THR ARG ASP TRP GLU SER ARG TRP TYR ALA GLY LYS LYS
SEQRES 3 C 206 GLN TYR ARG HIS LEU LEU LEU GLU ASP GLN ARG ILE ARG
SEQRES 4 C 206 GLY LEU LEU GLU LYS GLU LEU TYR SER ALA GLY LEU ALA
SEQRES 5 C 206 ARG VAL ASP ILE GLU ARG ALA ALA ASP ASN VAL ALA VAL
SEQRES 6 C 206 THR VAL HIS VAL ALA LYS PRO GLY VAL VAL ILE GLY ARG
SEQRES 7 C 206 GLY GLY GLU ARG ILE ARG VAL LEU ARG GLU GLU LEU ALA
SEQRES 8 C 206 LYS LEU THR GLY LYS ASN VAL ALA LEU ASN VAL GLN GLU
SEQRES 9 C 206 VAL GLN ASN PRO ASN LEU SER ALA PRO LEU VAL ALA GLN
SEQRES 10 C 206 ARG VAL ALA GLU GLN ILE GLU ARG ARG PHE ALA VAL ARG
SEQRES 11 C 206 ARG ALA ILE LYS GLN ALA VAL GLN ARG VAL MET GLU SER
SEQRES 12 C 206 GLY ALA LYS GLY ALA LYS VAL ILE VAL SER GLY ARG ILE
SEQRES 13 C 206 GLY GLY ALA GLU GLN ALA ARG THR GLU TRP ALA ALA GLN
SEQRES 14 C 206 GLY ARG VAL PRO LEU HIS THR LEU ARG ALA ASN ILE ASP
SEQRES 15 C 206 TYR GLY PHE ALA LEU ALA ARG THR THR TYR GLY VAL LEU
SEQRES 16 C 206 GLY VAL LYS ALA TYR ILE PHE LEU GLY GLU VAL
SEQRES 1 D 208 GLY ARG TYR ILE GLY PRO VAL CYS ARG LEU CYS ARG ARG
SEQRES 2 D 208 GLU GLY VAL LYS LEU TYR LEU LYS GLY GLU ARG CYS TYR
SEQRES 3 D 208 SER PRO LYS CYS ALA MET GLU ARG ARG PRO TYR PRO PRO
SEQRES 4 D 208 GLY GLN HIS GLY GLN LYS ARG ALA ARG ARG PRO SER ASP
SEQRES 5 D 208 TYR ALA VAL ARG LEU ARG GLU LYS GLN LYS LEU ARG ARG
SEQRES 6 D 208 ILE TYR GLY ILE SER GLU ARG GLN PHE ARG ASN LEU PHE
SEQRES 7 D 208 GLU GLU ALA SER LYS LYS LYS GLY VAL THR GLY SER VAL
SEQRES 8 D 208 PHE LEU GLY LEU LEU GLU SER ARG LEU ASP ASN VAL VAL
SEQRES 9 D 208 TYR ARG LEU GLY PHE ALA VAL SER ARG ARG GLN ALA ARG
SEQRES 10 D 208 GLN LEU VAL ARG HIS GLY HIS ILE THR VAL ASN GLY ARG
SEQRES 11 D 208 ARG VAL ASP LEU PRO SER TYR ARG VAL ARG PRO GLY ASP
SEQRES 12 D 208 GLU ILE ALA VAL ALA GLU LYS SER ARG ASN LEU GLU LEU
SEQRES 13 D 208 ILE ARG GLN ASN LEU GLU ALA MET LYS GLY ARG LYS VAL
SEQRES 14 D 208 GLY PRO TRP LEU SER LEU ASP VAL GLU GLY MET LYS GLY
SEQRES 15 D 208 LYS PHE LEU ARG LEU PRO ASP ARG GLU ASP LEU ALA LEU
SEQRES 16 D 208 PRO VAL ASN GLU GLN LEU VAL ILE GLU PHE TYR SER ARG
SEQRES 1 E 157 ASP PHE GLU GLU LYS MET ILE LEU ILE ARG ARG THR ALA
SEQRES 2 E 157 ARG MET GLN ALA GLY GLY ARG ARG PHE ARG PHE GLY ALA
SEQRES 3 E 157 LEU VAL VAL VAL GLY ASP ARG GLN GLY ARG VAL GLY LEU
SEQRES 4 E 157 GLY PHE GLY LYS ALA PRO GLU VAL PRO LEU ALA VAL GLN
SEQRES 5 E 157 LYS ALA GLY TYR TYR ALA ARG ARG ASN MET VAL GLU VAL
SEQRES 6 E 157 PRO LEU GLN ASN GLY THR ILE PRO HIS GLU ILE GLU VAL
SEQRES 7 E 157 GLU PHE GLY ALA SER LYS ILE VAL LEU LYS PRO ALA ALA
SEQRES 8 E 157 PRO GLY THR GLY VAL ILE ALA GLY ALA VAL PRO ARG ALA
SEQRES 9 E 157 ILE LEU GLU LEU ALA GLY VAL THR ASP ILE LEU THR LYS
SEQRES 10 E 157 GLU LEU GLY SER ARG ASN PRO ILE ASN ILE ALA TYR ALA
SEQRES 11 E 157 THR MET GLU ALA LEU ARG GLN LEU ARG THR LYS ALA ASP
SEQRES 12 E 157 VAL GLU ARG LEU ARG LYS GLY GLU ALA HIS ALA GLN ALA
SEQRES 13 E 157 GLN
SEQRES 1 F 101 MET ARG ARG TYR GLU VAL ASN ILE VAL LEU ASN PRO ASN
SEQRES 2 F 101 LEU ASP GLN SER GLN LEU ALA LEU GLU LYS GLU ILE ILE
SEQRES 3 F 101 GLN ARG ALA LEU GLU ASN TYR GLY ALA ARG VAL GLU LYS
SEQRES 4 F 101 VAL GLU GLU LEU GLY LEU ARG ARG LEU ALA TYR PRO ILE
SEQRES 5 F 101 ALA LYS ASP PRO GLN GLY TYR PHE LEU TRP TYR GLN VAL
SEQRES 6 F 101 GLU MET PRO GLU ASP ARG VAL ASN ASP LEU ALA ARG GLU
SEQRES 7 F 101 LEU ARG ILE ARG ASP ASN VAL ARG ARG VAL MET VAL VAL
SEQRES 8 F 101 LYS SER GLN GLU PRO PHE LEU ALA ASN ALA
SEQRES 1 G 155 ALA ARG ARG ARG ARG ALA GLU VAL ARG GLN LEU GLN PRO
SEQRES 2 G 155 ASP LEU VAL TYR GLY ASP VAL LEU VAL THR ALA PHE ILE
SEQRES 3 G 155 ASN LYS ILE MET ARG ASP GLY LYS LYS ASN LEU ALA ALA
SEQRES 4 G 155 ARG ILE PHE TYR ASP ALA CYS LYS ILE ILE GLN GLU LYS
SEQRES 5 G 155 THR GLY GLN GLU PRO LEU LYS VAL PHE LYS GLN ALA VAL
SEQRES 6 G 155 GLU ASN VAL LYS PRO ARG MET GLU VAL ARG SER ARG ARG
SEQRES 7 G 155 VAL GLY GLY ALA ASN TYR GLN VAL PRO MET GLU VAL SER
SEQRES 8 G 155 PRO ARG ARG GLN GLN SER LEU ALA LEU ARG TRP LEU VAL
SEQRES 9 G 155 GLN ALA ALA ASN GLN ARG PRO GLU ARG ARG ALA ALA VAL
SEQRES 10 G 155 ARG ILE ALA HIS GLU LEU MET ASP ALA ALA GLU GLY LYS
SEQRES 11 G 155 GLY GLY ALA VAL LYS LYS LYS GLU ASP VAL GLU ARG MET
SEQRES 12 G 155 ALA GLU ALA ASN ARG ALA TYR ALA HIS TYR ARG TRP
SEQRES 1 H 138 MET LEU THR ASP PRO ILE ALA ASP MET LEU THR ARG ILE
SEQRES 2 H 138 ARG ASN ALA THR ARG VAL TYR LYS GLU SER THR ASP VAL
SEQRES 3 H 138 PRO ALA SER ARG PHE LYS GLU GLU ILE LEU ARG ILE LEU
SEQRES 4 H 138 ALA ARG GLU GLY PHE ILE LYS GLY TYR GLU ARG VAL ASP
SEQRES 5 H 138 VAL ASP GLY LYS PRO TYR LEU ARG VAL TYR LEU LYS TYR
SEQRES 6 H 138 GLY PRO ARG ARG GLN GLY PRO ASP PRO ARG PRO GLU GLN
SEQRES 7 H 138 VAL ILE HIS HIS ILE ARG ARG ILE SER LYS PRO GLY ARG
SEQRES 8 H 138 ARG VAL TYR VAL GLY VAL LYS GLU ILE PRO ARG VAL ARG
SEQRES 9 H 138 ARG GLY LEU GLY ILE ALA ILE LEU SER THR SER LYS GLY
SEQRES 10 H 138 VAL LEU THR ASP ARG GLU ALA ARG LYS LEU GLY VAL GLY
SEQRES 11 H 138 GLY GLU LEU ILE CYS GLU VAL TRP
SEQRES 1 I 127 GLU GLN TYR TYR GLY THR GLY ARG ARG LYS GLU ALA VAL
SEQRES 2 I 127 ALA ARG VAL PHE LEU ARG PRO GLY ASN GLY LYS VAL THR
SEQRES 3 I 127 VAL ASN GLY GLN ASP PHE ASN GLU TYR PHE GLN GLY LEU
SEQRES 4 I 127 VAL ARG ALA VAL ALA ALA LEU GLU PRO LEU ARG ALA VAL
SEQRES 5 I 127 ASP ALA LEU GLY HIS PHE ASP ALA TYR ILE THR VAL ARG
SEQRES 6 I 127 GLY GLY GLY LYS SER GLY GLN ILE ASP ALA ILE LYS LEU
SEQRES 7 I 127 GLY ILE ALA ARG ALA LEU VAL GLN TYR ASN PRO ASP TYR
SEQRES 8 I 127 ARG ALA LYS LEU LYS PRO LEU GLY PHE LEU THR ARG ASP
SEQRES 9 I 127 ALA ARG VAL VAL GLU ARG LYS LYS TYR GLY LYS HIS LYS
SEQRES 10 I 127 ALA ARG ARG ALA PRO GLN TYR SER LYS ARG
SEQRES 1 J 99 LYS ILE ARG ILE LYS LEU ARG GLY PHE ASP HIS LYS THR
SEQRES 2 J 99 LEU ASP ALA SER ALA GLN LYS ILE VAL GLU ALA ALA ARG
SEQRES 3 J 99 ARG SER GLY ALA GLN VAL SER GLY PRO ILE PRO LEU PRO
SEQRES 4 J 99 THR ARG VAL ARG ARG PHE THR VAL ILE ARG GLY PRO PHE
SEQRES 5 J 99 LYS HIS LYS ASP SER ARG GLU HIS PHE GLU LEU ARG THR
SEQRES 6 J 99 HIS ASN ARG LEU VAL ASP ILE ILE ASN PRO ASN ARG LYS
SEQRES 7 J 99 THR ILE GLU GLN LEU MET THR LEU ASP LEU PRO THR GLY
SEQRES 8 J 99 VAL GLU ILE GLU ILE LYS THR VAL
SEQRES 1 K 115 LYS ARG GLN VAL ALA SER GLY ARG ALA TYR ILE HIS ALA
SEQRES 2 K 115 SER TYR ASN ASN THR ILE VAL THR ILE THR ASP PRO ASP
SEQRES 3 K 115 GLY ASN PRO ILE THR TRP SER SER GLY GLY VAL ILE GLY
SEQRES 4 K 115 TYR LYS GLY SER ARG LYS GLY THR PRO TYR ALA ALA GLN
SEQRES 5 K 115 LEU ALA ALA LEU ASP ALA ALA LYS LYS ALA MET ALA TYR
SEQRES 6 K 115 GLY MET GLN SER VAL ASP VAL ILE VAL ARG GLY THR GLY
SEQRES 7 K 115 ALA GLY ARG GLU GLN ALA ILE ARG ALA LEU GLN ALA SER
SEQRES 8 K 115 GLY LEU GLN VAL LYS SER ILE VAL ASP ASP THR PRO VAL
SEQRES 9 K 115 PRO HIS ASN GLY CYS ARG PRO LYS LYS LYS PHE
SEQRES 1 L 124 PRO THR ILE ASN GLN LEU VAL ARG LYS GLY ARG GLU LYS
SEQRES 2 L 124 VAL ARG LYS LYS SER LYS VAL PRO ALA LEU LYS GLY ALA
SEQRES 3 L 124 PRO PHE ARG ARG GLY VAL CYS THR VAL VAL ARG THR VAL
SEQRES 4 L 124 THR PRO LYS LYS PRO ASN SER ALA LEU ARG LYS VAL ALA
SEQRES 5 L 124 LYS VAL ARG LEU THR SER GLY TYR GLU VAL THR ALA TYR
SEQRES 6 L 124 ILE PRO GLY GLU GLY HIS ASN LEU GLN GLU HIS SER VAL
SEQRES 7 L 124 VAL LEU ILE ARG GLY GLY ARG VAL LYS ASP LEU PRO GLY
SEQRES 8 L 124 VAL ARG TYR HIS ILE VAL ARG GLY VAL TYR ASP ALA ALA
SEQRES 9 L 124 GLY VAL LYS ASP ARG LYS LYS SER ARG SER LYS TYR GLY
SEQRES 10 L 124 THR LYS LYS PRO LYS GLU ALA
SEQRES 1 M 119 ALA ARG ILE ALA GLY VAL GLU ILE PRO ARG ASN LYS ARG
SEQRES 2 M 119 VAL ASP VAL ALA LEU THR TYR ILE TYR GLY ILE GLY LYS
SEQRES 3 M 119 ALA ARG ALA LYS GLU ALA LEU GLU LYS THR GLY ILE ASN
SEQRES 4 M 119 PRO ALA THR ARG VAL LYS ASP LEU THR GLU ALA GLU VAL
SEQRES 5 M 119 VAL ARG LEU ARG GLU TYR VAL GLU ASN THR TRP LYS LEU
SEQRES 6 M 119 GLU GLY GLU LEU ARG ALA GLU VAL ALA ALA ASN ILE LYS
SEQRES 7 M 119 ARG LEU MET ASP ILE GLY CYS TYR ARG GLY LEU ARG HIS
SEQRES 8 M 119 ARG ARG GLY LEU PRO VAL ARG GLY GLN ARG THR ARG THR
SEQRES 9 M 119 ASN ALA ARG THR ARG LYS GLY PRO ARG LYS THR VAL ALA
SEQRES 10 M 119 GLY 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 85 MET VAL LYS ILE ARG LEU ALA ARG PHE GLY SER LYS HIS
SEQRES 2 P 85 ASN PRO HIS TYR ARG ILE VAL VAL THR ASP ALA ARG ARG
SEQRES 3 P 85 LYS ARG ASP GLY LYS TYR ILE GLU LYS ILE GLY TYR TYR
SEQRES 4 P 85 ASP PRO ARG LYS THR THR PRO ASP TRP LEU LYS VAL ASP
SEQRES 5 P 85 VAL GLU ARG ALA ARG TYR TRP LEU SER VAL GLY ALA GLN
SEQRES 6 P 85 PRO THR ASP THR ALA ARG ARG LEU LEU ARG GLN ALA GLY
SEQRES 7 P 85 VAL PHE ARG GLN GLU ALA ARG
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 73 PRO SER ARG LYS ALA LYS VAL LYS ALA THR LEU GLY GLU
SEQRES 2 R 73 PHE ASP LEU ARG ASP TYR ARG ASN VAL GLU VAL LEU LYS
SEQRES 3 R 73 ARG PHE LEU SER GLU THR GLY LYS ILE LEU PRO ARG ARG
SEQRES 4 R 73 ARG THR GLY LEU SER ALA LYS GLU GLN ARG ILE LEU ALA
SEQRES 5 R 73 LYS THR ILE LYS ARG ALA ARG ILE LEU GLY LEU LEU PRO
SEQRES 6 R 73 PHE THR GLU LYS LEU VAL ARG LYS
SEQRES 1 S 83 PRO ARG SER LEU LYS LYS GLY VAL PHE VAL ASP ASP HIS
SEQRES 2 S 83 LEU LEU GLU LYS VAL LEU GLU LEU ASN ALA LYS GLY GLU
SEQRES 3 S 83 LYS ARG LEU ILE LYS THR TRP SER ARG ARG SER THR ILE
SEQRES 4 S 83 VAL PRO GLU MET VAL GLY HIS THR ILE ALA VAL TYR ASN
SEQRES 5 S 83 GLY LYS GLN HIS VAL PRO VAL TYR ILE THR GLU ASN MET
SEQRES 6 S 83 VAL GLY HIS LYS LEU GLY GLU PHE ALA PRO THR ARG THR
SEQRES 7 S 83 TYR ARG GLY HIS GLY
SEQRES 1 T 99 ARG ASN LEU SER ALA LEU LYS ARG HIS ARG GLN SER LEU
SEQRES 2 T 99 LYS ARG ARG LEU ARG ASN LYS ALA LYS LYS SER ALA ILE
SEQRES 3 T 99 LYS THR LEU SER LYS LYS ALA ILE GLN LEU ALA GLN GLU
SEQRES 4 T 99 GLY LYS ALA GLU GLU ALA LEU LYS ILE MET ARG LYS ALA
SEQRES 5 T 99 GLU SER LEU ILE ASP LYS ALA ALA LYS GLY SER THR LEU
SEQRES 6 T 99 HIS LYS ASN ALA ALA ALA ARG ARG LYS SER ARG LEU MET
SEQRES 7 T 99 ARG LYS VAL ARG GLN LEU LEU GLU ALA ALA GLY ALA PRO
SEQRES 8 T 99 LEU ILE GLY GLY GLY LEU SER ALA
SEQRES 1 V 24 GLY LYS GLY ASP ARG ARG THR ARG ARG GLY LYS ILE TRP
SEQRES 2 V 24 ARG GLY THR TYR GLY LYS TYR ARG PRO ARG LYS
HET T1C A1601 42
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 ZN D 301 1
HET MG E 201 1
HET ZN N 101 1
HETNAM T1C TIGECYCLINE
HETNAM MG MAGNESIUM ION
HETNAM ZN ZINC ION
FORMUL 22 T1C C29 H41 N5 O8 2+
FORMUL 23 MG 103(MG 2+)
FORMUL 25 ZN 2(ZN 2+)
HELIX 1 AA1 THR B 6 GLY B 14 1 9
HELIX 2 AA2 ASN B 25 ILE B 32 5 8
HELIX 3 AA3 ASP B 43 THR B 47 5 5
HELIX 4 AA4 MET B 48 ARG B 64 1 17
HELIX 5 AA5 ALA B 77 GLU B 86 1 10
HELIX 6 AA6 ASN B 104 GLN B 110 1 7
HELIX 7 AA7 VAL B 112 SER B 124 1 13
HELIX 8 AA8 PRO B 125 ARG B 130 1 6
HELIX 9 AA9 PRO B 131 SER B 150 1 20
HELIX 10 AB1 ILE B 172 LEU B 180 1 9
HELIX 11 AB2 ARG B 209 VAL B 219 1 11
HELIX 12 AB3 VAL B 219 GLN B 224 1 6
HELIX 13 AB4 ALA B 225 GLY B 227 5 3
HELIX 14 AB5 PRO C 7 ARG C 11 5 5
HELIX 15 AB6 GLY C 25 TYR C 48 1 24
HELIX 16 AB7 SER C 49 GLY C 51 5 3
HELIX 17 AB8 LYS C 72 VAL C 76 5 5
HELIX 18 AB9 ARG C 83 GLU C 89 1 7
HELIX 19 AC1 SER C 112 ARG C 126 1 15
HELIX 20 AC2 ALA C 129 MET C 142 1 14
HELIX 21 AC3 GLU D 24 SER D 28 5 5
HELIX 22 AC4 CYS D 31 ARG D 35 5 5
HELIX 23 AC5 SER D 52 ILE D 67 1 16
HELIX 24 AC6 SER D 71 LYS D 84 1 14
HELIX 25 AC7 VAL D 88 LEU D 96 1 9
HELIX 26 AC8 LEU D 101 TYR D 106 1 6
HELIX 27 AC9 SER D 113 HIS D 123 1 11
HELIX 28 AD1 ALA D 149 ASN D 154 1 6
HELIX 29 AD2 LEU D 155 MET D 165 1 11
HELIX 30 AD3 VAL D 178 MET D 181 5 4
HELIX 31 AD4 GLU D 200 GLU D 205 1 6
HELIX 32 AD5 GLU E 50 ASN E 65 1 16
HELIX 33 AD6 GLY E 103 VAL E 115 1 13
HELIX 34 AD7 ASN E 127 GLN E 141 1 15
HELIX 35 AD8 LYS E 153 HIS E 157 5 5
HELIX 36 AD9 ASP F 15 TYR F 33 1 19
HELIX 37 AE1 PRO F 68 ASP F 70 5 3
HELIX 38 AE2 ARG F 71 ARG F 80 1 10
HELIX 39 AE3 ASP G 20 MET G 31 1 12
HELIX 40 AE4 LYS G 35 THR G 54 1 20
HELIX 41 AE5 GLU G 57 ASN G 68 1 12
HELIX 42 AE6 SER G 92 ARG G 111 1 20
HELIX 43 AE7 ARG G 115 ASP G 126 1 12
HELIX 44 AE8 LYS G 131 GLU G 139 1 9
HELIX 45 AE9 GLU G 142 ALA G 147 1 6
HELIX 46 AF1 ASN G 148 ALA G 152 5 5
HELIX 47 AF2 ASP H 4 ARG H 18 1 15
HELIX 48 AF3 ARG H 30 GLU H 42 1 13
HELIX 49 AF4 VAL H 103 LEU H 107 5 5
HELIX 50 AF5 ASP H 121 GLY H 128 1 8
HELIX 51 AF6 ARG I 42 ARG I 51 5 10
HELIX 52 AF7 GLY I 69 LEU I 85 1 17
HELIX 53 AF8 LYS J 14 VAL J 24 1 11
HELIX 54 AF9 GLY K 45 GLY K 49 1 5
HELIX 55 AG1 GLY K 52 GLY K 56 5 5
HELIX 56 AG2 THR K 57 ALA K 74 1 18
HELIX 57 AG3 GLY K 90 ALA K 100 1 11
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 GLU M 32 1 7
HELIX 61 AG7 GLU M 50 THR M 63 1 14
HELIX 62 AG8 LEU M 66 ILE M 84 1 19
HELIX 63 AG9 CYS M 86 GLY M 95 1 10
HELIX 64 AH1 ALA M 107 GLY M 112 1 6
HELIX 65 AH2 LYS N 4 ARG N 12 1 9
HELIX 66 AH3 PHE N 16 ALA N 20 5 5
HELIX 67 AH4 CYS N 40 HIS N 49 1 10
HELIX 68 AH5 THR O 4 GLU O 14 1 11
HELIX 69 AH6 SER O 24 HIS O 46 1 23
HELIX 70 AH7 ASP O 49 ASP O 74 1 26
HELIX 71 AH8 PRO O 75 LYS O 84 1 10
HELIX 72 AH9 ASP P 52 ARG P 57 1 6
HELIX 73 AI1 TYR P 58 GLY P 63 1 6
HELIX 74 AI2 ASP P 68 GLN P 76 1 9
HELIX 75 AI3 ARG Q 81 ASN Q 94 1 14
HELIX 76 AI4 TYR Q 95 SER Q 97 5 3
HELIX 77 AI5 PRO R 52 GLY R 57 1 6
HELIX 78 AI6 LYS R 61 ILE R 70 1 10
HELIX 79 AI7 LYS R 71 LEU R 76 1 6
HELIX 80 AI8 ASP S 12 LYS S 18 1 7
HELIX 81 AI9 LYS S 70 ALA S 75 5 6
HELIX 82 AJ1 SER T 11 GLU T 46 1 36
HELIX 83 AJ2 LYS T 48 GLY T 69 1 22
HELIX 84 AJ3 HIS T 73 LEU T 92 1 20
HELIX 85 AJ4 THR V 8 GLY V 16 1 9
SHEET 1 AA1 5 TYR B 92 VAL B 93 0
SHEET 2 AA1 5 ILE B 68 VAL B 71 1 N PHE B 70 O VAL B 93
SHEET 3 AA1 5 ALA B 161 VAL B 165 1 O PHE B 163 N VAL B 71
SHEET 4 AA1 5 VAL B 184 ALA B 188 1 O ILE B 185 N ILE B 162
SHEET 5 AA1 5 TYR B 199 PRO B 202 1 O ILE B 201 N ALA B 186
SHEET 1 AA2 2 ILE C 57 ALA C 60 0
SHEET 2 AA2 2 ASN C 63 VAL C 66 -1 O ASN C 63 N ALA C 60
SHEET 1 AA3 2 HIS C 69 VAL C 70 0
SHEET 2 AA3 2 GLN C 104 GLU C 105 1 O GLN C 104 N VAL C 70
SHEET 1 AA4 4 ALA C 168 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 VAL C 198 GLU C 206 -1 O LYS C 199 N ILE C 152
SHEET 4 AA4 4 ALA C 180 TYR C 184 -1 N ASN C 181 O LEU C 204
SHEET 1 AA5 2 ARG C 190 THR C 191 0
SHEET 2 AA5 2 GLY C 194 VAL C 195 -1 O GLY C 194 N THR C 191
SHEET 1 AA6 2 LEU D 174 LEU D 176 0
SHEET 2 AA6 2 GLY D 183 PHE D 185 -1 O LYS D 184 N SER D 175
SHEET 1 AA7 3 MET E 10 ALA E 17 0
SHEET 2 AA7 3 PHE E 26 VAL E 32 -1 O LEU E 31 N LEU E 12
SHEET 3 AA7 3 GLY E 44 ALA E 48 -1 O GLY E 46 N ALA E 30
SHEET 1 AA8 3 ILE E 80 PHE E 84 0
SHEET 2 AA8 3 SER E 87 PRO E 93 -1 O LEU E 91 N ILE E 80
SHEET 3 AA8 3 ILE E 118 LEU E 119 -1 O LEU E 119 N LYS E 92
SHEET 1 AA9 4 VAL F 40 ILE F 52 0
SHEET 2 AA9 4 ASP F 55 TYR F 63 -1 O PHE F 60 N GLY F 44
SHEET 3 AA9 4 GLU F 5 LEU F 10 -1 N LEU F 10 O TYR F 59
SHEET 4 AA9 4 VAL F 85 VAL F 91 -1 O MET F 89 N ASN F 7
SHEET 1 AB1 2 LEU F 98 ALA F 99 0
SHEET 2 AB1 2 PHE R 29 ASP R 30 -1 O PHE R 29 N ALA F 99
SHEET 1 AB2 2 MET G 73 VAL G 75 0
SHEET 2 AB2 2 PRO G 88 GLU G 90 -1 O MET G 89 N GLU G 74
SHEET 1 AB3 2 ARG G 78 ARG G 79 0
SHEET 2 AB3 2 ASN G 84 TYR G 85 -1 O TYR G 85 N ARG G 78
SHEET 1 AB4 3 SER H 23 VAL H 26 0
SHEET 2 AB4 3 LEU H 59 LEU H 63 -1 O LEU H 59 N VAL H 26
SHEET 3 AB4 3 ILE H 45 ARG H 50 -1 N GLU H 49 O ARG H 60
SHEET 1 AB5 4 TYR H 94 VAL H 95 0
SHEET 2 AB5 4 GLY H 131 VAL H 137 -1 O GLY H 131 N VAL H 95
SHEET 3 AB5 4 ILE H 109 THR H 114 -1 N ILE H 111 O ILE H 134
SHEET 4 AB5 4 GLY H 117 THR H 120 -1 O LEU H 119 N LEU H 112
SHEET 1 AB6 4 TYR I 4 ARG I 9 0
SHEET 2 AB6 4 ALA I 13 LEU I 19 -1 O ALA I 15 N GLY I 8
SHEET 3 AB6 4 ALA I 61 GLY I 67 -1 O THR I 64 N ARG I 16
SHEET 4 AB6 4 VAL I 26 VAL I 28 1 N THR I 27 O ALA I 61
SHEET 1 AB7 3 GLN J 33 SER J 35 0
SHEET 2 AB7 3 ARG J 60 ILE J 75 -1 O ILE J 75 N GLN J 33
SHEET 3 AB7 3 ARG J 43 ILE J 50 -1 N VAL J 49 O GLU J 61
SHEET 1 AB8 4 GLN J 33 SER J 35 0
SHEET 2 AB8 4 ARG J 60 ILE J 75 -1 O ILE J 75 N GLN J 33
SHEET 3 AB8 4 ILE J 4 GLY J 10 -1 N LEU J 8 O ARG J 70
SHEET 4 AB8 4 ILE J 96 THR J 100 -1 O LYS J 99 N ARG J 5
SHEET 1 AB9 5 THR K 41 SER K 44 0
SHEET 2 AB9 5 THR K 28 THR K 33 -1 N VAL K 30 O SER K 43
SHEET 3 AB9 5 SER K 16 ALA K 23 -1 N HIS K 22 O ILE K 29
SHEET 4 AB9 5 SER K 79 ARG K 85 1 O ARG K 85 N ILE K 21
SHEET 5 AB9 5 GLN K 104 ASP K 110 1 O LYS K 106 N VAL K 80
SHEET 1 AC1 5 VAL L 36 THR L 42 0
SHEET 2 AC1 5 LYS L 54 ARG L 59 -1 O VAL L 55 N ARG L 41
SHEET 3 AC1 5 GLU L 65 TYR L 69 -1 O VAL L 66 N VAL L 58
SHEET 4 AC1 5 TYR L 98 ILE L 100 1 O TYR L 98 N TYR L 69
SHEET 5 AC1 5 ILE L 85 ARG L 86 -1 N ARG L 86 O HIS L 99
SHEET 1 AC2 2 ARG M 3 ILE M 4 0
SHEET 2 AC2 2 VAL M 7 GLU M 8 -1 O VAL M 7 N ILE M 4
SHEET 1 AC3 5 LEU P 49 LYS P 50 0
SHEET 2 AC3 5 GLU P 34 TYR P 39 -1 N TYR P 38 O LYS P 50
SHEET 3 AC3 5 TYR P 17 ASP P 23 -1 N ILE P 19 O GLY P 37
SHEET 4 AC3 5 VAL P 2 ARG P 8 -1 N LYS P 3 O THR P 22
SHEET 5 AC3 5 GLN P 65 PRO P 66 1 O GLN P 65 N ILE P 4
SHEET 1 AC4 7 VAL Q 35 LYS Q 41 0
SHEET 2 AC4 7 THR Q 18 PRO Q 28 -1 N PHE Q 27 O ILE Q 36
SHEET 3 AC4 7 ALA Q 44 HIS Q 45 -1 O ALA Q 44 N VAL Q 19
SHEET 4 AC4 7 LYS Q 69 GLU Q 78 1 O PHE Q 71 N HIS Q 45
SHEET 5 AC4 7 VAL Q 56 SER Q 66 -1 N VAL Q 56 O GLU Q 78
SHEET 6 AC4 7 VAL Q 5 SER Q 12 -1 N GLY Q 8 O VAL Q 57
SHEET 7 AC4 7 THR Q 18 PRO Q 28 -1 O THR Q 20 N VAL Q 11
SHEET 1 AC5 3 LEU S 30 LYS S 32 0
SHEET 2 AC5 3 THR S 48 ASN S 53 1 O ALA S 50 N ILE S 31
SHEET 3 AC5 3 GLN S 56 TYR S 61 -1 O VAL S 58 N VAL S 51
SSBOND 1 CYS D 9 CYS D 12 1555 1555 2.03
SSBOND 2 CYS D 9 CYS D 31 1555 1555 2.02
SSBOND 3 CYS D 12 CYS D 31 1555 1555 2.03
SSBOND 4 CYS D 26 CYS D 31 1555 1555 2.05
LINK OP1 G A 21 MG MG A1603 1555 1555 2.74
LINK OP2 C A 48 MG MG A1611 1555 1555 2.85
LINK OP2 A A 53 MG MG A1608 1555 1555 2.80
LINK OP2 A A 195 MG MG A1616 1555 1555 2.72
LINK OP2 G A 289 MG MG A1618 1555 1555 2.63
LINK OP1 G A 297 MG MG A1620 1555 1555 2.97
LINK O6 G A 299 MG MG A1635 1555 1555 2.41
LINK OP2 C A 307 MG MG A1621 1555 1555 2.82
LINK OP2 C A 308 MG MG A1621 1555 1555 2.81
LINK OP1 A A 315 MG MG A1622 1555 1555 2.68
LINK OP2 C A 352 MG MG A1624 1555 1555 2.69
LINK OP1 G A 450 MG MG A1628 1555 1555 2.99
LINK OP2 A A 452 MG MG A1628 1555 1555 2.92
LINK OP1 G A 506 MG MG A1630 1555 1555 2.82
LINK OP2 A A 509 MG MG A1630 1555 1555 2.84
LINK OP2 A A 510 MG MG A1630 1555 1555 2.76
LINK OP1 A A 533 MG MG A1631 1555 1555 2.78
LINK OP1 A A 547 MG MG A1634 1555 1555 2.82
LINK OP1 G A 558 MG MG A1635 1555 1555 2.47
LINK OP1 C A 562 MG MG A1636 1555 1555 2.89
LINK OP1 A A 572 MG MG A1637 1555 1555 2.69
LINK OP2 A A 572 MG MG A1638 1555 1555 2.58
LINK OP2 A A 573 MG MG A1638 1555 1555 2.75
LINK OP2 A A 574 MG MG A1638 1555 1555 2.87
LINK OP1 C A 578 MG MG A1665 1555 1555 2.60
LINK O6 G A 581 MG MG A1640 1555 1555 2.72
LINK OP2 C A 596 MG MG A1643 1555 1555 2.64
LINK OP2 G A 597 MG MG A1643 1555 1555 2.68
LINK O4 U A 598 MG MG A1643 1555 1555 2.62
LINK OP2 A A 608 MG MG A1644 1555 1555 2.62
LINK OP1 G A 610 MG MG A1645 1555 1555 2.84
LINK OP2 G A 625 MG MG A1645 1555 1555 2.73
LINK OP2 C A 645 MG MG A1641 1555 1555 2.92
LINK OP2 C A 749 MG MG A1656 1555 1555 2.91
LINK OP2 G A 750 MG MG A1656 1555 1555 2.85
LINK OP2 A A 766 MG MG A1658 1555 1555 2.66
LINK OP2 A A 768 MG MG A1659 1555 1555 2.73
LINK O6 G A 771 MG MG A1663 1555 1555 2.95
LINK OP1 A A 782 MG MG A1662 1555 1555 2.85
LINK OP2 A A 860 MG MG A1668 1555 1555 2.84
LINK OP1 C A 904 MG MG A1671 1555 1555 2.99
LINK OP1 C A 934 MG MG A1672 1555 1555 2.75
LINK O5' C A 934 MG MG A1672 1555 1555 2.89
LINK OP2 A A 937 MG MG A1673 1555 1555 2.75
LINK O6 G A 939 MG MG A1673 1555 1555 2.99
LINK OP1 A A 964 MG MG A1675 1555 1555 2.57
LINK OP1 G A 966 MG MG A1702 1555 1555 2.28
LINK OP1 C A 972 MG MG A1676 1555 1555 2.83
LINK OP1 C A 979 MG MG A1690 1555 1555 2.96
LINK OP2 C A 980 MG MG A1690 1555 1555 2.71
LINK OP2 C A1054 MG MG A1677 1555 1555 2.16
LINK OP1 C A1054 MG MG A1688 1555 1555 2.20
LINK OP1 G A1068 MG MG A1682 1555 1555 2.99
LINK OP2 C A1069 MG MG A1679 1555 1555 2.66
LINK O2 U A1085 MG MG A1679 1555 1555 2.83
LINK OP2 U A1085 MG MG A1684 1555 1555 2.87
LINK OP1 G A1094 MG MG A1682 1555 1555 2.74
LINK OP2 U A1095 MG MG A1683 1555 1555 2.77
LINK O6 G A1108 MG MG A1683 1555 1555 2.77
LINK OP2 A A1110 MG MG A1685 1555 1555 2.69
LINK OP2 G A1197 MG MG A1677 1555 1555 2.03
LINK OP1 G A1197 MG MG A1688 1555 1555 2.70
LINK OP2 G A1198 MG MG A1688 1555 1555 2.12
LINK OP1 U A1199 MG MG A1675 1555 1555 2.84
LINK O6 G A1221 MG MG A1690 1555 1555 2.83
LINK O6 G A1222 MG MG A1690 1555 1555 2.80
LINK OP2 A A1238 MG MG A1694 1555 1555 2.77
LINK O5' A A1238 MG MG A1694 1555 1555 2.99
LINK OP2 G A1304 MG MG A1703 1555 1555 2.73
LINK O6 G A1370 MG MG A1697 1555 1555 2.74
LINK O3' U A1498 MG MG A1699 1555 1555 2.82
LINK OP2 A A1499 MG MG A1699 1555 1555 2.81
LINK OP2 A A1500 MG MG A1699 1555 1555 2.82
LINK OP1 A A1500 MG MG A1700 1555 1555 2.72
LINK OP1 G A1504 MG MG A1700 1555 1555 2.85
LINK OP1 G A1505 MG MG A1700 1555 1555 2.84
LINK OP1 G A1508 MG MG A1700 1555 1555 2.90
LINK O12 T1C A1601 MG MG A1688 1555 1555 2.28
LINK O11 T1C A1601 MG MG A1688 1555 1555 2.09
LINK O21 T1C A1601 MG MG A1702 1555 1555 2.03
LINK MG MG A1703 OD2 ASP V 5 1555 1555 2.98
LINK SG CYS D 9 ZN ZN D 301 1555 1555 2.86
LINK SG CYS D 26 ZN ZN D 301 1555 1555 2.45
LINK SG CYS D 31 ZN ZN D 301 1555 1555 2.69
LINK SG CYS N 24 ZN ZN N 101 1555 1555 2.83
LINK SG CYS N 27 ZN ZN N 101 1555 1555 2.66
LINK SG CYS N 40 ZN ZN N 101 1555 1555 2.79
SITE 1 AC1 10 U A 531 A A 965 G A 966 G A1053
SITE 2 AC1 10 C A1054 C A1195 G A1197 G A1198
SITE 3 AC1 10 MG A1688 MG A1702
SITE 1 AC2 3 U A 13 U A 14 A A 16
SITE 1 AC3 2 G A 21 G A 567
SITE 1 AC4 2 U A 37 G A 38
SITE 1 AC5 1 G A 41
SITE 1 AC6 2 A A 53 A A 353
SITE 1 AC7 2 U A 95 G A 96
SITE 1 AC8 2 G A 111 G A 112
SITE 1 AC9 4 C A 47 C A 48 A A 51 G A 115
SITE 1 AD1 1 U A 173
SITE 1 AD2 1 A A 151
SITE 1 AD3 2 C A 174 C A 175
SITE 1 AD4 3 A A 179 G A 181 A A 195
SITE 1 AD5 2 G A 285 G A 286
SITE 1 AD6 4 A A 116 G A 117 A A 288 G A 289
SITE 1 AD7 3 C A 290 C A 291 G A 305
SITE 1 AD8 2 G A 297 A A 298
SITE 1 AD9 2 C A 307 C A 308
SITE 1 AE1 1 A A 315
SITE 1 AE2 2 U A 323 G A 324
SITE 1 AE3 2 C A 330 C A 352
SITE 1 AE4 1 G A 376
SITE 1 AE5 2 G A 35 C A 398
SITE 1 AE6 3 G A 409 G A 410 A A 431
SITE 1 AE7 2 G A 450 A A 452
SITE 1 AE8 1 G A 492
SITE 1 AE9 3 G A 506 A A 509 A A 510
SITE 1 AF1 4 C A 514 G A 515 U A 516 A A 533
SITE 1 AF2 1 C A 536
SITE 1 AF3 1 C A 536
SITE 1 AF4 3 G A 402 A A 547 G A 548
SITE 1 AF5 3 A A 298 G A 299 G A 558
SITE 1 AF6 2 U A 560 C A 562
SITE 1 AF7 1 A A 572
SITE 1 AF8 4 U A 571 A A 572 A A 573 A A 574
SITE 1 AF9 2 G A 576 G A 577
SITE 1 AG1 2 G A 581 G A 758
SITE 1 AG2 2 G A 588 C A 645
SITE 1 AG3 4 G A 595 C A 596 G A 597 U A 598
SITE 1 AG4 2 A A 608 G A 610
SITE 1 AG5 3 G A 610 C A 624 G A 625
SITE 1 AG6 1 C A 620
SITE 1 AG7 1 C A 612
SITE 1 AG8 2 U A 636 MG A1649
SITE 1 AG9 3 G A 637 G A 638 MG A1648
SITE 1 AH1 1 G A 595
SITE 1 AH2 2 G A 649 G A 650
SITE 1 AH3 1 G A 683
SITE 1 AH4 1 G A 730
SITE 1 AH5 3 C A 748 C A 749 G A 750
SITE 1 AH6 3 A A 766 C A 811 C A 812
SITE 1 AH7 2 A A 767 A A 768
SITE 1 AH8 2 G A 773 G A 774
SITE 1 AH9 3 C A 797 G A 798 G A 799
SITE 1 AI1 5 A A 782 C A 783 U A 793 A A 794
SITE 2 AI1 5 C A1515
SITE 1 AI2 2 G A 771 U A 804
SITE 1 AI3 2 G A 576 C A 578
SITE 1 AI4 3 C A 857 G A 858 G A 869
SITE 1 AI5 2 A A 860 G A 861
SITE 1 AI6 2 A A 864 GLU E 83
SITE 1 AI7 3 U A 813 A A 814 C A 904
SITE 1 AI8 2 C A 934 U A1345
SITE 1 AI9 2 A A 937 G A 939
SITE 1 AJ1 2 G A 963 C A1200
SITE 1 AJ2 2 A A 964 U A1199
SITE 1 AJ3 2 C A 972 ASP J 58
SITE 1 AJ4 4 G A1053 C A1054 G A1197 G A1198
SITE 1 AJ5 2 C A1066 A A1067
SITE 1 AJ6 2 C A1069 U A1085
SITE 1 AJ7 2 G A1077 G A1079
SITE 1 AJ8 1 U A1086
SITE 1 AJ9 3 G A1068 G A1094 G A1387
SITE 1 AK1 2 U A1095 G A1108
SITE 1 AK2 2 U A1085 C A1103
SITE 1 AK3 2 A A1110 C A1189
SITE 1 AK4 4 C A1054 G A1197 G A1198 T1C A1601
SITE 1 AK5 1 A A1204
SITE 1 AK6 5 C A 979 C A 980 U A 981 G A1221
SITE 2 AK6 5 G A1222
SITE 1 AK7 2 G A 951 G A1224
SITE 1 AK8 2 G A1265 G A1266
SITE 1 AK9 1 G A1271
SITE 1 AL1 2 A A1238 C A1335
SITE 1 AL2 1 G A1355
SITE 1 AL3 2 C A 980 A A1360
SITE 1 AL4 1 G A1370
SITE 1 AL5 5 U A1498 A A1499 A A1500 G A1504
SITE 2 AL5 5 G A1505
SITE 1 AL6 5 A A1500 G A1504 G A1505 A A1507
SITE 2 AL6 5 G A1508
SITE 1 AL7 1 G A1526
SITE 1 AL8 2 G A 966 T1C A1601
SITE 1 AL9 3 C A1303 G A1304 ASP V 5
SITE 1 AM1 6 CYS D 9 CYS D 12 LEU D 19 LYS D 22
SITE 2 AM1 6 CYS D 26 CYS D 31
SITE 1 AM2 2 G A 21 GLY E 124
SITE 1 AM3 4 CYS N 24 CYS N 27 CYS N 40 CYS N 43
CRYST1 409.590 409.590 171.730 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 0.002441 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002441 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005823 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
