HEADER RIBOSOME/ANTIBIOTIC 07-NOV-10 3PIP
TITLE CRYSTAL STRUCTURE OF THE SYNERGISTIC ANTIBIOTIC PAIR LANKAMYCIN AND
TITLE 2 LANKACIDIN IN COMPLEX WITH THE LARGE RIBOSOMAL SUBUNIT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RIBOSOMAL 23S RNA;
COMPND 3 CHAIN: X;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: 5S RIBOSOMAL RNA;
COMPND 6 CHAIN: Y;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: 50S RIBOSOMAL PROTEIN L2;
COMPND 9 CHAIN: A;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: 50S RIBOSOMAL PROTEIN L3;
COMPND 12 CHAIN: B;
COMPND 13 MOL_ID: 5;
COMPND 14 MOLECULE: 50S RIBOSOMAL PROTEIN L4;
COMPND 15 CHAIN: C;
COMPND 16 MOL_ID: 6;
COMPND 17 MOLECULE: 50S RIBOSOMAL PROTEIN L5;
COMPND 18 CHAIN: D;
COMPND 19 MOL_ID: 7;
COMPND 20 MOLECULE: 50S RIBOSOMAL PROTEIN L6;
COMPND 21 CHAIN: E;
COMPND 22 MOL_ID: 8;
COMPND 23 MOLECULE: 50S RIBOSOMAL PROTEIN L11;
COMPND 24 CHAIN: F;
COMPND 25 MOL_ID: 9;
COMPND 26 MOLECULE: 50S RIBOSOMAL PROTEIN L13;
COMPND 27 CHAIN: G;
COMPND 28 MOL_ID: 10;
COMPND 29 MOLECULE: 50S RIBOSOMAL PROTEIN L14;
COMPND 30 CHAIN: H;
COMPND 31 MOL_ID: 11;
COMPND 32 MOLECULE: 50S RIBOSOMAL PROTEIN L15;
COMPND 33 CHAIN: I;
COMPND 34 MOL_ID: 12;
COMPND 35 MOLECULE: 50S RIBOSOMAL PROTEIN L16;
COMPND 36 CHAIN: J;
COMPND 37 MOL_ID: 13;
COMPND 38 MOLECULE: 50S RIBOSOMAL PROTEIN L17;
COMPND 39 CHAIN: K;
COMPND 40 MOL_ID: 14;
COMPND 41 MOLECULE: 50S RIBOSOMAL PROTEIN L18;
COMPND 42 CHAIN: L;
COMPND 43 MOL_ID: 15;
COMPND 44 MOLECULE: 50S RIBOSOMAL PROTEIN L19;
COMPND 45 CHAIN: M;
COMPND 46 MOL_ID: 16;
COMPND 47 MOLECULE: 50S RIBOSOMAL PROTEIN L20;
COMPND 48 CHAIN: N;
COMPND 49 MOL_ID: 17;
COMPND 50 MOLECULE: 50S RIBOSOMAL PROTEIN L21;
COMPND 51 CHAIN: O;
COMPND 52 MOL_ID: 18;
COMPND 53 MOLECULE: 50S RIBOSOMAL PROTEIN L22;
COMPND 54 CHAIN: P;
COMPND 55 MOL_ID: 19;
COMPND 56 MOLECULE: 50S RIBOSOMAL PROTEIN L23;
COMPND 57 CHAIN: Q;
COMPND 58 MOL_ID: 20;
COMPND 59 MOLECULE: 50S RIBOSOMAL PROTEIN L24;
COMPND 60 CHAIN: R;
COMPND 61 MOL_ID: 21;
COMPND 62 MOLECULE: 50S RIBOSOMAL PROTEIN L25;
COMPND 63 CHAIN: S;
COMPND 64 SYNONYM: GENERAL STRESS PROTEIN CTC;
COMPND 65 MOL_ID: 22;
COMPND 66 MOLECULE: 50S RIBOSOMAL PROTEIN L27;
COMPND 67 CHAIN: T;
COMPND 68 MOL_ID: 23;
COMPND 69 MOLECULE: 50S RIBOSOMAL PROTEIN L28;
COMPND 70 CHAIN: U;
COMPND 71 MOL_ID: 24;
COMPND 72 MOLECULE: 50S RIBOSOMAL PROTEIN L29;
COMPND 73 CHAIN: V;
COMPND 74 MOL_ID: 25;
COMPND 75 MOLECULE: 50S RIBOSOMAL PROTEIN L30;
COMPND 76 CHAIN: W;
COMPND 77 MOL_ID: 26;
COMPND 78 MOLECULE: 50S RIBOSOMAL PROTEIN L32;
COMPND 79 CHAIN: Z;
COMPND 80 MOL_ID: 27;
COMPND 81 MOLECULE: 50S RIBOSOMAL PROTEIN L33;
COMPND 82 CHAIN: 1;
COMPND 83 MOL_ID: 28;
COMPND 84 MOLECULE: 50S RIBOSOMAL PROTEIN L34;
COMPND 85 CHAIN: 2;
COMPND 86 MOL_ID: 29;
COMPND 87 MOLECULE: 50S RIBOSOMAL PROTEIN L35;
COMPND 88 CHAIN: 3;
COMPND 89 MOL_ID: 30;
COMPND 90 MOLECULE: 50S RIBOSOMAL PROTEIN L36;
COMPND 91 CHAIN: 4
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS R1;
SOURCE 3 ORGANISM_TAXID: 243230;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS R1;
SOURCE 6 ORGANISM_TAXID: 243230;
SOURCE 7 MOL_ID: 3;
SOURCE 8 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 9 ORGANISM_TAXID: 1299;
SOURCE 10 MOL_ID: 4;
SOURCE 11 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 12 ORGANISM_TAXID: 1299;
SOURCE 13 MOL_ID: 5;
SOURCE 14 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 15 ORGANISM_TAXID: 1299;
SOURCE 16 MOL_ID: 6;
SOURCE 17 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 18 ORGANISM_TAXID: 1299;
SOURCE 19 MOL_ID: 7;
SOURCE 20 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 21 ORGANISM_TAXID: 1299;
SOURCE 22 MOL_ID: 8;
SOURCE 23 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 24 ORGANISM_TAXID: 1299;
SOURCE 25 MOL_ID: 9;
SOURCE 26 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 27 ORGANISM_TAXID: 1299;
SOURCE 28 MOL_ID: 10;
SOURCE 29 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 30 ORGANISM_TAXID: 1299;
SOURCE 31 MOL_ID: 11;
SOURCE 32 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 33 ORGANISM_TAXID: 1299;
SOURCE 34 MOL_ID: 12;
SOURCE 35 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 36 ORGANISM_TAXID: 1299;
SOURCE 37 MOL_ID: 13;
SOURCE 38 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 39 ORGANISM_TAXID: 1299;
SOURCE 40 MOL_ID: 14;
SOURCE 41 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 42 ORGANISM_TAXID: 1299;
SOURCE 43 MOL_ID: 15;
SOURCE 44 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 45 ORGANISM_TAXID: 1299;
SOURCE 46 MOL_ID: 16;
SOURCE 47 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 48 ORGANISM_TAXID: 1299;
SOURCE 49 MOL_ID: 17;
SOURCE 50 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 51 ORGANISM_TAXID: 1299;
SOURCE 52 MOL_ID: 18;
SOURCE 53 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 54 ORGANISM_TAXID: 1299;
SOURCE 55 MOL_ID: 19;
SOURCE 56 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 57 ORGANISM_TAXID: 1299;
SOURCE 58 MOL_ID: 20;
SOURCE 59 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 60 ORGANISM_TAXID: 1299;
SOURCE 61 MOL_ID: 21;
SOURCE 62 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 63 ORGANISM_TAXID: 1299;
SOURCE 64 MOL_ID: 22;
SOURCE 65 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 66 ORGANISM_TAXID: 1299;
SOURCE 67 MOL_ID: 23;
SOURCE 68 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 69 ORGANISM_TAXID: 1299;
SOURCE 70 MOL_ID: 24;
SOURCE 71 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 72 ORGANISM_TAXID: 1299;
SOURCE 73 MOL_ID: 25;
SOURCE 74 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 75 ORGANISM_TAXID: 1299;
SOURCE 76 MOL_ID: 26;
SOURCE 77 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 78 ORGANISM_TAXID: 1299;
SOURCE 79 MOL_ID: 27;
SOURCE 80 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 81 ORGANISM_TAXID: 1299;
SOURCE 82 MOL_ID: 28;
SOURCE 83 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 84 ORGANISM_TAXID: 1299;
SOURCE 85 MOL_ID: 29;
SOURCE 86 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 87 ORGANISM_TAXID: 1299;
SOURCE 88 MOL_ID: 30;
SOURCE 89 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 90 ORGANISM_TAXID: 1299
KEYWDS RIBOSOME, LARGE RIBOSOMAL SUBUNIT, 50S, RIBONUCLEOPROTEIN, RIBOSOMAL
KEYWDS 2 PROTEIN, RNA-BINDING, RRNA-BINDING, TRNA-BINDING, LANKAMYCIN,
KEYWDS 3 LANKACIDIN, MACROLIDE, RIBOSOME-ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.J.BELOUSOFF,T.SHAPIRA,A.BASHAN,E.ZIMMERMAN,H.KINASHI,H.ROZENBERG,
AUTHOR 2 A.YONATH
REVDAT 3 06-SEP-23 3PIP 1 REMARK HETSYN LINK
REVDAT 2 02-MAR-11 3PIP 1 JRNL
REVDAT 1 23-FEB-11 3PIP 0
JRNL AUTH M.J.BELOUSOFF,T.SHAPIRA,A.BASHAN,E.ZIMMERMAN,H.ROZENBERG,
JRNL AUTH 2 K.ARAKAWA,H.KINASHI,A.YONATH
JRNL TITL CRYSTAL STRUCTURE OF THE SYNERGISTIC ANTIBIOTIC PAIR,
JRNL TITL 2 LANKAMYCIN AND LANKACIDIN, IN COMPLEX WITH THE LARGE
JRNL TITL 3 RIBOSOMAL SUBUNIT.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 108 2717 2011
JRNL REFN ISSN 0027-8424
JRNL PMID 21282615
JRNL DOI 10.1073/PNAS.1019406108
REMARK 2
REMARK 2 RESOLUTION. 3.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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) : 3.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.580
REMARK 3 COMPLETENESS FOR RANGE (%) : 83.3
REMARK 3 NUMBER OF REFLECTIONS : 260194
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.257
REMARK 3 R VALUE (WORKING SET) : 0.257
REMARK 3 FREE R VALUE : 0.301
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.010
REMARK 3 FREE R VALUE TEST SET COUNT : 2635
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 19.9979 - 7.3217 0.82 25880 259 0.2390 0.2625
REMARK 3 2 7.3217 - 5.8596 0.83 25998 256 0.2486 0.2999
REMARK 3 3 5.8596 - 5.1332 0.83 25604 260 0.2314 0.2866
REMARK 3 4 5.1332 - 4.6704 0.83 25672 260 0.2275 0.2747
REMARK 3 5 4.6704 - 4.3393 0.84 25949 272 0.2390 0.2866
REMARK 3 6 4.3393 - 4.0858 0.85 26317 279 0.2498 0.3167
REMARK 3 7 4.0858 - 3.8827 0.85 26097 258 0.2740 0.3258
REMARK 3 8 3.8827 - 3.7148 0.85 26184 265 0.2896 0.3316
REMARK 3 9 3.7148 - 3.5726 0.85 26151 281 0.3144 0.3319
REMARK 3 10 3.5726 - 3.4500 0.77 23707 245 0.3486 0.4010
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 : 0.83
REMARK 3 K_SOL : 0.21
REMARK 3 B_SOL : 40.01
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.520
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -20.51400
REMARK 3 B22 (A**2) : 6.81600
REMARK 3 B33 (A**2) : -25.67170
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 : 0.013 92455
REMARK 3 ANGLE : 1.271 138773
REMARK 3 CHIRALITY : 0.067 17767
REMARK 3 PLANARITY : 0.010 7157
REMARK 3 DIHEDRAL : 14.358 43386
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 44.1537 126.6952 108.9806
REMARK 3 T TENSOR
REMARK 3 T11: -0.0252 T22: 0.8794
REMARK 3 T33: 0.0579 T12: -0.2826
REMARK 3 T13: -0.0609 T23: 0.1625
REMARK 3 L TENSOR
REMARK 3 L11: 0.1314 L22: 0.0206
REMARK 3 L33: 0.4524 L12: 0.0615
REMARK 3 L13: 0.0653 L23: -0.1326
REMARK 3 S TENSOR
REMARK 3 S11: 0.0202 S12: 0.5227 S13: -0.0102
REMARK 3 S21: -0.4529 S22: -0.0298 S23: 0.0459
REMARK 3 S31: -0.0940 S32: 0.1273 S33: 0.0626
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 3PIP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000062419.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 8
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) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 260194
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.450
REMARK 200 RESOLUTION RANGE LOW (A) : 19.998
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.200
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 84.3
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.21600
REMARK 200 R SYM (I) : 0.09600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 85.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: ISOMORPHOUS REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 2ZJR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP. 15% 2:1
REMARK 280 ETHANOL:METHYLPENTANEDIOL WAS DIFFUSED TO A HANGING DROP OF 180
REMARK 280 AU/ML SOLUTION OF D50S.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 84.86150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 204.28100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 346.66700
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 84.86150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 204.28100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 346.66700
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 84.86150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 204.28100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 346.66700
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 84.86150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 204.28100
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 346.66700
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: 30-MERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, Y, A, B, C, D, E, F, G, H,
REMARK 350 AND CHAINS: I, J, K, L, M, N, O, P, Q,
REMARK 350 AND CHAINS: R, S, T, U, V, W, Z, 1, 2, 3,
REMARK 350 AND CHAINS: 4
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 A X 249
REMARK 465 C X 250
REMARK 465 C X 251
REMARK 465 G X 252
REMARK 465 A X 253
REMARK 465 A X 254
REMARK 465 A X 255
REMARK 465 C X 256
REMARK 465 G X 257
REMARK 465 C X 258
REMARK 465 U X 259
REMARK 465 U X 260
REMARK 465 G X 261
REMARK 465 C X 262
REMARK 465 G X 263
REMARK 465 U X 264
REMARK 465 U X 265
REMARK 465 U X 266
REMARK 465 C X 267
REMARK 465 G X 268
REMARK 465 G X 269
REMARK 465 G X 270
REMARK 465 G X 271
REMARK 465 U X 272
REMARK 465 U X 273
REMARK 465 G X 274
REMARK 465 U X 275
REMARK 465 A X 276
REMARK 465 G X 277
REMARK 465 G X 278
REMARK 465 A X 279
REMARK 465 C X 280
REMARK 465 C X 281
REMARK 465 A X 282
REMARK 465 G X 283
REMARK 465 U X 284
REMARK 465 U X 285
REMARK 465 U X 286
REMARK 465 U X 287
REMARK 465 U X 288
REMARK 465 A X 289
REMARK 465 A X 290
REMARK 465 G X 291
REMARK 465 A X 292
REMARK 465 U X 293
REMARK 465 U X 294
REMARK 465 C X 295
REMARK 465 A X 296
REMARK 465 A X 297
REMARK 465 C X 298
REMARK 465 C X 299
REMARK 465 C X 300
REMARK 465 C X 301
REMARK 465 C X 362
REMARK 465 G X 363
REMARK 465 G X 364
REMARK 465 U X 365
REMARK 465 U X 366
REMARK 465 G X 367
REMARK 465 A X 368
REMARK 465 C X 369
REMARK 465 U X 370
REMARK 465 G X 371
REMARK 465 U X 372
REMARK 465 A X 373
REMARK 465 C X 374
REMARK 465 U X 375
REMARK 465 G X 376
REMARK 465 G X 377
REMARK 465 C X 378
REMARK 465 A X 379
REMARK 465 C X 380
REMARK 465 C X 381
REMARK 465 U X 382
REMARK 465 G X 383
REMARK 465 A X 384
REMARK 465 G X 385
REMARK 465 U X 386
REMARK 465 G X 726
REMARK 465 U X 727
REMARK 465 G X 728
REMARK 465 A X 729
REMARK 465 C X 730
REMARK 465 A X 731
REMARK 465 A X 891
REMARK 465 G X 892
REMARK 465 G X 893
REMARK 465 G X 894
REMARK 465 G X 895
REMARK 465 G X 896
REMARK 465 C X 897
REMARK 465 C X 898
REMARK 465 U X 899
REMARK 465 A X 900
REMARK 465 C X 901
REMARK 465 C X 902
REMARK 465 A X 903
REMARK 465 G X 904
REMARK 465 C X 905
REMARK 465 U X 906
REMARK 465 U X 907
REMARK 465 A X 908
REMARK 465 C X 909
REMARK 465 C X 910
REMARK 465 A X 1055
REMARK 465 U X 1056
REMARK 465 A X 1057
REMARK 465 A X 1080
REMARK 465 G X 1184
REMARK 465 C X 1185
REMARK 465 G X 1186
REMARK 465 A X 1187
REMARK 465 A X 1188
REMARK 465 G X 1189
REMARK 465 C X 1190
REMARK 465 G X 1191
REMARK 465 A X 1192
REMARK 465 G X 1427
REMARK 465 C X 1522
REMARK 465 A X 1523
REMARK 465 C X 1524
REMARK 465 A X 1525
REMARK 465 G X 1809
REMARK 465 G X 1889
REMARK 465 G X 1890
REMARK 465 C X 1891
REMARK 465 C X 1892
REMARK 465 G X 1893
REMARK 465 U X 1894
REMARK 465 A X 1895
REMARK 465 A X 1896
REMARK 465 C X 1897
REMARK 465 U X 1898
REMARK 465 A X 1899
REMARK 465 U X 1900
REMARK 465 A X 1901
REMARK 465 A X 1902
REMARK 465 C X 1903
REMARK 465 G X 1904
REMARK 465 G X 1905
REMARK 465 U X 1906
REMARK 465 C X 1907
REMARK 465 C X 1908
REMARK 465 U X 2087
REMARK 465 U X 2088
REMARK 465 C X 2089
REMARK 465 U X 2090
REMARK 465 C X 2091
REMARK 465 U X 2092
REMARK 465 G X 2093
REMARK 465 C X 2094
REMARK 465 G X 2095
REMARK 465 U X 2096
REMARK 465 A X 2097
REMARK 465 G X 2098
REMARK 465 G X 2099
REMARK 465 A X 2100
REMARK 465 U X 2101
REMARK 465 A X 2102
REMARK 465 G X 2103
REMARK 465 G X 2104
REMARK 465 U X 2105
REMARK 465 G X 2106
REMARK 465 G X 2107
REMARK 465 G X 2108
REMARK 465 A X 2109
REMARK 465 G X 2110
REMARK 465 C X 2111
REMARK 465 C X 2112
REMARK 465 U X 2113
REMARK 465 G X 2114
REMARK 465 C X 2115
REMARK 465 G X 2116
REMARK 465 A X 2117
REMARK 465 A X 2118
REMARK 465 A X 2119
REMARK 465 C X 2120
REMARK 465 U X 2121
REMARK 465 G X 2122
REMARK 465 G X 2123
REMARK 465 C X 2124
REMARK 465 C X 2125
REMARK 465 U X 2126
REMARK 465 U X 2127
REMARK 465 U X 2128
REMARK 465 U X 2129
REMARK 465 G X 2130
REMARK 465 G X 2131
REMARK 465 G X 2132
REMARK 465 G X 2133
REMARK 465 U X 2134
REMARK 465 C X 2135
REMARK 465 G X 2136
REMARK 465 G X 2137
REMARK 465 U X 2138
REMARK 465 G X 2139
REMARK 465 G X 2140
REMARK 465 A X 2141
REMARK 465 G X 2142
REMARK 465 G X 2143
REMARK 465 C X 2144
REMARK 465 A X 2145
REMARK 465 A X 2146
REMARK 465 C X 2147
REMARK 465 G X 2148
REMARK 465 G X 2149
REMARK 465 U X 2150
REMARK 465 G X 2151
REMARK 465 A X 2152
REMARK 465 A X 2153
REMARK 465 A X 2154
REMARK 465 U X 2155
REMARK 465 A X 2156
REMARK 465 C X 2157
REMARK 465 C X 2158
REMARK 465 A X 2159
REMARK 465 C X 2160
REMARK 465 C X 2161
REMARK 465 C X 2162
REMARK 465 U X 2163
REMARK 465 G X 2164
REMARK 465 A X 2165
REMARK 465 G X 2166
REMARK 465 A X 2167
REMARK 465 A X 2168
REMARK 465 A X 2169
REMARK 465 U X 2774
REMARK 465 U X 2775
REMARK 465 U X 2776
REMARK 465 A X 2777
REMARK 465 U X 2778
REMARK 465 C X 2779
REMARK 465 A X 2877
REMARK 465 C X 2878
REMARK 465 U X 2879
REMARK 465 C X 2880
REMARK 465 A Y 1
REMARK 465 C Y 2
REMARK 465 U Y 123
REMARK 465 ALA A 3
REMARK 465 VAL A 4
REMARK 465 LYS A 5
REMARK 465 LYS A 6
REMARK 465 TYR A 7
REMARK 465 ARG A 8
REMARK 465 PRO A 9
REMARK 465 TYR A 10
REMARK 465 THR A 11
REMARK 465 PRO A 12
REMARK 465 SER A 13
REMARK 465 ARG A 14
REMARK 465 ARG A 15
REMARK 465 GLN A 16
REMARK 465 MET A 17
REMARK 465 THR A 18
REMARK 465 THR A 19
REMARK 465 ALA A 20
REMARK 465 ARG A 274
REMARK 465 ARG A 275
REMARK 465 LYS A 276
REMARK 465 ALA B 206
REMARK 465 ALA B 207
REMARK 465 LYS B 208
REMARK 465 GLY B 209
REMARK 465 GLY B 210
REMARK 465 LYS B 211
REMARK 465 MET C 1
REMARK 465 VAL C 196
REMARK 465 GLU C 197
REMARK 465 GLU C 198
REMARK 465 GLU C 199
REMARK 465 ALA C 200
REMARK 465 GLY C 201
REMARK 465 GLU C 202
REMARK 465 GLU C 203
REMARK 465 GLN C 204
REMARK 465 GLN C 205
REMARK 465 MET D 1
REMARK 465 GLN D 2
REMARK 465 GLN D 180
REMARK 465 MET E 1
REMARK 465 SER E 2
REMARK 465 ARG E 3
REMARK 465 ILE E 4
REMARK 465 ALA E 176
REMARK 465 GLY E 177
REMARK 465 ALA E 178
REMARK 465 THR E 179
REMARK 465 GLY E 180
REMARK 465 GLY E 181
REMARK 465 LYS E 182
REMARK 465 GLY E 183
REMARK 465 LYS E 184
REMARK 465 LYS E 185
REMARK 465 MET F 1
REMARK 465 LYS F 2
REMARK 465 LYS F 3
REMARK 465 VAL F 4
REMARK 465 ALA F 5
REMARK 465 GLY F 6
REMARK 465 ILE F 7
REMARK 465 VAL F 8
REMARK 465 LYS F 9
REMARK 465 LEU F 10
REMARK 465 GLN F 11
REMARK 465 LEU F 12
REMARK 465 PRO F 13
REMARK 465 ALA F 14
REMARK 465 GLY F 15
REMARK 465 LYS F 16
REMARK 465 ALA F 17
REMARK 465 THR F 18
REMARK 465 PRO F 19
REMARK 465 ALA F 20
REMARK 465 PRO F 21
REMARK 465 PRO F 22
REMARK 465 VAL F 23
REMARK 465 GLY F 24
REMARK 465 PRO F 25
REMARK 465 ALA F 26
REMARK 465 LEU F 27
REMARK 465 GLY F 28
REMARK 465 GLN F 29
REMARK 465 TYR F 30
REMARK 465 GLY F 31
REMARK 465 ALA F 32
REMARK 465 ASN F 33
REMARK 465 ILE F 34
REMARK 465 MET F 35
REMARK 465 GLU F 36
REMARK 465 PHE F 37
REMARK 465 THR F 38
REMARK 465 LYS F 39
REMARK 465 ALA F 40
REMARK 465 PHE F 41
REMARK 465 ASN F 42
REMARK 465 ALA F 43
REMARK 465 GLN F 44
REMARK 465 THR F 45
REMARK 465 ALA F 46
REMARK 465 ASP F 47
REMARK 465 LYS F 48
REMARK 465 GLY F 49
REMARK 465 ASP F 50
REMARK 465 ALA F 51
REMARK 465 ILE F 52
REMARK 465 ILE F 53
REMARK 465 PRO F 54
REMARK 465 VAL F 55
REMARK 465 GLU F 56
REMARK 465 ILE F 57
REMARK 465 THR F 58
REMARK 465 ILE F 59
REMARK 465 TYR F 60
REMARK 465 ALA F 61
REMARK 465 ASP F 62
REMARK 465 ARG F 63
REMARK 465 SER F 64
REMARK 465 PHE F 65
REMARK 465 THR F 66
REMARK 465 PHE F 67
REMARK 465 ILE F 68
REMARK 465 THR F 69
REMARK 465 LYS F 70
REMARK 465 THR F 71
REMARK 465 PRO F 72
REMARK 465 PRO F 73
REMARK 465 THR F 137
REMARK 465 VAL F 138
REMARK 465 GLU F 139
REMARK 465 GLY F 140
REMARK 465 GLY F 141
REMARK 465 PRO F 142
REMARK 465 ASN F 143
REMARK 465 ALA F 144
REMARK 465 MET G 1
REMARK 465 ALA G 2
REMARK 465 PHE G 3
REMARK 465 PRO G 4
REMARK 465 ASP G 5
REMARK 465 THR G 6
REMARK 465 ASP G 7
REMARK 465 VAL G 8
REMARK 465 SER G 9
REMARK 465 PRO G 10
REMARK 465 PRO G 11
REMARK 465 ARG G 12
REMARK 465 GLY G 13
REMARK 465 GLY G 14
REMARK 465 PRO G 15
REMARK 465 SER G 16
REMARK 465 SER G 17
REMARK 465 PRO G 18
REMARK 465 ALA G 19
REMARK 465 LYS G 20
REMARK 465 SER G 21
REMARK 465 PRO G 22
REMARK 465 LEU G 23
REMARK 465 LEU G 24
REMARK 465 ARG G 25
REMARK 465 SER G 26
REMARK 465 PHE G 27
REMARK 465 LYS G 28
REMARK 465 VAL G 29
REMARK 465 GLU G 172
REMARK 465 VAL G 173
REMARK 465 LYS G 174
REMARK 465 MET I 1
REMARK 465 LYS I 2
REMARK 465 LEU I 3
REMARK 465 HIS I 4
REMARK 465 ASP I 5
REMARK 465 LEU I 6
REMARK 465 LYS I 7
REMARK 465 PRO I 8
REMARK 465 THR I 9
REMARK 465 PRO I 10
REMARK 465 VAL I 145
REMARK 465 GLN I 146
REMARK 465 THR I 147
REMARK 465 GLN I 148
REMARK 465 GLN I 149
REMARK 465 ASP I 150
REMARK 465 ASP I 151
REMARK 465 ALA I 152
REMARK 465 GLN I 153
REMARK 465 LYS I 154
REMARK 465 ALA I 155
REMARK 465 GLU I 156
REMARK 465 MET J 2
REMARK 465 LEU J 3
REMARK 465 LEU J 4
REMARK 465 PRO J 5
REMARK 465 GLN J 142
REMARK 465 MET K 1
REMARK 465 ARG K 2
REMARK 465 VAL K 116
REMARK 465 MET L 1
REMARK 465 ALA L 2
REMARK 465 THR L 3
REMARK 465 ALA L 4
REMARK 465 THR L 5
REMARK 465 THR L 6
REMARK 465 ILE L 7
REMARK 465 LEU L 112
REMARK 465 ASP L 113
REMARK 465 PHE L 114
REMARK 465 MET M 1
REMARK 465 LEU M 110
REMARK 465 ARG M 111
REMARK 465 GLY M 112
REMARK 465 LYS M 113
REMARK 465 ALA M 114
REMARK 465 ALA M 115
REMARK 465 ARG M 116
REMARK 465 ILE M 117
REMARK 465 LYS M 118
REMARK 465 SER M 119
REMARK 465 ASP M 120
REMARK 465 ARG M 121
REMARK 465 SER M 122
REMARK 465 ARG M 123
REMARK 465 VAL M 124
REMARK 465 MET M 125
REMARK 465 LYS M 126
REMARK 465 ASP M 127
REMARK 465 ALA M 128
REMARK 465 ALA M 129
REMARK 465 ARG M 130
REMARK 465 ALA M 131
REMARK 465 GLN M 132
REMARK 465 GLN M 133
REMARK 465 ASP M 134
REMARK 465 LYS M 135
REMARK 465 ALA M 136
REMARK 465 ASN M 137
REMARK 465 ALA M 138
REMARK 465 SER M 139
REMARK 465 ALA M 140
REMARK 465 SER M 141
REMARK 465 GLN M 142
REMARK 465 ALA M 143
REMARK 465 ALA M 144
REMARK 465 ALA M 145
REMARK 465 ALA M 146
REMARK 465 GLN M 147
REMARK 465 ALA M 148
REMARK 465 ASP M 149
REMARK 465 VAL M 150
REMARK 465 THR M 151
REMARK 465 VAL M 152
REMARK 465 ILE M 153
REMARK 465 SER M 154
REMARK 465 ALA M 155
REMARK 465 ALA M 156
REMARK 465 PRO M 157
REMARK 465 GLU M 158
REMARK 465 VAL M 159
REMARK 465 ALA M 160
REMARK 465 PRO M 161
REMARK 465 GLU M 162
REMARK 465 THR M 163
REMARK 465 GLN M 164
REMARK 465 GLY M 165
REMARK 465 GLU M 166
REMARK 465 MET N 1
REMARK 465 MET O 1
REMARK 465 PHE O 2
REMARK 465 ALA O 3
REMARK 465 ILE O 4
REMARK 465 GLN O 99
REMARK 465 GLY O 100
REMARK 465 MET P 1
REMARK 465 THR P 2
REMARK 465 ALA P 3
REMARK 465 PRO P 4
REMARK 465 GLU P 5
REMARK 465 GLN P 6
REMARK 465 THR P 7
REMARK 465 LYS P 134
REMARK 465 MET Q 1
REMARK 465 ALA Q 95
REMARK 465 MET R 1
REMARK 465 PRO R 2
REMARK 465 ARG R 3
REMARK 465 ILE R 114
REMARK 465 ASP R 115
REMARK 465 LEU S 176
REMARK 465 THR S 177
REMARK 465 ALA S 178
REMARK 465 GLU S 179
REMARK 465 GLU S 180
REMARK 465 LEU S 181
REMARK 465 GLU S 182
REMARK 465 ALA S 183
REMARK 465 GLU S 184
REMARK 465 VAL S 185
REMARK 465 GLN S 186
REMARK 465 ALA S 187
REMARK 465 ALA S 188
REMARK 465 GLN S 189
REMARK 465 VAL S 190
REMARK 465 ALA S 191
REMARK 465 GLY S 192
REMARK 465 LEU S 193
REMARK 465 VAL S 194
REMARK 465 ALA S 195
REMARK 465 ALA S 196
REMARK 465 GLY S 197
REMARK 465 GLU S 198
REMARK 465 LEU S 199
REMARK 465 SER S 200
REMARK 465 GLU S 201
REMARK 465 GLU S 202
REMARK 465 ALA S 203
REMARK 465 ALA S 204
REMARK 465 GLU S 205
REMARK 465 ALA S 206
REMARK 465 VAL S 207
REMARK 465 LEU S 208
REMARK 465 GLU S 209
REMARK 465 GLY S 210
REMARK 465 ASP S 211
REMARK 465 ALA S 212
REMARK 465 SER S 213
REMARK 465 LEU S 214
REMARK 465 GLU S 215
REMARK 465 GLU S 216
REMARK 465 VAL S 217
REMARK 465 LYS S 218
REMARK 465 ALA S 219
REMARK 465 GLU S 220
REMARK 465 ALA S 221
REMARK 465 SER S 222
REMARK 465 GLU S 223
REMARK 465 ASP S 224
REMARK 465 ASN S 225
REMARK 465 ALA S 226
REMARK 465 GLY S 227
REMARK 465 THR S 228
REMARK 465 ASP S 229
REMARK 465 SER S 230
REMARK 465 GLU S 231
REMARK 465 ASP S 232
REMARK 465 ASN S 233
REMARK 465 SER S 234
REMARK 465 ASP S 235
REMARK 465 ALA S 236
REMARK 465 GLN S 237
REMARK 465 MET T 1
REMARK 465 ALA T 2
REMARK 465 HIS T 3
REMARK 465 LYS T 4
REMARK 465 LYS T 5
REMARK 465 GLY T 6
REMARK 465 VAL T 7
REMARK 465 GLY T 8
REMARK 465 SER T 9
REMARK 465 SER T 10
REMARK 465 LYS T 11
REMARK 465 THR T 86
REMARK 465 GLU T 87
REMARK 465 VAL T 88
REMARK 465 ALA T 89
REMARK 465 ALA T 90
REMARK 465 ASP T 91
REMARK 465 MET U 1
REMARK 465 SER U 2
REMARK 465 ARG U 3
REMARK 465 GLU U 4
REMARK 465 CYS U 5
REMARK 465 TYR U 6
REMARK 465 LEU U 7
REMARK 465 LEU U 80
REMARK 465 ILE U 81
REMARK 465 MET V 1
REMARK 465 GLN V 67
REMARK 465 MET Z 1
REMARK 465 ALA Z 2
REMARK 465 VAL Z 60
REMARK 465 MET 1 1
REMARK 465 VAL 1 55
REMARK 465 GLU 2 47
REMARK 465 MET 3 1
REMARK 465 PRO 3 2
REMARK 465 LYS 3 3
REMARK 465 MET 3 4
REMARK 465 LYS 3 5
REMARK 465 GLY 3 65
REMARK 465 LYS 3 66
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 LEU A 25 CG CD1 CD2
REMARK 470 ARG A 29 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 112 CG CD NE CZ NH1 NH2
REMARK 470 ARG I 53 CG CD NE CZ NH1 NH2
REMARK 470 ARG Q 62 CG CD NE CZ NH1 NH2
REMARK 470 ARG Q 64 CG CD NE CZ NH1 NH2
REMARK 470 ARG U 25 CG CD NE CZ NH1 NH2
REMARK 470 ASP U 27 CG OD1 OD2
REMARK 470 ARG U 40 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OP1 A X 1771 MG MG X 2930 1.37
REMARK 500 O6 G X 2426 O4 U X 2483 1.47
REMARK 500 OP1 G X 2555 MG MG X 2885 1.52
REMARK 500 O2 C X 1692 O SER B 128 1.62
REMARK 500 OP1 U X 2000 MG MG X 2903 1.64
REMARK 500 O2 C X 2662 NZ LYS H 82 1.71
REMARK 500 C ARG A 29 CD PRO A 30 1.78
REMARK 500 OP1 C X 2494 O GLY G 108 1.81
REMARK 500 OP1 G X 309 O ARG R 93 1.81
REMARK 500 N6 A X 1685 O2 U X 1974 1.82
REMARK 500 NH2 ARG O 21 OE1 GLN O 88 1.86
REMARK 500 O2' A X 123 O ALA 2 13 1.89
REMARK 500 OP1 G X 1291 OG1 THR K 36 1.89
REMARK 500 N2 G X 699 CE1 TYR 2 5 1.89
REMARK 500 N6 A X 2427 NH2 ARG I 40 1.90
REMARK 500 OP1 U X 919 OD2 ASP J 26 1.91
REMARK 500 NH2 ARG S 129 OE1 GLU S 156 1.93
REMARK 500 O TYR L 39 O ALA L 54 1.96
REMARK 500 OP2 U X 348 NH2 ARG R 93 1.98
REMARK 500 O2' A X 834 OP2 G X 957 1.98
REMARK 500 N6 A X 2257 OD1 ASP T 15 1.99
REMARK 500 CB LYS G 35 OD2 ASP G 37 2.00
REMARK 500 OP1 A X 587 O2' U X 1268 2.03
REMARK 500 CG LYS G 35 OD2 ASP G 37 2.03
REMARK 500 OP1 A X 1203 O GLY I 33 2.05
REMARK 500 O SER A 90 ND2 ASN A 199 2.05
REMARK 500 O ARG N 59 OE1 GLN N 63 2.07
REMARK 500 O2' G X 1684 O4 U X 1974 2.08
REMARK 500 OP1 G X 2664 NH1 ARG H 90 2.08
REMARK 500 O2' A X 703 OP1 G X 793 2.09
REMARK 500 O2' C X 863 OG1 THR W 19 2.09
REMARK 500 O ILE C 7 O VAL C 120 2.09
REMARK 500 N7 A X 1391 C6 G X 1393 2.10
REMARK 500 O2' A X 1686 OP1 G X 2528 2.11
REMARK 500 O2' A X 1750 O2' G X 2694 2.12
REMARK 500 OD1 ASN H 100 N GLN H 102 2.12
REMARK 500 C8 A X 1391 O6 G X 1393 2.14
REMARK 500 O2 U X 2668 O5' U X 2693 2.14
REMARK 500 OP1 U X 845 NZ LYS I 38 2.14
REMARK 500 O TYR J 66 OE1 GLU J 106 2.14
REMARK 500 OP1 G X 1336 NZ LYS P 119 2.15
REMARK 500 O2' A X 626 OD1 ASN C 176 2.15
REMARK 500 O2 U X 1939 OP1 U X 2531 2.15
REMARK 500 N2 G X 334 NH2 ARG C 162 2.15
REMARK 500 N1 G X 1691 O6 G X 1972 2.16
REMARK 500 O2' A X 2060 O2' A X 2413 2.17
REMARK 500 N7 A X 1391 O6 G X 1393 2.17
REMARK 500 OE2 GLU A 102 NE ARG A 104 2.18
REMARK 500 O2 U X 1365 N2 G X 1393 2.18
REMARK 500 O2' G X 2806 OP1 U X 2859 2.18
REMARK 500
REMARK 500 THIS ENTRY HAS 52 CLOSE CONTACTS
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O2 C X 1552 ND2 ASN M 43 8455 0.99
REMARK 500 O2 C X 1552 CG ASN M 43 8455 1.93
REMARK 500 C2 C X 1552 ND2 ASN M 43 8455 2.03
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 A X 461 C5 A X 461 N7 -0.052
REMARK 500 A X 461 C8 A X 461 N9 -0.050
REMARK 500 C X 465 N1 C X 465 C6 -0.040
REMARK 500 G X 499 N1 G X 499 C2 -0.049
REMARK 500 G X 522 C4 G X 522 C5 0.049
REMARK 500 G X 540 C5' G X 540 C4' -0.044
REMARK 500 A X 542 N9 A X 542 C4 -0.051
REMARK 500 C X 569 C4 C X 569 N4 -0.059
REMARK 500 U X 571 N1 U X 571 C2 -0.055
REMARK 500 U X 575 N1 U X 575 C2 -0.060
REMARK 500 G X 579 C5 G X 579 C6 0.069
REMARK 500 A X 581 N9 A X 581 C4 -0.056
REMARK 500 C X 583 C4 C X 583 C5 -0.061
REMARK 500 G X 586 C5 G X 586 N7 -0.043
REMARK 500 U X 616 C3' U X 616 C2' -0.149
REMARK 500 C X 679 N1 C X 679 C6 -0.045
REMARK 500 A X 690 N3 A X 690 C4 -0.037
REMARK 500 C X 691 N3 C X 691 C4 -0.053
REMARK 500 A X 740 N3 A X 740 C4 -0.039
REMARK 500 A X 747 C8 A X 747 N9 -0.076
REMARK 500 U X 753 N1 U X 753 C2 -0.057
REMARK 500 G X 754 C4 G X 754 C5 -0.050
REMARK 500 A X 807 N9 A X 807 C4 -0.036
REMARK 500 C X 827 N1 C X 827 C6 -0.047
REMARK 500 G X 836 C5 G X 836 N7 -0.040
REMARK 500 G X 955 O3' A X 956 P -0.092
REMARK 500 C X 975 N1 C X 975 C6 -0.044
REMARK 500 C X 982 N1 C X 982 C6 -0.049
REMARK 500 A X 986 N9 A X 986 C4 -0.037
REMARK 500 A X1166 N9 A X1166 C4 0.036
REMARK 500 G X1246 C6 G X1246 N1 -0.048
REMARK 500 A X1250 N9 A X1250 C4 -0.038
REMARK 500 A X1260 N9 A X1260 C4 -0.067
REMARK 500 G X1261 C5 G X1261 N7 -0.039
REMARK 500 G X1265 C8 G X1265 N9 -0.044
REMARK 500 A X1281 C6 A X1281 N6 0.050
REMARK 500 G X1284 N3 G X1284 C4 -0.053
REMARK 500 A X1288 C4 A X1288 C5 0.049
REMARK 500 A X1288 C8 A X1288 N9 0.048
REMARK 500 A X1290 C8 A X1290 N9 -0.072
REMARK 500 A X1292 C5 A X1292 N7 0.039
REMARK 500 A X1299 N9 A X1299 C4 -0.068
REMARK 500 G X1316 N3 G X1316 C4 -0.065
REMARK 500 G X1332 C8 G X1332 N9 -0.043
REMARK 500 G X1333 N3 G X1333 C4 -0.048
REMARK 500 G X1333 N9 G X1333 C4 -0.055
REMARK 500 A X1334 C5 A X1334 N7 -0.038
REMARK 500 C X1621 C3' C X1621 C2' -0.075
REMARK 500 G X1629 C5 G X1629 N7 -0.036
REMARK 500 G X1635 N3 G X1635 C4 -0.063
REMARK 500
REMARK 500 THIS ENTRY HAS 101 BOND DEVIATIONS.
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 U X 9 N3 - C2 - O2 ANGL. DEV. = -4.9 DEGREES
REMARK 500 G X 11 N1 - C6 - O6 ANGL. DEV. = 4.1 DEGREES
REMARK 500 G X 15 C4 - C5 - N7 ANGL. DEV. = -3.7 DEGREES
REMARK 500 G X 15 N9 - C4 - C5 ANGL. DEV. = 2.9 DEGREES
REMARK 500 G X 15 C5 - C6 - O6 ANGL. DEV. = 4.8 DEGREES
REMARK 500 U X 18 C6 - N1 - C2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 U X 18 C5 - C6 - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 A X 21 C2 - N3 - C4 ANGL. DEV. = -3.5 DEGREES
REMARK 500 U X 25 N3 - C4 - O4 ANGL. DEV. = 4.6 DEGREES
REMARK 500 U X 25 C5 - C4 - O4 ANGL. DEV. = -3.9 DEGREES
REMARK 500 G X 27 C2 - N3 - C4 ANGL. DEV. = 3.1 DEGREES
REMARK 500 U X 29 N3 - C4 - O4 ANGL. DEV. = 4.3 DEGREES
REMARK 500 U X 29 C5 - C4 - O4 ANGL. DEV. = -4.8 DEGREES
REMARK 500 C X 31 C6 - N1 - C2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 C X 31 N1 - C2 - O2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 C X 31 N3 - C2 - O2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 C X 32 C6 - N1 - C2 ANGL. DEV. = 2.6 DEGREES
REMARK 500 U X 34 C6 - N1 - C2 ANGL. DEV. = 3.9 DEGREES
REMARK 500 U X 34 C5 - C6 - N1 ANGL. DEV. = -3.9 DEGREES
REMARK 500 C X 37 C6 - N1 - C2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 C X 37 C5 - C6 - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 C X 46 C6 - N1 - C2 ANGL. DEV. = -2.5 DEGREES
REMARK 500 G X 50 N3 - C4 - C5 ANGL. DEV. = 3.4 DEGREES
REMARK 500 G X 50 C8 - N9 - C4 ANGL. DEV. = 3.7 DEGREES
REMARK 500 G X 50 N9 - C4 - C5 ANGL. DEV. = -3.0 DEGREES
REMARK 500 G X 57 N7 - C8 - N9 ANGL. DEV. = 3.5 DEGREES
REMARK 500 G X 57 C8 - N9 - C4 ANGL. DEV. = -4.4 DEGREES
REMARK 500 G X 67 C4 - C5 - N7 ANGL. DEV. = 2.7 DEGREES
REMARK 500 A X 70 N7 - C8 - N9 ANGL. DEV. = 3.0 DEGREES
REMARK 500 A X 70 C8 - N9 - C4 ANGL. DEV. = -2.9 DEGREES
REMARK 500 G X 82 N1 - C6 - O6 ANGL. DEV. = -4.0 DEGREES
REMARK 500 C X 126 C6 - N1 - C2 ANGL. DEV. = 2.5 DEGREES
REMARK 500 A X 137 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 G X 156 C8 - N9 - C4 ANGL. DEV. = 3.0 DEGREES
REMARK 500 G X 165 C8 - N9 - C4 ANGL. DEV. = 2.8 DEGREES
REMARK 500 G X 166 N3 - C4 - C5 ANGL. DEV. = 3.1 DEGREES
REMARK 500 G X 166 C8 - N9 - C4 ANGL. DEV. = 2.6 DEGREES
REMARK 500 A X 174 C3' - O3' - P ANGL. DEV. = -14.1 DEGREES
REMARK 500 C X 175 C6 - N1 - C2 ANGL. DEV. = 3.0 DEGREES
REMARK 500 C X 175 N3 - C4 - C5 ANGL. DEV. = 2.9 DEGREES
REMARK 500 U X 187 N1 - C2 - O2 ANGL. DEV. = -5.1 DEGREES
REMARK 500 A X 190 C8 - N9 - C4 ANGL. DEV. = 2.7 DEGREES
REMARK 500 G X 219 N3 - C2 - N2 ANGL. DEV. = 4.3 DEGREES
REMARK 500 G X 231 C8 - N9 - C4 ANGL. DEV. = -2.4 DEGREES
REMARK 500 C X 236 C6 - N1 - C2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 C X 236 N3 - C2 - O2 ANGL. DEV. = -4.7 DEGREES
REMARK 500 G X 309 C4 - C5 - N7 ANGL. DEV. = 3.9 DEGREES
REMARK 500 G X 309 C5 - N7 - C8 ANGL. DEV. = -3.5 DEGREES
REMARK 500 G X 309 C5 - C6 - O6 ANGL. DEV. = -4.4 DEGREES
REMARK 500 G X 319 N3 - C4 - C5 ANGL. DEV. = 3.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 983 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 LEU A 25 156.13 96.27
REMARK 500 THR A 26 178.07 170.47
REMARK 500 GLU A 31 164.30 77.15
REMARK 500 LYS A 32 142.47 177.84
REMARK 500 ALA A 33 -56.54 -142.20
REMARK 500 ASN A 46 -153.80 -100.87
REMARK 500 THR A 51 -65.36 -109.72
REMARK 500 PHE A 54 -135.16 63.37
REMARK 500 LYS A 60 12.85 49.79
REMARK 500 ARG A 61 144.84 -35.81
REMARK 500 PRO A 87 -163.83 -74.94
REMARK 500 ARG A 89 -43.80 -177.35
REMARK 500 THR A 113 -150.43 -101.65
REMARK 500 LYS A 152 -13.09 59.29
REMARK 500 SER A 159 -139.32 -101.05
REMARK 500 GLU A 170 -80.79 -84.99
REMARK 500 SER A 171 -65.90 -132.74
REMARK 500 PRO A 179 1.17 -69.06
REMARK 500 ALA A 200 -133.67 51.00
REMARK 500 ALA A 210 155.09 -49.83
REMARK 500 HIS A 221 130.42 -11.46
REMARK 500 MET A 227 -156.50 -78.52
REMARK 500 PRO A 250 95.33 -64.33
REMARK 500 TRP A 251 -63.05 -148.85
REMARK 500 THR A 255 51.90 33.24
REMARK 500 PHE A 270 75.92 60.76
REMARK 500 ASN B 17 -106.02 61.68
REMARK 500 ALA B 28 63.39 -103.53
REMARK 500 TYR B 51 -79.55 -147.47
REMARK 500 GLU B 56 -7.84 -56.55
REMARK 500 VAL B 72 -85.57 -113.99
REMARK 500 ALA B 73 139.97 178.65
REMARK 500 PRO B 74 108.30 -59.28
REMARK 500 PRO B 86 179.78 -11.63
REMARK 500 ASP B 89 -165.00 -106.65
REMARK 500 ASP B 94 -33.28 68.66
REMARK 500 SER B 108 177.71 -56.04
REMARK 500 ASN B 121 -145.07 56.57
REMARK 500 PHE B 122 169.08 120.42
REMARK 500 HIS B 135 -123.47 60.24
REMARK 500 ARG B 137 93.02 120.49
REMARK 500 GLN B 143 -119.57 -111.18
REMARK 500 ARG B 144 -124.02 -142.06
REMARK 500 SER B 200 154.62 -45.55
REMARK 500 ALA B 202 -77.96 -57.86
REMARK 500 GLN C 9 -150.19 -80.18
REMARK 500 ASN C 10 83.45 -178.33
REMARK 500 ILE C 15 149.78 87.77
REMARK 500 VAL C 22 107.76 58.16
REMARK 500 ALA C 43 108.12 -165.18
REMARK 500
REMARK 500 THIS ENTRY HAS 345 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 VAL E 125 PRO E 126 145.98
REMARK 500 VAL E 165 GLY E 166 138.05
REMARK 500 GLY E 174 LYS E 175 -97.36
REMARK 500 ASN F 116 ALA F 117 -139.30
REMARK 500 ALA F 117 GLY F 118 -114.26
REMARK 500 GLY F 118 SER F 119 142.56
REMARK 500 LYS G 35 ASN G 36 147.34
REMARK 500 ASN G 36 ASP G 37 -128.91
REMARK 500 GLU G 38 GLN G 39 129.73
REMARK 500 ALA G 85 ALA G 86 136.60
REMARK 500 THR G 91 GLY G 92 -137.36
REMARK 500 LEU G 110 LYS G 111 -128.84
REMARK 500 LYS G 111 THR G 112 -141.67
REMARK 500 PRO G 170 LEU G 171 -142.52
REMARK 500 GLY H 40 ASN H 41 -134.81
REMARK 500 ASN H 41 LYS H 42 148.95
REMARK 500 ARG I 18 VAL I 19 -149.22
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 ARG E 130 0.14 SIDE CHAIN
REMARK 500 ARG J 83 0.13 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 X2900 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 579 O6
REMARK 620 2 G X2426 O3' 124.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2897 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 743 OP2
REMARK 620 2 G X 776 OP1 139.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2927 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 761 O3'
REMARK 620 2 A X 762 OP1 53.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2919 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 796 OP2
REMARK 620 2 A X2568 OP1 74.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2937 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X 800 OP1
REMARK 620 2 C X 803 OP2 82.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2909 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 956 OP2
REMARK 620 2 A X 956 O5' 53.5
REMARK 620 3 G X 957 OP2 138.7 105.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2887 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1281 OP1
REMARK 620 2 C X1989 OP1 62.4
REMARK 620 3 A X2031 OP1 139.1 108.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2888 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1282 OP2
REMARK 620 2 A X1988 OP1 72.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2947 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X1687 OP1
REMARK 620 2 U X1688 OP2 75.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2930 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X1773 OP1
REMARK 620 2 A X1774 OP2 65.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2922 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X1999 OP1
REMARK 620 2 A X2041 OP1 86.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2899 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X2039 OP2
REMARK 620 2 A X2040 OP2 89.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2911 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2246 OP2
REMARK 620 2 A X2248 OP1 125.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2951 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X2486 OP1
REMARK 620 2 C X2552 OP1 113.5
REMARK 620 3 C X2554 OP2 136.2 80.7
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2933 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X2561 OP2
REMARK 620 2 G X2562 OP2 110.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2891 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2690 OP1
REMARK 620 2 A X2692 OP1 61.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2892 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2692 OP2
REMARK 620 2 G X2694 OP2 97.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X2945 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2705 O3'
REMARK 620 2 A X2705 O2' 59.7
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LC2 X 2881
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMA X 2882
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2883
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2884
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2885
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2887
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2888
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2889
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2890
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2891
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2892
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2893
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2894
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2895
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2896
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2897
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2898
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2899
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2900
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2901
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2902
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2903
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2904
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2905
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2906
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2907
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2908
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2909
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2911
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG U 82
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2912
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2913
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2915
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2916
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2917
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2918
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2919
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2920
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2921
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2922
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2923
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2924
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2925
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2926
REMARK 800
REMARK 800 SITE_IDENTIFIER: EC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2927
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2928
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2929
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2930
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2931
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2932
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2933
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2934
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2935
REMARK 800
REMARK 800 SITE_IDENTIFIER: FC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2937
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2938
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2939
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2940
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2941
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2942
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2943
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2944
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2945
REMARK 800
REMARK 800 SITE_IDENTIFIER: GC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2946
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2947
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2948
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2949
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2950
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 2951
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG I 157
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K X 2954
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K X 2955
REMARK 800
REMARK 800 SITE_IDENTIFIER: HC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA X 2958
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA X 2959
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA X 2960
REMARK 800
REMARK 800 SITE_IDENTIFIER: IC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA X 2961
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZJR RELATED DB: PDB
REMARK 900 NATIVE D50S
REMARK 900 RELATED ID: 1NKW RELATED DB: PDB
REMARK 900 NATIVE D50S
REMARK 900 RELATED ID: 1SM1 RELATED DB: PDB
REMARK 900 D50S-SYNERCID
REMARK 900 RELATED ID: 3JQ4 RELATED DB: PDB
REMARK 900 D50S-LANKACIDIN
REMARK 900 RELATED ID: 1YI2 RELATED DB: PDB
REMARK 900 H50S-ERYTHROMYCIN
REMARK 900 RELATED ID: 3PIO RELATED DB: PDB
REMARK 900 D50S-LANKAMYCIN
DBREF1 3PIP X 1 2880 GB AE000513
DBREF2 3PIP X AE000513.1 2585058 2587937
DBREF1 3PIP Y 1 123 GB AE000513
DBREF2 3PIP Y AE000513.1 254392 254514
DBREF 3PIP A 3 275 UNP Q9RXJ9 RL2_DEIRA 2 275
DBREF 3PIP B 1 211 UNP Q9RXK2 RL3_DEIRA 1 211
DBREF 3PIP C 1 205 UNP Q9RXK1 RL4_DEIRA 1 205
DBREF 3PIP D 1 180 UNP Q9RXJ0 RL5_DEIRA 1 180
DBREF 3PIP E 1 185 UNP Q9RSL3 RL6_DEIRA 1 185
DBREF 3PIP F 1 144 UNP Q9RSS7 RL11_DEIRA 1 144
DBREF 3PIP G 1 174 UNP Q9RXY1 RL13_DEIRA 1 174
DBREF 3PIP H 1 134 UNP Q9RXJ2 RL14_DEIRA 1 134
DBREF 3PIP I 1 156 UNP Q9RSK9 RL15_DEIRA 1 156
DBREF 3PIP J 2 142 UNP Q9RXJ5 RL16_DEIRA 1 141
DBREF 3PIP K 1 116 UNP Q9RSJ5 RL17_DEIRA 1 116
DBREF 3PIP L 1 114 UNP Q9RSL2 RL18_DEIRA 1 114
DBREF 3PIP M 1 166 UNP Q9RWB4 RL19_DEIRA 1 166
DBREF 3PIP N 1 118 UNP Q9RSW7 RL20_DEIRA 1 118
DBREF 3PIP O 1 100 UNP Q9RY64 RL21_DEIRA 1 100
DBREF 3PIP P 1 134 UNP Q9RXJ7 RL22_DEIRA 1 134
DBREF 3PIP Q 1 95 UNP Q9RXK0 RL23_DEIRA 1 95
DBREF 3PIP R 1 115 UNP Q9RXJ1 RL24_DEIRA 1 115
DBREF 3PIP S 1 237 UNP Q9RX88 RL25_DEIRA 1 237
DBREF 3PIP T 1 91 UNP Q9RY65 RL27_DEIRA 1 91
DBREF 3PIP U 1 81 UNP Q9RRG8 RL28_DEIRA 1 81
DBREF 3PIP V 1 67 UNP Q9RXJ4 RL29_DEIRA 1 67
DBREF 3PIP W 1 55 UNP Q9RSL0 RL30_DEIRA 1 55
DBREF 3PIP Z 1 60 UNP P49228 RL32_DEIRA 1 60
DBREF 3PIP 1 1 55 UNP Q9RSS4 RL33_DEIRA 1 55
DBREF 3PIP 2 1 47 UNP Q9RSH2 RL34_DEIRA 1 47
DBREF 3PIP 3 1 66 UNP Q9RSW6 RL35_DEIRA 1 66
DBREF 3PIP 4 1 37 UNP Q9RSK0 RL36_DEIRA 1 37
SEQRES 1 X 2880 G G U C A A G A U A G U A
SEQRES 2 X 2880 A G G G U C C A C G G U G
SEQRES 3 X 2880 G A U G C C C U G G C G C
SEQRES 4 X 2880 U G G A G C C G A U G A A
SEQRES 5 X 2880 G G A C G C G A U U A C C
SEQRES 6 X 2880 U G C G A A A A G C C C C
SEQRES 7 X 2880 G A C G A G C U G G A G A
SEQRES 8 X 2880 U A C G C U U U G A C U C
SEQRES 9 X 2880 G G G G A U G U C C G A A
SEQRES 10 X 2880 U G G G G A A A C C C A C
SEQRES 11 X 2880 C U C G U A A G A G G U A
SEQRES 12 X 2880 U C C G C A A G G A U G G
SEQRES 13 X 2880 G A A C U C A G G G A A C
SEQRES 14 X 2880 U G A A A C A U C U C A G
SEQRES 15 X 2880 U A C C U G A A G G A G A
SEQRES 16 X 2880 A G A A A G A G A A U U C
SEQRES 17 X 2880 G A U U C C G U U A G U A
SEQRES 18 X 2880 G C G G C G A G C G A A C
SEQRES 19 X 2880 C C G G A U C A G C C C A
SEQRES 20 X 2880 A A C C G A A A C G C U U
SEQRES 21 X 2880 G C G U U U C G G G G U U
SEQRES 22 X 2880 G U A G G A C C A G U U U
SEQRES 23 X 2880 U U A A G A U U C A A C C
SEQRES 24 X 2880 C C U C A A G C C G A A G
SEQRES 25 X 2880 U G G C U G G A A A G C U
SEQRES 26 X 2880 A C A C C U C A G A A G G
SEQRES 27 X 2880 U G A G A G U C C U G U A
SEQRES 28 X 2880 G G C G A A C G A G C G G
SEQRES 29 X 2880 U U G A C U G U A C U G G
SEQRES 30 X 2880 C A C C U G A G U A G G U
SEQRES 31 X 2880 C G U U G U U C G U G A A
SEQRES 32 X 2880 A C G A U G A C U G A A U
SEQRES 33 X 2880 C C G C G C G G A C C A C
SEQRES 34 X 2880 C G C G C A A G G C U A A
SEQRES 35 X 2880 A U A C U C C C A G U G A
SEQRES 36 X 2880 C C G A U A G C G C A U A
SEQRES 37 X 2880 G U A C C G U G A G G G A
SEQRES 38 X 2880 A A G G U G A A A A G A A
SEQRES 39 X 2880 C C C C G G G A G G G G A
SEQRES 40 X 2880 G U G A A A G A G A A C C
SEQRES 41 X 2880 U G A A A C C G U G G A C
SEQRES 42 X 2880 U U A C A A G C A G U C A
SEQRES 43 X 2880 U G G C A C C U U A U G C
SEQRES 44 X 2880 G U G U U A U G G C G U G
SEQRES 45 X 2880 C C U A U U G A A G C A U
SEQRES 46 X 2880 G A G C C G G C G A C U U
SEQRES 47 X 2880 A G A C C U G A C G U G C
SEQRES 48 X 2880 G A G C U U A A G U U G A
SEQRES 49 X 2880 A A A A C G G A G G C G G
SEQRES 50 X 2880 A G C G A A A G C G A G U
SEQRES 51 X 2880 C C G A A U A G G G C G G
SEQRES 52 X 2880 C A U U A G U A C G U C G
SEQRES 53 X 2880 G G C U A G A C U C G A A
SEQRES 54 X 2880 A C C A G G U G A G C U A
SEQRES 55 X 2880 A G C A U G A C C A G G U
SEQRES 56 X 2880 U G A A A C C C C C G U G
SEQRES 57 X 2880 A C A G G G G G C G G A G
SEQRES 58 X 2880 G A C C G A A C C G G U G
SEQRES 59 X 2880 C C U G C U G A A A C A G
SEQRES 60 X 2880 U C U C G G A U G A G U U
SEQRES 61 X 2880 G U G U U U A G G A G U G
SEQRES 62 X 2880 A A A A G C U A A C C G A
SEQRES 63 X 2880 A C C U G G A G A U A G C
SEQRES 64 X 2880 U A G U U C U C C C C G A
SEQRES 65 X 2880 A A U G U A U U G A G G U
SEQRES 66 X 2880 A C A G C C U C G G A U G
SEQRES 67 X 2880 U U G A C C A U G U C C U
SEQRES 68 X 2880 G U A G A G C A C U C A C
SEQRES 69 X 2880 A A G G C U A G G G G G C
SEQRES 70 X 2880 C U A C C A G C U U A C C
SEQRES 71 X 2880 A A A C C U U A U G A A A
SEQRES 72 X 2880 C U C C G A A G G G G C A
SEQRES 73 X 2880 C G C G U U U A G U C C G
SEQRES 74 X 2880 G G A G U G A G G C U G C
SEQRES 75 X 2880 G A G A G C U A A C U U C
SEQRES 76 X 2880 C G U A G C C G A G A G G
SEQRES 77 X 2880 G A A A C A A C C C A G A
SEQRES 78 X 2880 C C A U C A G C U A A G G
SEQRES 79 X 2880 U C C C U A A A U G A U C
SEQRES 80 X 2880 G C U C A G U G G U U A A
SEQRES 81 X 2880 G G A U G U G U C G U C G
SEQRES 82 X 2880 C A U A G A C A G C C A G
SEQRES 83 X 2880 G A G G U U G G C U U A G
SEQRES 84 X 2880 A A G C A G C C A C C C U
SEQRES 85 X 2880 U C A A A G A G U G C G U
SEQRES 86 X 2880 A A U A G C U C A C U G G
SEQRES 87 X 2880 U C G A G U G A C G A U G
SEQRES 88 X 2880 C G C C G A A A A U G A U
SEQRES 89 X 2880 C G G G G C U C A A G U G
SEQRES 90 X 2880 A U C U A C C G A A G C U
SEQRES 91 X 2880 A U G G A U U C A A C U C
SEQRES 92 X 2880 G C G A A G C G A G U U G
SEQRES 93 X 2880 U C U G G U A G G G G A G
SEQRES 94 X 2880 C G U U C A G U C C G C G
SEQRES 95 X 2880 G A G A A G C C A U A C C
SEQRES 96 X 2880 G G A A G G A G U G G U G
SEQRES 97 X 2880 G A G C C G A C U G A A G
SEQRES 98 X 2880 U G C G G A U G C C G G C
SEQRES 99 X 2880 A U G A G U A A C G A U A
SEQRES 100 X 2880 A A A G A A G U G A G A A
SEQRES 101 X 2880 U C U U C U U C G C C G U
SEQRES 102 X 2880 A A G G A C A A G G G U U
SEQRES 103 X 2880 C C U G G G G A A G G G U
SEQRES 104 X 2880 C G U C C G C C C A G G G
SEQRES 105 X 2880 A A A G U C G G G A C C U
SEQRES 106 X 2880 A A G G U G A G G C C G A
SEQRES 107 X 2880 A C G G C G C A G C C G A
SEQRES 108 X 2880 U G G A C A G C A G G U C
SEQRES 109 X 2880 A A G A U U C C U G C A C
SEQRES 110 X 2880 C G A U C A U G U G G A G
SEQRES 111 X 2880 U G A U G G A G G G A C G
SEQRES 112 X 2880 C A U U A C G C U A U C C
SEQRES 113 X 2880 A A U G C C A A G C U A U
SEQRES 114 X 2880 G G C U A U G C U G G U U
SEQRES 115 X 2880 G G U A C G C U C A A G G
SEQRES 116 X 2880 G C G A U C G G G U C A G
SEQRES 117 X 2880 A A A A U C U A C C G G U
SEQRES 118 X 2880 C A C A U G C C U C A G A
SEQRES 119 X 2880 C G U A U C G G G A G C U
SEQRES 120 X 2880 U C C U C G G A A G C G A
SEQRES 121 X 2880 A G U U G G A A A C G C G
SEQRES 122 X 2880 A C G G U G C C A A G A A
SEQRES 123 X 2880 A A G C U U C U A A A C G
SEQRES 124 X 2880 U U G A A A C A U G A U U
SEQRES 125 X 2880 G C C C G U A C C G C A A
SEQRES 126 X 2880 A C C G A C A C A G G U G
SEQRES 127 X 2880 U C C G A G U G U C A A U
SEQRES 128 X 2880 G C A C U A A G G C G C G
SEQRES 129 X 2880 C G A G A G A A C C C U C
SEQRES 130 X 2880 G U U A A G G A A C U U U
SEQRES 131 X 2880 G C A A U C U C A C C C C
SEQRES 132 X 2880 G U A A C U U C G G A A G
SEQRES 133 X 2880 A A G G G G U C C C C A C
SEQRES 134 X 2880 G C U U C G C G U G G G G
SEQRES 135 X 2880 C G C A G U G A A U A G G
SEQRES 136 X 2880 C C C A G G C G A C U G U
SEQRES 137 X 2880 U U A C C A A A A U C A C
SEQRES 138 X 2880 A G C A C U C U G C C A A
SEQRES 139 X 2880 C A C G A A C A G U G G A
SEQRES 140 X 2880 C G U A U A G G G U G U G
SEQRES 141 X 2880 A C G C C U G C C C G G U
SEQRES 142 X 2880 G C C G G A A G G U C A A
SEQRES 143 X 2880 G U G G A G C G G U G C A
SEQRES 144 X 2880 A G C U G C G A A A U G A
SEQRES 145 X 2880 A G C C C C G G U G A A C
SEQRES 146 X 2880 G G C G G C C G U A A C U
SEQRES 147 X 2880 A U A A C G G U C C U A A
SEQRES 148 X 2880 G G U A G C G A A A U U C
SEQRES 149 X 2880 C U U G U C G G G U A A G
SEQRES 150 X 2880 U U C C G A C C U G C A C
SEQRES 151 X 2880 G A A A G G C G U A A C G
SEQRES 152 X 2880 A U C U G G G C G C U G U
SEQRES 153 X 2880 C U C A A C G A G G G A C
SEQRES 154 X 2880 U C G G U G A A A U U G A
SEQRES 155 X 2880 A U U G G C U G U A A A G
SEQRES 156 X 2880 A U G C G G C C U A C C C
SEQRES 157 X 2880 G U A G C A G G A C G A A
SEQRES 158 X 2880 A A G A C C C C G U G G A
SEQRES 159 X 2880 G C U U U A C U A U A G U
SEQRES 160 X 2880 C U G G C A U U G G G A U
SEQRES 161 X 2880 U C G G G U U U C U C U G
SEQRES 162 X 2880 C G U A G G A U A G G U G
SEQRES 163 X 2880 G G A G C C U G C G A A A
SEQRES 164 X 2880 C U G G C C U U U U G G G
SEQRES 165 X 2880 G U C G G U G G A G G C A
SEQRES 166 X 2880 A C G G U G A A A U A C C
SEQRES 167 X 2880 A C C C U G A G A A A C U
SEQRES 168 X 2880 U G G A U U U C U A A C C
SEQRES 169 X 2880 U G A A A A A U C A C U U
SEQRES 170 X 2880 U C G G G G A C C G U G C
SEQRES 171 X 2880 U U G G C G G G U A G U U
SEQRES 172 X 2880 U G A C U G G G G C G G U
SEQRES 173 X 2880 C G C C U C C C A A A A U
SEQRES 174 X 2880 G U A A C G G A G G C G C
SEQRES 175 X 2880 C C A A A G G U C A C C U
SEQRES 176 X 2880 C A A G A C G G U U G G A
SEQRES 177 X 2880 A A U C G U C U G U A G A
SEQRES 178 X 2880 G C G C A A A G G U A G A
SEQRES 179 X 2880 A G G U G G C U U G A C U
SEQRES 180 X 2880 G C G A G A C U G A C A C
SEQRES 181 X 2880 G U C G A G C A G G G A G
SEQRES 182 X 2880 G A A A C U C G G G C U U
SEQRES 183 X 2880 A G U G A A C C G G U G G
SEQRES 184 X 2880 U A C C G U G U G G A A G
SEQRES 185 X 2880 G G C C A U C G A U C A A
SEQRES 186 X 2880 C G G A U A A A A G U U A
SEQRES 187 X 2880 C C C C G G G G A U A A C
SEQRES 188 X 2880 A G G C U G A U C U C C C
SEQRES 189 X 2880 C C G A G A G U C C A U A
SEQRES 190 X 2880 U C G G C G G G G A G G U
SEQRES 191 X 2880 U U G G C A C C U C G A U
SEQRES 192 X 2880 G U C G G C U C G U C G C
SEQRES 193 X 2880 A U C C U G G G G C U G A
SEQRES 194 X 2880 A G A A G G U C C C A A G
SEQRES 195 X 2880 G G U U G G G C U G U U C
SEQRES 196 X 2880 G C C C A U U A A A G C G
SEQRES 197 X 2880 G C A C G C G A G C U G G
SEQRES 198 X 2880 G U U C A G A A C G U C G
SEQRES 199 X 2880 U G A G A C A G U U C G G
SEQRES 200 X 2880 U C U C U A U C C G C U A
SEQRES 201 X 2880 C G G G C G C A G G A G A
SEQRES 202 X 2880 A U U G A G G G G A G U U
SEQRES 203 X 2880 G C U C C U A G U A C G A
SEQRES 204 X 2880 G A G G A C C G G A G U G
SEQRES 205 X 2880 A A C G G A C C G C U G G
SEQRES 206 X 2880 U C U C C C U G C U G U C
SEQRES 207 X 2880 G U A C C A A C G G C A C
SEQRES 208 X 2880 A U G C A G G G U A G C U
SEQRES 209 X 2880 A U G U C C G G A A C G G
SEQRES 210 X 2880 A U A A C C G C U G A A A
SEQRES 211 X 2880 G C A U C U A A G C G G G
SEQRES 212 X 2880 A A G C C A G C C C C A A
SEQRES 213 X 2880 G A U G A G U U C U C C C
SEQRES 214 X 2880 A C U G U U U A U C A G G
SEQRES 215 X 2880 U A A G A C U C C C G G A
SEQRES 216 X 2880 A G A C C A C C G G G U U
SEQRES 217 X 2880 A A G A G G C C A G G C G
SEQRES 218 X 2880 U G C A C G C A U A G C A
SEQRES 219 X 2880 A U G U G U U C A G C G G
SEQRES 220 X 2880 A C U G G U G C U C A U C
SEQRES 221 X 2880 A G U C G A G G U C U U G
SEQRES 222 X 2880 A C C A C U C
SEQRES 1 Y 123 A C A C C C C C G U G C C
SEQRES 2 Y 123 C A U A G C A C U G U G G
SEQRES 3 Y 123 A A C C A C C C C A C C C
SEQRES 4 Y 123 C A U G C C G A A C U G G
SEQRES 5 Y 123 G U C G U G A A A C A C A
SEQRES 6 Y 123 G C A G C G C C A A U G A
SEQRES 7 Y 123 U A C U C G G A C C G C A
SEQRES 8 Y 123 G G G U C C C G G A A A A
SEQRES 9 Y 123 G U C G G U C A G C G C G
SEQRES 10 Y 123 G G G G U U
SEQRES 1 A 274 ALA VAL LYS LYS TYR ARG PRO TYR THR PRO SER ARG ARG
SEQRES 2 A 274 GLN MET THR THR ALA ASP PHE SER GLY LEU THR LYS LYS
SEQRES 3 A 274 ARG PRO GLU LYS ALA LEU THR GLU ALA LEU PRO LYS THR
SEQRES 4 A 274 GLY GLY ARG ASN ASN ARG GLY ARG ILE THR SER ARG PHE
SEQRES 5 A 274 ILE GLY GLY GLY HIS LYS ARG LEU TYR ARG ILE ILE ASP
SEQRES 6 A 274 PHE LYS ARG ARG ASP LYS SER GLY VAL ASN ALA LYS VAL
SEQRES 7 A 274 ALA ALA ILE GLU TYR ASP PRO ASN ARG SER ALA ARG ILE
SEQRES 8 A 274 ALA LEU LEU HIS TYR ALA ASP GLY GLU LYS ARG TYR ILE
SEQRES 9 A 274 LEU ALA PRO GLU GLY LEU THR VAL GLY ALA THR VAL ASN
SEQRES 10 A 274 ALA GLY PRO GLU ALA GLU PRO LYS LEU GLY ASN ALA LEU
SEQRES 11 A 274 PRO LEU ARG PHE VAL PRO VAL GLY ALA VAL VAL HIS ALA
SEQRES 12 A 274 LEU GLU LEU VAL PRO GLY LYS GLY ALA GLN LEU ALA ARG
SEQRES 13 A 274 SER ALA GLY THR SER VAL GLN VAL GLN GLY LYS GLU SER
SEQRES 14 A 274 ASP TYR VAL ILE VAL ARG LEU PRO SER GLY GLU LEU ARG
SEQRES 15 A 274 ARG VAL HIS SER GLU CYS TYR ALA THR ILE GLY ALA VAL
SEQRES 16 A 274 GLY ASN ALA GLU HIS LYS ASN ILE VAL LEU GLY LYS ALA
SEQRES 17 A 274 GLY ARG SER ARG TRP LEU GLY ARG LYS PRO HIS GLN ARG
SEQRES 18 A 274 GLY SER ALA MET ASN PRO VAL ASP HIS PRO HIS GLY GLY
SEQRES 19 A 274 GLY GLU GLY ARG THR GLY ALA GLY ARG VAL PRO VAL THR
SEQRES 20 A 274 PRO TRP GLY LYS PRO THR LYS GLY LEU LYS THR ARG ARG
SEQRES 21 A 274 LYS ARG LYS THR SER ASP ARG PHE ILE VAL THR ARG ARG
SEQRES 22 A 274 LYS
SEQRES 1 B 211 MET LYS GLY ILE LEU GLY THR LYS ILE GLY MET THR GLN
SEQRES 2 B 211 ILE TRP LYS ASN ASP ARG ALA ILE PRO VAL THR VAL VAL
SEQRES 3 B 211 LEU ALA GLY PRO CYS PRO ILE VAL GLN ARG LYS THR ALA
SEQRES 4 B 211 GLN THR ASP GLY TYR GLU ALA VAL GLN ILE GLY TYR ALA
SEQRES 5 B 211 PRO LYS ALA GLU ARG LYS VAL ASN LYS PRO MET GLN GLY
SEQRES 6 B 211 HIS PHE ALA LYS ALA GLY VAL ALA PRO THR ARG ILE LEU
SEQRES 7 B 211 ARG GLU PHE ARG GLY PHE ALA PRO ASP GLY ASP SER VAL
SEQRES 8 B 211 ASN VAL ASP ILE PHE ALA GLU GLY GLU LYS ILE ASP ALA
SEQRES 9 B 211 THR GLY THR SER LYS GLY LYS GLY THR GLN GLY VAL MET
SEQRES 10 B 211 LYS ARG TRP ASN PHE ALA GLY GLY PRO ALA SER HIS GLY
SEQRES 11 B 211 SER LYS LYS TRP HIS ARG ARG PRO GLY SER ILE GLY GLN
SEQRES 12 B 211 ARG LYS THR PRO GLY ARG VAL TYR LYS GLY LYS ARG MET
SEQRES 13 B 211 ALA GLY HIS MET GLY MET GLU ARG VAL THR VAL GLN ASN
SEQRES 14 B 211 LEU GLU VAL VAL GLU ILE ARG ALA GLY GLU ASN LEU ILE
SEQRES 15 B 211 LEU VAL LYS GLY ALA ILE PRO GLY ALA ASN GLY GLY LEU
SEQRES 16 B 211 VAL VAL LEU ARG SER ALA ALA LYS ALA SER ALA ALA LYS
SEQRES 17 B 211 GLY GLY LYS
SEQRES 1 C 205 MET ALA GLN ILE ASN VAL ILE GLY GLN ASN GLY GLY ARG
SEQRES 2 C 205 THR ILE GLU LEU PRO LEU PRO GLU VAL ASN SER GLY VAL
SEQRES 3 C 205 LEU HIS GLU VAL VAL THR TRP GLN LEU ALA SER ARG ARG
SEQRES 4 C 205 ARG GLY THR ALA SER THR ARG THR ARG ALA GLN VAL SER
SEQRES 5 C 205 LYS THR GLY ARG LYS MET TYR GLY GLN LYS GLY THR GLY
SEQRES 6 C 205 ASN ALA ARG HIS GLY ASP ARG SER VAL PRO THR PHE VAL
SEQRES 7 C 205 GLY GLY GLY VAL ALA PHE GLY PRO LYS PRO ARG SER TYR
SEQRES 8 C 205 ASP TYR THR LEU PRO ARG GLN VAL ARG GLN LEU GLY LEU
SEQRES 9 C 205 ALA MET ALA ILE ALA SER ARG GLN GLU GLY GLY LYS LEU
SEQRES 10 C 205 VAL ALA VAL ASP GLY PHE ASP ILE ALA ASP ALA LYS THR
SEQRES 11 C 205 LYS ASN PHE ILE SER TRP ALA LYS GLN ASN GLY LEU ASP
SEQRES 12 C 205 GLY THR GLU LYS VAL LEU LEU VAL THR ASP ASP GLU ASN
SEQRES 13 C 205 THR ARG ARG ALA ALA ARG ASN VAL SER TRP VAL SER VAL
SEQRES 14 C 205 LEU PRO VAL ALA GLY VAL ASN VAL TYR ASP ILE LEU ARG
SEQRES 15 C 205 HIS ASP ARG LEU VAL ILE ASP ALA ALA ALA LEU GLU ILE
SEQRES 16 C 205 VAL GLU GLU GLU ALA GLY GLU GLU GLN GLN
SEQRES 1 D 180 MET GLN GLN LEU LYS THR LYS TYR ASN ASP GLN VAL ARG
SEQRES 2 D 180 PRO ALA LEU MET GLN GLN PHE GLY TYR SER SER VAL MET
SEQRES 3 D 180 ALA VAL PRO ARG ILE GLU LYS ILE VAL VAL ASN GLU GLY
SEQRES 4 D 180 LEU GLY SER SER LYS GLU ASP SER LYS ALA ILE ASP LYS
SEQRES 5 D 180 ALA ALA LYS GLU LEU ALA LEU ILE THR LEU GLN LYS PRO
SEQRES 6 D 180 ILE ILE THR LYS ALA LYS LYS SER ILE SER ASN PHE LYS
SEQRES 7 D 180 LEU ARG GLN GLY MET PRO VAL GLY ILE LYS VAL THR LEU
SEQRES 8 D 180 ARG GLY GLU ARG MET TYR VAL PHE LEU GLU LYS LEU ILE
SEQRES 9 D 180 ASN ILE GLY LEU PRO ARG ILE ARG ASP PHE ARG GLY ILE
SEQRES 10 D 180 ASN PRO ASN ALA PHE ASP GLY ARG GLY ASN TYR ASN LEU
SEQRES 11 D 180 GLY ILE LYS GLU GLN LEU ILE PHE PRO GLU ILE THR TYR
SEQRES 12 D 180 ASP MET VAL ASP LYS THR ARG GLY MET ASP ILE THR ILE
SEQRES 13 D 180 VAL THR THR ALA LYS THR ASP GLU GLU ALA ARG ALA LEU
SEQRES 14 D 180 LEU GLN SER MET GLY LEU PRO PHE ARG LYS GLN
SEQRES 1 E 185 MET SER ARG ILE GLY LYS GLN PRO ILE ALA VAL PRO SER
SEQRES 2 E 185 GLY VAL THR VAL ASN ALA GLN ASP GLY VAL PHE LYS VAL
SEQRES 3 E 185 LYS GLY PRO LYS GLY GLU LEU THR VAL PRO TYR ASN THR
SEQRES 4 E 185 GLU LEU THR VAL ARG GLN ASP GLY ASP GLN LEU LEU VAL
SEQRES 5 E 185 GLU ARG PRO SER ASP ALA GLN LYS HIS ARG ALA LEU HIS
SEQRES 6 E 185 GLY LEU THR ARG THR LEU VAL ALA ASN ALA VAL LYS GLY
SEQRES 7 E 185 VAL SER ASP GLY TYR THR ILE ASN LEU GLU LEU ARG GLY
SEQRES 8 E 185 VAL GLY PHE ARG ALA LYS LEU THR GLY LYS ALA LEU GLU
SEQRES 9 E 185 MET ASN ILE GLY TYR SER HIS PRO VAL ILE ILE GLU PRO
SEQRES 10 E 185 PRO ALA GLY VAL THR PHE ALA VAL PRO GLU PRO THR ARG
SEQRES 11 E 185 ILE ASP VAL SER GLY ILE ASP LYS GLN LEU VAL GLY GLN
SEQRES 12 E 185 VAL ALA ALA ASN VAL ARG LYS VAL ARG LYS PRO ASP ALA
SEQRES 13 E 185 TYR HIS GLY LYS GLY VAL ARG PHE VAL GLY GLU GLN ILE
SEQRES 14 E 185 ALA LEU LYS ALA GLY LYS ALA GLY ALA THR GLY GLY LYS
SEQRES 15 E 185 GLY LYS LYS
SEQRES 1 F 144 MET LYS LYS VAL ALA GLY ILE VAL LYS LEU GLN LEU PRO
SEQRES 2 F 144 ALA GLY LYS ALA THR PRO ALA PRO PRO VAL GLY PRO ALA
SEQRES 3 F 144 LEU GLY GLN TYR GLY ALA ASN ILE MET GLU PHE THR LYS
SEQRES 4 F 144 ALA PHE ASN ALA GLN THR ALA ASP LYS GLY ASP ALA ILE
SEQRES 5 F 144 ILE PRO VAL GLU ILE THR ILE TYR ALA ASP ARG SER PHE
SEQRES 6 F 144 THR PHE ILE THR LYS THR PRO PRO MET SER TYR LEU ILE
SEQRES 7 F 144 ARG LYS ALA ALA GLY ILE GLY LYS GLY SER SER THR PRO
SEQRES 8 F 144 ASN LYS ALA LYS VAL GLY LYS LEU ASN TRP ASP GLN VAL
SEQRES 9 F 144 LEU GLU ILE ALA LYS THR LYS MET PRO ASP LEU ASN ALA
SEQRES 10 F 144 GLY SER VAL GLU ALA ALA ALA ASN THR VAL ALA GLY THR
SEQRES 11 F 144 ALA ARG SER MET GLY VAL THR VAL GLU GLY GLY PRO ASN
SEQRES 12 F 144 ALA
SEQRES 1 G 174 MET ALA PHE PRO ASP THR ASP VAL SER PRO PRO ARG GLY
SEQRES 2 G 174 GLY PRO SER SER PRO ALA LYS SER PRO LEU LEU ARG SER
SEQRES 3 G 174 PHE LYS VAL LYS THR TYR ILE PRO LYS ASN ASP GLU GLN
SEQRES 4 G 174 ASN TRP VAL VAL VAL ASP ALA SER GLY VAL PRO LEU GLY
SEQRES 5 G 174 ARG LEU ALA THR LEU ILE ALA SER ARG ILE ARG GLY LYS
SEQRES 6 G 174 HIS ARG PRO ASP PHE THR PRO ASN MET ILE GLN GLY ASP
SEQRES 7 G 174 PHE VAL VAL VAL ILE ASN ALA ALA GLN VAL ALA LEU THR
SEQRES 8 G 174 GLY LYS LYS LEU ASP ASP LYS VAL TYR THR ARG TYR THR
SEQRES 9 G 174 GLY TYR GLN GLY GLY LEU LYS THR GLU THR ALA ARG GLU
SEQRES 10 G 174 ALA LEU SER LYS HIS PRO GLU ARG VAL ILE GLU HIS ALA
SEQRES 11 G 174 VAL PHE GLY MET LEU PRO LYS GLY ARG GLN GLY ARG ALA
SEQRES 12 G 174 MET HIS THR ARG LEU LYS VAL TYR ALA GLY GLU THR HIS
SEQRES 13 G 174 PRO HIS SER ALA GLN LYS PRO GLN VAL LEU LYS THR GLN
SEQRES 14 G 174 PRO LEU GLU VAL LYS
SEQRES 1 H 134 MET ILE MET PRO GLN SER ARG LEU ASP VAL ALA ASP ASN
SEQRES 2 H 134 SER GLY ALA ARG GLU ILE MET CYS ILE ARG VAL LEU ASN
SEQRES 3 H 134 SER GLY ILE GLY GLY LYS GLY LEU THR THR GLY GLY GLY
SEQRES 4 H 134 GLY ASN LYS ARG TYR ALA HIS VAL GLY ASP ILE ILE VAL
SEQRES 5 H 134 ALA SER VAL LYS ASP ALA ALA PRO ARG GLY ALA VAL LYS
SEQRES 6 H 134 ALA GLY ASP VAL VAL LYS ALA VAL VAL VAL ARG THR SER
SEQRES 7 H 134 HIS ALA ILE LYS ARG ALA ASP GLY SER THR ILE ARG PHE
SEQRES 8 H 134 ASP ARG ASN ALA ALA VAL ILE ILE ASN ASN GLN GLY GLU
SEQRES 9 H 134 PRO ARG GLY THR ARG VAL PHE GLY PRO VAL ALA ARG GLU
SEQRES 10 H 134 LEU ARG ASP ARG ARG PHE MET LYS ILE VAL SER LEU ALA
SEQRES 11 H 134 PRO GLU VAL LEU
SEQRES 1 I 156 MET LYS LEU HIS ASP LEU LYS PRO THR PRO GLY SER ARG
SEQRES 2 I 156 LYS ASP ARG LYS ARG VAL GLY ARG GLY PRO GLY GLY THR
SEQRES 3 I 156 ASP LYS THR ALA GLY ARG GLY HIS LYS GLY GLN LYS SER
SEQRES 4 I 156 ARG SER GLY ALA GLY LYS GLY ALA PHE PHE GLU GLY GLY
SEQRES 5 I 156 ARG SER ARG LEU ILE ALA ARG LEU PRO LYS ARG GLY PHE
SEQRES 6 I 156 ASN ASN VAL GLY THR THR TYR GLU VAL VAL LYS LEU SER
SEQRES 7 I 156 GLN LEU GLN ASP LEU GLU ASP THR THR PHE ASP ARG ASP
SEQRES 8 I 156 THR LEU GLU ALA TYR ARG LEU VAL ARG ARG LYS ASN ARG
SEQRES 9 I 156 PRO VAL LYS LEU LEU ALA SER GLY GLU ILE SER ARG ALA
SEQRES 10 I 156 VAL THR VAL HIS VAL ASP ALA ALA SER ALA ALA ALA ILE
SEQRES 11 I 156 LYS ALA VAL GLU ALA ALA GLY GLY ARG VAL VAL LEU PRO
SEQRES 12 I 156 GLU VAL GLN THR GLN GLN ASP ASP ALA GLN LYS ALA GLU
SEQRES 1 J 141 MET LEU LEU PRO LYS ARG THR LYS PHE ARG LYS GLN PHE
SEQRES 2 J 141 ARG GLY ARG MET THR GLY ASP ALA LYS GLY GLY ASP TYR
SEQRES 3 J 141 VAL ALA PHE GLY ASP TYR GLY LEU ILE ALA MET GLU PRO
SEQRES 4 J 141 ALA TRP ILE LYS SER ASN GLN ILE GLU ALA CYS ARG ILE
SEQRES 5 J 141 VAL MET SER ARG HIS PHE ARG ARG GLY GLY LYS ILE TYR
SEQRES 6 J 141 ILE ARG ILE PHE PRO ASP LYS PRO VAL THR LYS LYS PRO
SEQRES 7 J 141 ALA GLU THR ARG MET GLY LYS GLY LYS GLY ALA VAL GLU
SEQRES 8 J 141 TYR TRP VAL SER VAL VAL LYS PRO GLY ARG VAL MET PHE
SEQRES 9 J 141 GLU VAL ALA GLY VAL THR GLU GLU GLN ALA LYS GLU ALA
SEQRES 10 J 141 PHE ARG LEU ALA GLY HIS LYS LEU PRO ILE GLN THR LYS
SEQRES 11 J 141 MET VAL LYS ARG GLU VAL TYR ASP GLU ALA GLN
SEQRES 1 K 116 MET ARG HIS GLY LYS ALA GLY ARG LYS LEU ASN ARG ASN
SEQRES 2 K 116 SER SER ALA ARG VAL ALA LEU ALA ARG ALA GLN ALA THR
SEQRES 3 K 116 ALA LEU LEU ARG GLU GLY ARG ILE GLN THR THR LEU THR
SEQRES 4 K 116 LYS ALA LYS GLU LEU ARG PRO PHE VAL GLU GLN LEU ILE
SEQRES 5 K 116 THR THR ALA LYS GLY GLY ASP LEU HIS SER ARG ARG LEU
SEQRES 6 K 116 VAL ALA GLN ASP ILE HIS ASP LYS ASP VAL VAL ARG LYS
SEQRES 7 K 116 VAL MET ASP GLU VAL ALA PRO LYS TYR ALA GLU ARG PRO
SEQRES 8 K 116 GLY GLY TYR THR ARG ILE LEU ARG VAL GLY THR ARG ARG
SEQRES 9 K 116 GLY ASP GLY VAL THR MET ALA LEU ILE GLU LEU VAL
SEQRES 1 L 114 MET ALA THR ALA THR THR ILE ARG ARG LYS LEU ARG THR
SEQRES 2 L 114 ARG ARG LYS VAL ARG THR THR THR ALA ALA SER GLY ARG
SEQRES 3 L 114 LEU ARG LEU SER VAL TYR ARG SER SER LYS HIS ILE TYR
SEQRES 4 L 114 ALA GLN ILE ILE ASP ASP SER ARG GLY GLN THR LEU ALA
SEQRES 5 L 114 ALA ALA SER SER ALA ALA LEU LYS SER GLY ASN LYS THR
SEQRES 6 L 114 ASP THR ALA ALA ALA VAL GLY LYS ALA LEU ALA ALA ALA
SEQRES 7 L 114 ALA ALA GLU LYS GLY ILE LYS GLN VAL VAL PHE ASP ARG
SEQRES 8 L 114 GLY SER TYR LYS TYR HIS GLY ARG VAL LYS ALA LEU ALA
SEQRES 9 L 114 ASP ALA ALA ARG GLU GLY GLY LEU ASP PHE
SEQRES 1 M 166 MET GLN THR HIS ILE LYS ILE ASN ARG GLY GLU LEU LEU
SEQRES 2 M 166 ARG GLY ILE GLU GLN ASP HIS THR ARG GLN LEU PRO ASP
SEQRES 3 M 166 PHE ARG PRO GLY ASP THR VAL ARG VAL ASP THR LYS VAL
SEQRES 4 M 166 ARG GLU GLY ASN ARG THR ARG SER GLN ALA PHE GLU GLY
SEQRES 5 M 166 VAL VAL ILE ALA ILE ASN GLY SER GLY SER ARG LYS SER
SEQRES 6 M 166 PHE THR VAL ARG LYS ILE SER PHE GLY GLU GLY VAL GLU
SEQRES 7 M 166 ARG VAL PHE PRO PHE ALA SER PRO LEU VAL ASN GLN VAL
SEQRES 8 M 166 THR ILE VAL GLU ARG GLY LYS VAL ARG ARG ALA LYS LEU
SEQRES 9 M 166 TYR TYR LEU ARG GLU LEU ARG GLY LYS ALA ALA ARG ILE
SEQRES 10 M 166 LYS SER ASP ARG SER ARG VAL MET LYS ASP ALA ALA ARG
SEQRES 11 M 166 ALA GLN GLN ASP LYS ALA ASN ALA SER ALA SER GLN ALA
SEQRES 12 M 166 ALA ALA ALA GLN ALA ASP VAL THR VAL ILE SER ALA ALA
SEQRES 13 M 166 PRO GLU VAL ALA PRO GLU THR GLN GLY GLU
SEQRES 1 N 118 MET PRO ARG ALA LYS THR GLY ILE VAL ARG ARG ARG ARG
SEQRES 2 N 118 HIS LYS LYS VAL LEU LYS ARG ALA LYS GLY PHE TRP GLY
SEQRES 3 N 118 SER ARG SER LYS GLN TYR ARG ASN ALA PHE GLN THR LEU
SEQRES 4 N 118 LEU ASN ALA ALA THR TYR GLU TYR ARG ASP ARG ARG ASN
SEQRES 5 N 118 LYS LYS ARG ASP PHE ARG ARG LEU TRP ILE GLN ARG ILE
SEQRES 6 N 118 ASN ALA GLY ALA ARG LEU HIS GLY MET ASN TYR SER THR
SEQRES 7 N 118 PHE ILE ASN GLY LEU LYS ARG ALA ASN ILE ASP LEU ASN
SEQRES 8 N 118 ARG LYS VAL LEU ALA ASP ILE ALA ALA ARG GLU PRO GLU
SEQRES 9 N 118 ALA PHE LYS ALA LEU VAL ASP ALA SER ARG ASN ALA ARG
SEQRES 10 N 118 GLN
SEQRES 1 O 100 MET PHE ALA ILE ILE GLN THR GLY GLY LYS GLN TYR ARG
SEQRES 2 O 100 VAL SER GLU GLY ASP VAL ILE ARG VAL GLU SER LEU GLN
SEQRES 3 O 100 GLY GLU ALA GLY ASP LYS VAL GLU LEU LYS ALA LEU PHE
SEQRES 4 O 100 VAL GLY GLY GLU GLN THR VAL PHE GLY GLU ASP ALA GLY
SEQRES 5 O 100 LYS TYR THR VAL GLN ALA GLU VAL VAL GLU HIS GLY ARG
SEQRES 6 O 100 GLY LYS LYS ILE TYR ILE ARG LYS TYR LYS SER GLY VAL
SEQRES 7 O 100 GLN TYR ARG ARG ARG THR GLY HIS ARG GLN ASN PHE THR
SEQRES 8 O 100 ALA ILE LYS ILE LEU GLY ILE GLN GLY
SEQRES 1 P 134 MET THR ALA PRO GLU GLN THR PHE ARG ASN LYS LYS GLN
SEQRES 2 P 134 ARG LYS GLN GLN VAL LYS LEU ARG LYS PRO GLY PHE ALA
SEQRES 3 P 134 VAL ALA LYS TYR VAL ARG MET SER PRO ARG LYS VAL ARG
SEQRES 4 P 134 LEU VAL VAL ASP VAL ILE ARG GLY LYS SER VAL GLN ASP
SEQRES 5 P 134 ALA GLU ASP LEU LEU ARG PHE ILE PRO ARG SER ALA SER
SEQRES 6 P 134 GLU PRO VAL ALA LYS VAL LEU ASN SER ALA LYS ALA ASN
SEQRES 7 P 134 ALA LEU HIS ASN ASP GLU MET LEU GLU ASP ARG LEU PHE
SEQRES 8 P 134 VAL LYS GLU ALA TYR VAL ASP ALA GLY PRO THR LEU LYS
SEQRES 9 P 134 ARG LEU ILE PRO ARG ALA ARG GLY SER ALA ASN ILE ILE
SEQRES 10 P 134 LYS LYS ARG THR SER HIS ILE THR ILE ILE VAL ALA GLU
SEQRES 11 P 134 LYS GLY ASN LYS
SEQRES 1 Q 95 MET SER HIS TYR ASP ILE LEU GLN ALA PRO VAL ILE SER
SEQRES 2 Q 95 GLU LYS ALA TYR SER ALA MET GLU ARG GLY VAL TYR SER
SEQRES 3 Q 95 PHE TRP VAL SER PRO LYS ALA THR LYS THR GLU ILE LYS
SEQRES 4 Q 95 ASP ALA ILE GLN GLN ALA PHE GLY VAL ARG VAL ILE GLY
SEQRES 5 Q 95 ILE SER THR MET ASN VAL PRO GLY LYS ARG LYS ARG VAL
SEQRES 6 Q 95 GLY ARG PHE ILE GLY GLN ARG ASN ASP ARG LYS LYS ALA
SEQRES 7 Q 95 ILE VAL ARG LEU ALA GLU GLY GLN SER ILE GLU ALA LEU
SEQRES 8 Q 95 ALA GLY GLN ALA
SEQRES 1 R 115 MET PRO ARG PRO SER ALA GLY SER HIS HIS ASN ASP LYS
SEQRES 2 R 115 LEU HIS PHE LYS LYS GLY ASP THR VAL ILE VAL LEU SER
SEQRES 3 R 115 GLY LYS HIS LYS GLY GLN THR GLY LYS VAL LEU LEU ALA
SEQRES 4 R 115 LEU PRO ARG ASP GLN LYS VAL VAL VAL GLU GLY VAL ASN
SEQRES 5 R 115 VAL ILE THR LYS ASN VAL LYS PRO SER MET THR ASN PRO
SEQRES 6 R 115 GLN GLY GLY GLN GLU GLN ARG GLU LEU ALA LEU HIS ALA
SEQRES 7 R 115 SER LYS VAL ALA LEU VAL ASP PRO GLU THR GLY LYS ALA
SEQRES 8 R 115 THR ARG VAL ARG LYS GLN ILE VAL ASP GLY LYS LYS VAL
SEQRES 9 R 115 ARG VAL ALA VAL ALA SER GLY LYS THR ILE ASP
SEQRES 1 S 237 MET GLU LEU THR ALA LYS PRO ARG THR PRO LYS GLN LYS
SEQRES 2 S 237 LEU ASP GLU SER MET ILE ALA ALA VAL ALA TYR ASN LYS
SEQRES 3 S 237 GLU ASN ASN VAL SER PHE ALA LEU ASP ARG LYS ALA PHE
SEQRES 4 S 237 ASP ARG ALA PHE ARG GLN GLN SER THR THR GLY LEU PHE
SEQRES 5 S 237 ASP ILE THR VAL GLU GLY GLY GLU THR PHE PRO ALA LEU
SEQRES 6 S 237 VAL LYS ALA VAL GLN MET ASP LYS ARG LYS ARG ALA PRO
SEQRES 7 S 237 ILE HIS VAL ASP PHE TYR MET VAL THR TYR GLY GLU PRO
SEQRES 8 S 237 VAL GLU VAL SER VAL PRO VAL HIS THR THR GLY ARG SER
SEQRES 9 S 237 GLN GLY GLU VAL GLN GLY GLY LEU VAL ASP ILE VAL VAL
SEQRES 10 S 237 HIS ASN LEU GLN ILE VAL ALA PRO GLY PRO ARG ARG ILE
SEQRES 11 S 237 PRO GLN GLU LEU VAL VAL ASP VAL THR LYS MET ASN ILE
SEQRES 12 S 237 GLY ASP HIS ILE THR ALA GLY ASP ILE LYS LEU PRO GLU
SEQRES 13 S 237 GLY CYS THR LEU ALA ALA ASP PRO GLU LEU THR VAL VAL
SEQRES 14 S 237 SER VAL LEU PRO PRO ARG LEU THR ALA GLU GLU LEU GLU
SEQRES 15 S 237 ALA GLU VAL GLN ALA ALA GLN VAL ALA GLY LEU VAL ALA
SEQRES 16 S 237 ALA GLY GLU LEU SER GLU GLU ALA ALA GLU ALA VAL LEU
SEQRES 17 S 237 GLU GLY ASP ALA SER LEU GLU GLU VAL LYS ALA GLU ALA
SEQRES 18 S 237 SER GLU ASP ASN ALA GLY THR ASP SER GLU ASP ASN SER
SEQRES 19 S 237 ASP ALA GLN
SEQRES 1 T 91 MET ALA HIS LYS LYS GLY VAL GLY SER SER LYS ASN GLY
SEQRES 2 T 91 ARG ASP SER ASN PRO LYS TYR LEU GLY VAL LYS LYS PHE
SEQRES 3 T 91 GLY GLY GLU VAL VAL LYS ALA GLY ASN ILE LEU VAL ARG
SEQRES 4 T 91 GLN ARG GLY THR LYS PHE LYS ALA GLY GLN GLY VAL GLY
SEQRES 5 T 91 MET GLY ARG ASP HIS THR LEU PHE ALA LEU SER ASP GLY
SEQRES 6 T 91 LYS VAL VAL PHE ILE ASN LYS GLY LYS GLY ALA ARG PHE
SEQRES 7 T 91 ILE SER ILE GLU ALA ALA GLN THR GLU VAL ALA ALA ASP
SEQRES 1 U 81 MET SER ARG GLU CYS TYR LEU THR GLY LYS LYS ASN LEU
SEQRES 2 U 81 VAL VAL ASN SER VAL ILE ARG ARG GLY LYS ALA ARG ALA
SEQRES 3 U 81 ASP GLY GLY VAL GLY ARG LYS THR THR GLY ILE THR LYS
SEQRES 4 U 81 ARG VAL GLN ARG ALA ASN LEU HIS LYS LYS ALA ILE ARG
SEQRES 5 U 81 GLU ASN GLY GLN VAL LYS THR VAL TRP LEU SER ALA ASN
SEQRES 6 U 81 ALA LEU ARG THR LEU SER LYS GLY PRO TYR LYS GLY ILE
SEQRES 7 U 81 GLU LEU ILE
SEQRES 1 V 67 MET LYS PRO SER GLU MET ARG ASN LEU GLN ALA THR ASP
SEQRES 2 V 67 PHE ALA LYS GLU ILE ASP ALA ARG LYS LYS GLU LEU MET
SEQRES 3 V 67 GLU LEU ARG PHE GLN ALA ALA ALA GLY GLN LEU ALA GLN
SEQRES 4 V 67 PRO HIS ARG VAL ARG GLN LEU ARG ARG GLU VAL ALA GLN
SEQRES 5 V 67 LEU ASN THR VAL LYS ALA GLU LEU ALA ARG LYS GLY GLU
SEQRES 6 V 67 GLN GLN
SEQRES 1 W 55 MET LYS ILE LYS LEU VAL ARG SER VAL ILE GLY ARG PRO
SEQRES 2 W 55 GLY ASN GLN VAL LYS THR VAL GLN ALA LEU GLY LEU ARG
SEQRES 3 W 55 LYS ILE GLY ASP SER ARG GLU VAL SER ASP THR PRO ALA
SEQRES 4 W 55 VAL ARG GLY MET VAL LYS THR VAL LYS HIS LEU LEU GLU
SEQRES 5 W 55 VAL GLN GLU
SEQRES 1 Z 60 MET ALA LYS HIS PRO VAL PRO LYS LYS LYS THR SER LYS
SEQRES 2 Z 60 SER LYS ARG ASP MET ARG ARG SER HIS HIS ALA LEU THR
SEQRES 3 Z 60 ALA PRO ASN LEU THR GLU CYS PRO GLN CYS HIS GLY LYS
SEQRES 4 Z 60 LYS LEU SER HIS HIS ILE CYS PRO ASN CYS GLY TYR TYR
SEQRES 5 Z 60 ASP GLY ARG GLN VAL LEU ALA VAL
SEQRES 1 1 55 MET ALA LYS ASP GLY PRO ARG ILE ILE VAL LYS MET GLU
SEQRES 2 1 55 SER SER ALA GLY THR GLY PHE TYR TYR THR THR THR LYS
SEQRES 3 1 55 ASN ARG ARG ASN THR GLN ALA LYS LEU GLU LEU LYS LYS
SEQRES 4 1 55 TYR ASP PRO VAL ALA LYS LYS HIS VAL VAL PHE ARG GLU
SEQRES 5 1 55 LYS LYS VAL
SEQRES 1 2 47 MET LYS ARG THR TYR GLN PRO ASN ASN ARG LYS ARG ALA
SEQRES 2 2 47 LYS THR HIS GLY PHE ARG ALA ARG MET LYS THR LYS SER
SEQRES 3 2 47 GLY ARG ASN ILE LEU ALA ARG ARG ARG ALA LYS GLY ARG
SEQRES 4 2 47 HIS GLN LEU THR VAL SER ASP GLU
SEQRES 1 3 66 MET PRO LYS MET LYS THR HIS LYS MET ALA LYS ARG ARG
SEQRES 2 3 66 ILE LYS ILE THR GLY THR GLY LYS VAL MET ALA PHE LYS
SEQRES 3 3 66 SER GLY LYS ARG HIS GLN ASN THR GLY LYS SER GLY ASP
SEQRES 4 3 66 GLU ILE ARG GLY LYS GLY LYS GLY PHE VAL LEU ALA LYS
SEQRES 5 3 66 ALA GLU TRP ALA ARG MET LYS LEU MET LEU PRO ARG GLY
SEQRES 6 3 66 LYS
SEQRES 1 4 37 MET LYS VAL ARG SER SER VAL LYS LYS MET CYS ASP ASN
SEQRES 2 4 37 CYS LYS VAL VAL ARG ARG HIS GLY ARG VAL LEU VAL ILE
SEQRES 3 4 37 CYS SER ASN VAL LYS HIS LYS GLN ARG GLN GLY
HET LC2 X2881 33
HET LMA X2882 58
HET MG X2883 1
HET MG X2884 1
HET MG X2885 1
HET MG X2886 1
HET MG X2887 1
HET MG X2888 1
HET MG X2889 1
HET MG X2890 1
HET MG X2891 1
HET MG X2892 1
HET MG X2893 1
HET MG X2894 1
HET MG X2895 1
HET MG X2896 1
HET MG X2897 1
HET MG X2898 1
HET MG X2899 1
HET MG X2900 1
HET MG X2901 1
HET MG X2902 1
HET MG X2903 1
HET MG X2904 1
HET MG X2905 1
HET MG X2906 1
HET MG X2907 1
HET MG X2908 1
HET MG X2909 1
HET MG X2910 1
HET MG X2911 1
HET MG X2912 1
HET MG X2913 1
HET MG X2914 1
HET MG X2915 1
HET MG X2916 1
HET MG X2917 1
HET MG X2918 1
HET MG X2919 1
HET MG X2920 1
HET MG X2921 1
HET MG X2922 1
HET MG X2923 1
HET MG X2924 1
HET MG X2925 1
HET MG X2926 1
HET MG X2927 1
HET MG X2928 1
HET MG X2929 1
HET MG X2930 1
HET MG X2931 1
HET MG X2932 1
HET MG X2933 1
HET MG X2934 1
HET MG X2935 1
HET MG X2936 1
HET MG X2937 1
HET MG X2938 1
HET MG X2939 1
HET MG X2940 1
HET MG X2941 1
HET MG X2942 1
HET MG X2943 1
HET MG X2944 1
HET MG X2945 1
HET MG X2946 1
HET MG X2947 1
HET MG X2948 1
HET MG X2949 1
HET MG X2950 1
HET MG X2951 1
HET MG X2952 1
HET MG X2953 1
HET K X2954 1
HET K X2955 1
HET K X2956 1
HET K X2957 1
HET NA X2958 1
HET NA X2959 1
HET NA X2960 1
HET NA X2961 1
HET NA X2962 1
HET MG I 157 1
HET MG U 82 1
HETNAM LC2 N-[(1S,2R,3E,5E,7S,9E,11E,13S,15R,19R)-7,13-DIHYDROXY-
HETNAM 2 LC2 1,4,10,19-TETRAMETHYL-17,18-DIOXO-16-
HETNAM 3 LC2 OXABICYCLO[13.2.2]NONADECA-3,5,9,11-TETRAEN-2-YL]-2-
HETNAM 4 LC2 OXOPROPANAMIDE
HETNAM LMA LANKAMYCIN
HETNAM MG MAGNESIUM ION
HETNAM K POTASSIUM ION
HETNAM NA SODIUM ION
HETSYN LC2 LANKACIDIN C
HETSYN LMA [(2S,3R,4R,6R)-6-[[(1S,2R,3S,4S,6S,8R,9S,10S,11R,14R)-
HETSYN 2 LMA 9-ACETYLOXY-6-HYDROXY-11-[(2R,3R)-3-HYDROXYBUTAN-2-
HETSYN 3 LMA YL]-3-[(2S,3R, 4S,6R)-4-METHOXY-3,6-DIMETHYL-OXAN-2-
HETSYN 4 LMA YL]OXY-2,4,6,8,10,14-HEXAMETHYL-7,13-DIOXO-12-
HETSYN 5 LMA OXACYCLOTETRADEC-1-YL]OXY]-4-METHOXY- 2,4-DIMETHYL-
HETSYN 6 LMA OXAN-3-YL] ETHANOATE
FORMUL 31 LC2 C25 H33 N O7
FORMUL 32 LMA C43 H74 O15
FORMUL 33 MG 73(MG 2+)
FORMUL 04 K 4(K 1+)
FORMUL 08 NA 5(NA 1+)
HELIX 1 1 ARG A 135 VAL A 137 5 3
HELIX 2 2 ARG A 262 SER A 267 1 6
HELIX 3 3 ASN B 60 LYS B 69 1 10
HELIX 4 4 VAL B 91 PHE B 96 1 6
HELIX 5 5 GLY B 115 TRP B 120 1 6
HELIX 6 6 ASN C 23 ARG C 39 1 17
HELIX 7 7 PRO C 96 GLU C 113 1 18
HELIX 8 8 GLY C 122 ALA C 126 5 5
HELIX 9 9 THR C 130 GLN C 139 1 10
HELIX 10 10 ASP C 154 ALA C 160 1 7
HELIX 11 11 ASN C 176 HIS C 183 1 8
HELIX 12 12 LYS D 5 GLN D 11 1 7
HELIX 13 13 VAL D 12 MET D 17 1 6
HELIX 14 14 GLY D 41 GLU D 45 5 5
HELIX 15 15 LYS D 48 THR D 61 1 14
HELIX 16 16 GLY D 93 ILE D 106 1 14
HELIX 17 17 THR D 142 VAL D 146 5 5
HELIX 18 18 THR D 162 LEU D 175 1 14
HELIX 19 19 HIS E 61 ASP E 81 1 21
HELIX 20 20 ASP E 137 VAL E 151 1 15
HELIX 21 21 MET F 74 ALA F 82 1 9
HELIX 22 22 TRP F 101 LYS F 111 1 11
HELIX 23 23 VAL F 120 SER F 133 1 14
HELIX 24 24 PRO G 50 LYS G 65 1 16
HELIX 25 25 PRO G 123 PHE G 132 1 10
HELIX 26 26 GLY G 133 LEU G 135 5 3
HELIX 27 27 GLY G 138 THR G 146 1 9
HELIX 28 28 HIS G 156 GLN G 161 5 6
HELIX 29 29 ARG H 116 ARG H 121 1 6
HELIX 30 30 PHE H 123 LEU H 129 1 7
HELIX 31 31 LEU I 77 GLN I 81 1 5
HELIX 32 32 THR I 92 LEU I 98 5 7
HELIX 33 33 SER I 126 GLU I 134 1 9
HELIX 34 34 SER J 45 PHE J 59 1 15
HELIX 35 35 GLU J 112 LYS J 125 1 14
HELIX 36 36 ASN K 13 GLY K 32 1 20
HELIX 37 37 LEU K 38 LYS K 56 1 19
HELIX 38 38 ASP K 59 ALA K 67 1 9
HELIX 39 39 ASP K 72 GLU K 82 1 11
HELIX 40 40 GLU K 82 TYR K 87 1 6
HELIX 41 41 ARG L 9 ARG L 14 1 6
HELIX 42 42 THR L 65 ALA L 68 5 4
HELIX 43 43 ALA L 69 ALA L 80 1 12
HELIX 44 44 VAL L 100 GLY L 110 1 11
HELIX 45 45 ASN M 8 ILE M 16 1 9
HELIX 46 46 GLU M 17 THR M 21 5 5
HELIX 47 47 VAL N 9 LYS N 19 1 11
HELIX 48 48 TRP N 25 SER N 29 5 5
HELIX 49 49 GLN N 31 LEU N 71 1 41
HELIX 50 50 ASN N 75 ARG N 85 1 11
HELIX 51 51 VAL N 94 GLU N 102 1 9
HELIX 52 52 GLU N 102 ALA N 116 1 15
HELIX 53 53 GLU O 49 TYR O 54 5 6
HELIX 54 54 GLN P 13 GLN P 17 5 5
HELIX 55 55 SER P 34 ARG P 46 1 13
HELIX 56 56 SER P 49 LEU P 57 1 9
HELIX 57 57 ALA P 64 ASN P 82 1 19
HELIX 58 58 LEU P 86 ASP P 88 5 3
HELIX 59 59 SER Q 13 ALA Q 19 1 7
HELIX 60 60 MET Q 20 ARG Q 22 5 3
HELIX 61 61 THR Q 36 GLY Q 47 1 12
HELIX 62 62 THR S 9 LYS S 13 5 5
HELIX 63 63 ARG S 36 SER S 47 1 12
HELIX 64 64 THR S 148 ILE S 152 5 5
HELIX 65 65 SER U 63 GLY U 73 1 11
HELIX 66 66 GLN V 10 GLY V 35 1 26
HELIX 67 67 GLN V 39 LEU V 60 1 22
HELIX 68 68 PRO W 13 LEU W 23 1 11
HELIX 69 69 THR W 37 VAL W 47 1 11
HELIX 70 70 SER Z 12 ARG Z 20 1 9
HELIX 71 71 SER Z 21 HIS Z 23 5 3
HELIX 72 72 ASN 2 8 LYS 2 14 1 7
HELIX 73 73 PHE 2 18 MET 2 22 5 5
HELIX 74 74 THR 2 24 ARG 2 35 1 12
HELIX 75 75 LEU 2 42 ASP 2 46 5 5
HELIX 76 76 THR 3 6 LYS 3 11 1 6
HELIX 77 77 ALA 3 53 MET 3 58 1 6
HELIX 78 78 ASN 4 29 LYS 4 33 5 5
SHEET 1 A 3 ALA A 78 ASP A 86 0
SHEET 2 A 3 ALA A 91 TYR A 98 -1 O LEU A 95 N ALA A 82
SHEET 3 A 3 LYS A 103 LEU A 107 -1 O ILE A 106 N ALA A 94
SHEET 1 B 3 ALA A 131 PRO A 133 0
SHEET 2 B 3 TYR A 191 ILE A 194 -1 O ALA A 192 N LEU A 132
SHEET 3 B 3 VAL A 143 HIS A 144 -1 N HIS A 144 O THR A 193
SHEET 1 C 4 VAL A 166 LYS A 169 0
SHEET 2 C 4 TYR A 173 LEU A 178 -1 O ILE A 175 N GLN A 167
SHEET 3 C 4 GLU A 182 HIS A 187 -1 O GLU A 182 N LEU A 178
SHEET 4 C 4 ASP A 268 ARG A 269 -1 O ARG A 269 N LEU A 183
SHEET 1 D 7 GLY B 3 THR B 12 0
SHEET 2 D 7 VAL B 23 LEU B 27 -1 O VAL B 25 N GLY B 10
SHEET 3 D 7 LEU B 181 LYS B 185 -1 O ILE B 182 N VAL B 26
SHEET 4 D 7 ARG B 164 ARG B 176 -1 N GLU B 171 O LYS B 185
SHEET 5 D 7 LYS B 101 THR B 107 -1 N ILE B 102 O LEU B 170
SHEET 6 D 7 LEU B 195 SER B 200 -1 O ARG B 199 N ASP B 103
SHEET 7 D 7 GLY B 3 THR B 12 -1 N GLY B 6 O VAL B 196
SHEET 1 E 2 TRP B 15 LYS B 16 0
SHEET 2 E 2 ARG B 19 ALA B 20 -1 O ARG B 19 N LYS B 16
SHEET 1 F 4 LEU B 78 ARG B 82 0
SHEET 2 F 4 ALA B 46 GLY B 50 -1 N ILE B 49 O ARG B 79
SHEET 3 F 4 CYS B 31 GLN B 35 -1 N GLN B 35 O GLN B 48
SHEET 4 F 4 ASP B 89 SER B 90 -1 O SER B 90 N CYS B 31
SHEET 1 G 2 GLY B 110 THR B 113 0
SHEET 2 G 2 HIS B 159 GLY B 161 -1 O MET B 160 N GLY B 112
SHEET 1 H 3 LYS C 116 LEU C 117 0
SHEET 2 H 3 ARG C 185 VAL C 187 1 O LEU C 186 N LEU C 117
SHEET 3 H 3 VAL C 148 LEU C 150 1 N LEU C 149 O VAL C 187
SHEET 1 I 4 GLY D 86 LEU D 91 0
SHEET 2 I 4 ILE D 31 GLY D 39 -1 N ILE D 34 O LEU D 91
SHEET 3 I 4 MET D 152 THR D 158 -1 O THR D 155 N VAL D 35
SHEET 4 I 4 TYR D 128 ASN D 129 -1 N TYR D 128 O ILE D 156
SHEET 1 J 3 THR E 16 GLN E 20 0
SHEET 2 J 3 VAL E 23 LYS E 27 -1 O LYS E 25 N ASN E 18
SHEET 3 J 3 LEU E 33 THR E 34 -1 O LEU E 33 N VAL E 26
SHEET 1 K 2 VAL E 43 ARG E 44 0
SHEET 2 K 2 LEU E 51 VAL E 52 -1 O LEU E 51 N ARG E 44
SHEET 1 L 4 VAL E 121 GLU E 127 0
SHEET 2 L 4 ARG E 130 GLY E 135 -1 O SER E 134 N THR E 122
SHEET 3 L 4 TYR E 83 LEU E 89 -1 N ILE E 85 O VAL E 133
SHEET 4 L 4 VAL E 162 PHE E 164 -1 O ARG E 163 N GLU E 88
SHEET 1 M 3 ARG E 95 THR E 99 0
SHEET 2 M 3 ALA E 102 ASN E 106 -1 O ALA E 102 N THR E 99
SHEET 3 M 3 ILE E 114 ILE E 115 -1 O ILE E 115 N LEU E 103
SHEET 1 N 4 LEU G 148 VAL G 150 0
SHEET 2 N 4 PHE G 79 ILE G 83 1 N VAL G 80 O LYS G 149
SHEET 3 N 4 TRP G 41 ASP G 45 1 N VAL G 42 O PHE G 79
SHEET 4 N 4 LEU G 166 LYS G 167 1 O LEU G 166 N TRP G 41
SHEET 1 O 2 VAL G 99 ARG G 102 0
SHEET 2 O 2 THR G 112 ALA G 115 -1 O THR G 114 N TYR G 100
SHEET 1 P 6 LEU H 8 VAL H 10 0
SHEET 2 P 6 ALA H 16 CYS H 21 -1 O ILE H 19 N LEU H 8
SHEET 3 P 6 ILE H 50 ALA H 58 -1 O SER H 54 N MET H 20
SHEET 4 P 6 VAL H 69 ARG H 76 -1 O ALA H 72 N ILE H 51
SHEET 5 P 6 ALA H 95 ILE H 98 -1 O ALA H 95 N VAL H 75
SHEET 6 P 6 LEU H 8 VAL H 10 1 N ASP H 9 O ALA H 96
SHEET 1 Q 7 ILE H 81 LYS H 82 0
SHEET 2 Q 7 THR H 88 PHE H 91 -1 O ILE H 89 N ILE H 81
SHEET 3 Q 7 GLU M 75 PRO M 82 -1 O GLU M 78 N ARG H 90
SHEET 4 Q 7 SER M 65 SER M 72 -1 N PHE M 66 O PHE M 81
SHEET 5 Q 7 ARG M 44 ALA M 56 -1 N ILE M 55 O THR M 67
SHEET 6 Q 7 ASP M 31 GLU M 41 -1 N ASP M 36 O GLN M 48
SHEET 7 Q 7 VAL M 91 THR M 92 -1 O THR M 92 N VAL M 33
SHEET 1 R 3 GLU I 73 LYS I 76 0
SHEET 2 R 3 VAL I 106 LEU I 109 1 O LYS I 107 N GLU I 73
SHEET 3 R 3 ALA I 124 ALA I 125 1 O ALA I 124 N VAL I 106
SHEET 1 S 4 ILE J 65 ILE J 67 0
SHEET 2 S 4 VAL J 103 VAL J 107 -1 O GLU J 106 N TYR J 66
SHEET 3 S 4 TYR J 33 ALA J 37 -1 N LEU J 35 O PHE J 105
SHEET 4 S 4 THR J 130 VAL J 133 -1 O LYS J 131 N ILE J 36
SHEET 1 T 3 ALA J 41 LYS J 44 0
SHEET 2 T 3 TYR J 93 VAL J 98 -1 O SER J 96 N ILE J 43
SHEET 3 T 3 PRO J 74 VAL J 75 -1 N VAL J 75 O TYR J 93
SHEET 1 U 3 ARG K 33 THR K 37 0
SHEET 2 U 3 MET K 110 GLU K 114 -1 O ALA K 111 N THR K 36
SHEET 3 U 3 ARG K 96 ARG K 99 -1 N LEU K 98 O LEU K 112
SHEET 1 V 3 ILE L 42 ILE L 43 0
SHEET 2 V 3 ARG L 28 SER L 30 -1 N ARG L 28 O ILE L 43
SHEET 3 V 3 VAL L 88 ASP L 90 1 O ASP L 90 N LEU L 29
SHEET 1 W 4 GLY O 17 ILE O 20 0
SHEET 2 W 4 THR O 91 ILE O 95 -1 O THR O 91 N ILE O 20
SHEET 3 W 4 VAL O 56 GLU O 62 -1 N GLU O 59 O LYS O 94
SHEET 4 W 4 ASP O 31 GLU O 34 -1 N LYS O 32 O ALA O 58
SHEET 1 X 2 PHE O 39 VAL O 40 0
SHEET 2 X 2 THR O 45 VAL O 46 -1 O VAL O 46 N PHE O 39
SHEET 1 Y 2 ILE O 71 LYS O 73 0
SHEET 2 Y 2 ARG O 82 THR O 84 -1 O THR O 84 N ILE O 71
SHEET 1 Z 3 PHE P 25 VAL P 31 0
SHEET 2 Z 3 SER P 122 GLU P 130 -1 O ILE P 126 N ALA P 26
SHEET 3 Z 3 LEU P 90 ALA P 99 -1 N TYR P 96 O THR P 125
SHEET 1 AA 2 LEU P 103 ALA P 110 0
SHEET 2 AA 2 SER P 113 LYS P 119 -1 O ILE P 117 N ARG P 105
SHEET 1 AB 4 LEU Q 7 PRO Q 10 0
SHEET 2 AB 4 VAL Q 24 VAL Q 29 -1 O TRP Q 28 N ALA Q 9
SHEET 3 AB 4 ARG Q 75 LEU Q 82 -1 O LYS Q 76 N VAL Q 29
SHEET 4 AB 4 VAL Q 50 VAL Q 58 -1 N VAL Q 58 O ARG Q 75
SHEET 1 AC 5 GLU R 70 LEU R 76 0
SHEET 2 AC 5 LYS R 45 THR R 55 -1 N VAL R 53 O ARG R 72
SHEET 3 AC 5 GLY R 34 LEU R 40 -1 N LEU R 38 O VAL R 47
SHEET 4 AC 5 THR R 21 ILE R 23 -1 N VAL R 22 O GLY R 34
SHEET 5 AC 5 VAL R 81 ALA R 82 -1 O VAL R 81 N ILE R 23
SHEET 1 AD 5 SER S 31 ASP S 35 0
SHEET 2 AD 5 MET S 18 TYR S 24 -1 N ILE S 19 O LEU S 34
SHEET 3 AD 5 PRO S 78 MET S 85 1 O PHE S 83 N VAL S 22
SHEET 4 AD 5 GLU S 60 MET S 71 -1 N LYS S 67 O ASP S 82
SHEET 5 AD 5 PHE S 52 VAL S 56 -1 N ILE S 54 O PHE S 62
SHEET 1 AE 3 SER S 95 PRO S 97 0
SHEET 2 AE 3 ASN S 119 VAL S 123 -1 O LEU S 120 N VAL S 96
SHEET 3 AE 3 THR S 159 LEU S 160 -1 O THR S 159 N VAL S 123
SHEET 1 AF 3 LEU S 112 ILE S 115 0
SHEET 2 AF 3 VAL S 169 LEU S 172 -1 O SER S 170 N ASP S 114
SHEET 3 AF 3 HIS S 146 ILE S 147 -1 N ILE S 147 O VAL S 169
SHEET 1 AG 2 GLY T 22 VAL T 23 0
SHEET 2 AG 2 VAL T 38 ARG T 39 -1 O ARG T 39 N GLY T 22
SHEET 1 AH 4 VAL T 30 VAL T 31 0
SHEET 2 AH 4 GLY T 65 ASN T 71 -1 O GLY T 65 N VAL T 31
SHEET 3 AH 4 ARG T 77 GLU T 82 -1 O PHE T 78 N ILE T 70
SHEET 4 AH 4 PHE T 45 ALA T 47 1 N LYS T 46 O ARG T 77
SHEET 1 AI 2 VAL T 51 MET T 53 0
SHEET 2 AI 2 LEU T 59 ALA T 61 -1 O PHE T 60 N GLY T 52
SHEET 1 AJ 2 ILE U 19 ARG U 20 0
SHEET 2 AJ 2 VAL U 41 GLN U 42 -1 O VAL U 41 N ARG U 20
SHEET 1 AK 2 LYS U 23 ALA U 24 0
SHEET 2 AK 2 GLY U 36 ILE U 37 -1 O GLY U 36 N ALA U 24
SHEET 1 AL 2 LYS W 2 LYS W 4 0
SHEET 2 AL 2 SER W 31 GLU W 33 -1 O ARG W 32 N ILE W 3
SHEET 1 AM 2 LEU Z 30 GLU Z 32 0
SHEET 2 AM 2 LYS Z 39 LEU Z 41 -1 O LYS Z 40 N THR Z 31
SHEET 1 AN 2 LYS 1 11 MET 1 12 0
SHEET 2 AN 2 THR 1 25 LYS 1 26 -1 O THR 1 25 N MET 1 12
SHEET 1 AO 2 LEU 1 37 LYS 1 38 0
SHEET 2 AO 2 PHE 1 50 ARG 1 51 -1 O PHE 1 50 N LYS 1 38
SHEET 1 AP 2 LYS 4 15 ARG 4 18 0
SHEET 2 AP 2 VAL 4 23 ILE 4 26 -1 O ILE 4 26 N LYS 4 15
SSBOND 1 CYS Z 36 CYS Z 49 1555 1555 2.04
LINK OP1 C X 226 MG MG X2918 1555 1555 2.45
LINK OP2 G X 572 MG MG X2916 1555 1555 2.24
LINK O6 G X 579 MG MG X2900 1555 1555 2.88
LINK OP2 C X 583 MG MG X2934 1555 1555 2.31
LINK OP1 C X 583 MG MG X2938 1555 1555 2.39
LINK OP2 A X 743 MG MG X2897 1555 1555 2.99
LINK OP1 G X 754 MG MG X2932 1555 1555 2.81
LINK O3' G X 761 MG MG X2927 1555 1555 2.94
LINK OP1 A X 762 MG MG X2927 1555 1555 2.36
LINK OP1 G X 776 MG MG X2897 1555 1555 2.11
LINK OP2 A X 796 MG MG X2919 1555 1555 2.98
LINK OP1 U X 800 MG MG X2937 1555 1555 2.14
LINK OP2 C X 803 MG MG X2937 1555 1555 2.99
LINK OP1 A X 813 NA NA X2961 1555 1555 2.05
LINK OP1 A X 815 MG MG X2948 1555 1555 2.29
LINK O4 U X 823 MG MG X2926 1555 1555 2.48
LINK OP2 A X 956 MG MG X2909 1555 1555 2.70
LINK O5' A X 956 MG MG X2909 1555 1555 2.83
LINK OP2 G X 957 MG MG X2909 1555 1555 2.57
LINK OP2 A X 984 MG MG X2890 1555 1555 2.61
LINK OP1 A X1001 MG MG X2923 1555 1555 2.70
LINK OP2 G X1201 MG MG X2920 1555 1555 2.92
LINK O6 G X1245 K K X2955 1555 1555 3.25
LINK OP1 A X1281 MG MG X2887 1555 1555 2.74
LINK OP2 A X1282 MG MG X2888 1555 1555 1.95
LINK OP1 G X1284 MG MG X2884 1555 1555 2.66
LINK OP2 C X1340 MG MG X2898 1555 1555 1.80
LINK OP1 U X1365 MG MG X2889 1555 1555 2.81
LINK OP1 G X1465 MG MG X2924 1555 1555 2.07
LINK OP2 C X1653 MG MG X2943 1555 1555 2.38
LINK OP2 A X1681 MG MG X2950 1555 1555 2.29
LINK OP2 A X1682 MG MG X2935 1555 1555 2.29
LINK OP1 C X1687 MG MG X2947 1555 1555 2.49
LINK OP2 U X1688 MG MG X2947 1555 1555 2.21
LINK OP2 A X1693 MG MG X2907 1555 1555 2.21
LINK OP2 G X1767 MG MG X2906 1555 1555 2.72
LINK OP1 C X1773 MG MG X2930 1555 1555 1.74
LINK OP2 A X1774 MG MG X2930 1555 1555 2.75
LINK O4 U X1934 MG MG X2902 1555 1555 2.97
LINK OP2 C X1973 MG MG X2893 1555 1555 2.70
LINK O5' U X1976 NA NA X2960 1555 1555 3.13
LINK O6 G X1985 NA NA X2959 1555 1555 3.15
LINK OP1 A X1988 MG MG X2888 1555 1555 2.42
LINK OP1 C X1989 MG MG X2887 1555 1555 2.52
LINK OP1 U X1999 MG MG X2922 1555 1555 2.97
LINK O6 G X2015 K K X2954 1555 1555 3.20
LINK OP1 G X2018 MG MG X2908 1555 1555 2.10
LINK OP1 A X2031 MG MG X2887 1555 1555 2.62
LINK OP2 G X2039 MG MG X2899 1555 1555 2.39
LINK OP2 A X2040 MG MG X2899 1555 1555 2.58
LINK OP1 A X2041 MG MG X2922 1555 1555 2.84
LINK OP1 A X2045 MG MG X2894 1555 1555 2.73
LINK OP1 U X2057 MG MG X2940 1555 1555 2.21
LINK OP2 A X2246 MG MG X2911 1555 1555 2.92
LINK OP1 A X2248 MG MG X2911 1555 1555 2.98
LINK O3' G X2426 MG MG X2900 1555 1555 2.93
LINK OP2 G X2426 MG MG X2929 1555 1555 2.96
LINK OP2 G X2481 MG MG X2928 1555 1555 2.36
LINK OP1 C X2486 MG MG X2951 1555 1555 2.97
LINK OP2 A X2497 MG MG X2913 1555 1555 2.37
LINK OP2 A X2512 MG MG X2917 1555 1555 2.95
LINK OP1 C X2552 MG MG X2951 1555 1555 2.76
LINK OP2 C X2554 MG MG X2951 1555 1555 2.20
LINK OP1 A X2556 MG MG X2885 1555 1555 2.26
LINK OP2 G X2561 MG MG X2933 1555 1555 1.98
LINK OP2 G X2562 MG MG X2933 1555 1555 1.75
LINK OP1 A X2568 MG MG X2919 1555 1555 2.67
LINK O4 U X2572 MG MG X2921 1555 1555 2.72
LINK OP2 G X2657 MG MG X2946 1555 1555 2.03
LINK OP1 A X2690 MG MG X2891 1555 1555 2.64
LINK OP1 A X2692 MG MG X2891 1555 1555 2.15
LINK OP2 A X2692 MG MG X2892 1555 1555 2.19
LINK OP2 G X2694 MG MG X2892 1555 1555 2.13
LINK O3' A X2705 MG MG X2945 1555 1555 2.76
LINK O2' A X2705 MG MG X2945 1555 1555 2.77
LINK MG MG X2912 O GLN P 16 1555 1555 2.92
LINK OG SER I 54 MG MG I 157 1555 1555 2.30
CISPEP 1 LEU C 19 PRO C 20 0 2.76
SITE 1 AC1 8 G X2044 A X2430 C X2431 U X2483
SITE 2 AC1 8 G X2484 U X2485 U X2564 LMA X2882
SITE 1 AC2 12 ARG P 111 C X 759 U X 760 A X2041
SITE 2 AC2 12 A X2042 A X2045 A X2482 G X2484
SITE 3 AC2 12 U X2588 C X2589 U X2590 LC2 X2881
SITE 1 AC3 1 A X1667
SITE 1 AC4 1 G X1284
SITE 1 AC5 3 C X2554 G X2555 A X2556
SITE 1 AC6 3 A X1281 C X1989 A X2031
SITE 1 AC7 2 A X1282 A X1988
SITE 1 AC8 1 U X1365
SITE 1 AC9 3 G X 579 G X 983 A X 984
SITE 1 BC1 4 C X1310 C X2689 A X2690 A X2692
SITE 1 BC2 4 A X2690 A X2692 U X2693 G X2694
SITE 1 BC3 1 C X1973
SITE 1 BC4 1 A X2045
SITE 1 BC5 1 G X2698
SITE 1 BC6 1 G X2699
SITE 1 BC7 6 G X 742 A X 743 C X 744 A X 774
SITE 2 BC7 6 U X 775 G X 776
SITE 1 BC8 1 C X1340
SITE 1 BC9 2 G X2039 A X2040
SITE 1 CC1 4 G X 579 G X2426 A X2427 C X2478
SITE 1 CC2 1 A X1980
SITE 1 CC3 1 U X1934
SITE 1 CC4 2 A X 587 U X2000
SITE 1 CC5 1 G X 758
SITE 1 CC6 1 C X2431
SITE 1 CC7 2 G X1767 A X1964
SITE 1 CC8 1 A X1693
SITE 1 CC9 5 G X2007 C X2008 G X2018 G X2020
SITE 2 CC9 5 G X2021
SITE 1 DC1 3 G X 955 A X 956 G X 957
SITE 1 DC2 4 A X2246 A X2247 A X2248 U X2249
SITE 1 DC3 1 THR U 8
SITE 1 DC4 2 GLN P 16 A X 512
SITE 1 DC5 2 A X2497 A X2520
SITE 1 DC6 1 G X1754
SITE 1 DC7 1 G X 572
SITE 1 DC8 2 A X2512 A X2513
SITE 1 DC9 1 C X 226
SITE 1 EC1 4 ALA A 226 A X 796 A X 797 A X2568
SITE 1 EC2 2 C X 829 G X1201
SITE 1 EC3 1 U X2572
SITE 1 EC4 4 ASN C 66 U X1999 U X2000 A X2041
SITE 1 EC5 4 G X1000 A X1001 G X1168 C X1169
SITE 1 EC6 2 G X1465 G X2634
SITE 1 EC7 1 G X1371
SITE 1 EC8 2 A X 576 U X 823
SITE 1 EC9 2 G X 761 A X 762
SITE 1 FC1 3 A X2043 G X2425 G X2481
SITE 1 FC2 1 G X2426
SITE 1 FC3 3 A X1771 C X1773 A X1774
SITE 1 FC4 2 G X 752 U X1769
SITE 1 FC5 1 G X 754
SITE 1 FC6 2 G X2561 G X2562
SITE 1 FC7 2 C X 583 U X 585
SITE 1 FC8 2 A X1681 A X1682
SITE 1 FC9 4 U X 800 A X 801 A X 802 C X 803
SITE 1 GC1 1 C X 583
SITE 1 GC2 2 G X 798 G X 805
SITE 1 GC3 4 PRO A 229 PRO A 233 U X2057 G X2218
SITE 1 GC4 1 G X1983
SITE 1 GC5 1 G X 713
SITE 1 GC6 1 C X1653
SITE 1 GC7 2 A X1751 C X2691
SITE 1 GC8 2 A X2705 U X2706
SITE 1 GC9 1 G X2657
SITE 1 HC1 2 C X1687 U X1688
SITE 1 HC2 3 G X 687 A X 815 A X 817
SITE 1 HC3 1 C X 185
SITE 1 HC4 4 A X1681 A X1682 G X1683 G X1975
SITE 1 HC5 5 C X2486 A X2551 C X2552 G X2553
SITE 2 HC5 5 C X2554
SITE 1 HC6 1 SER I 54
SITE 1 HC7 2 G X2015 A X2432
SITE 1 HC8 1 G X1245
SITE 1 HC9 1 A X2220
SITE 1 IC1 2 G X1985 G X1986
SITE 1 IC2 3 A X1693 A X1694 U X1976
SITE 1 IC3 1 A X 813
CRYST1 169.723 408.562 693.334 90.00 90.00 90.00 I 2 2 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 0.005892 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002448 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001442 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
