HEADER RIBOSOME 08-SEP-15 5DM6
TITLE CRYSTAL STRUCTURE OF THE 50S RIBOSOMAL SUBUNIT FROM DEINOCOCCUS
TITLE 2 RADIODURANS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 50S RIBOSOMAL PROTEIN L1;
COMPND 3 CHAIN: 0;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: 50S RIBOSOMAL PROTEIN L2;
COMPND 6 CHAIN: A;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: 50S RIBOSOMAL PROTEIN L3;
COMPND 9 CHAIN: B;
COMPND 10 MOL_ID: 4;
COMPND 11 MOLECULE: 50S RIBOSOMAL PROTEIN L4;
COMPND 12 CHAIN: C;
COMPND 13 MOL_ID: 5;
COMPND 14 MOLECULE: 50S RIBOSOMAL PROTEIN L5;
COMPND 15 CHAIN: D;
COMPND 16 MOL_ID: 6;
COMPND 17 MOLECULE: 50S RIBOSOMAL PROTEIN L6;
COMPND 18 CHAIN: E;
COMPND 19 MOL_ID: 7;
COMPND 20 MOLECULE: 50S RIBOSOMAL PROTEIN L11;
COMPND 21 CHAIN: F;
COMPND 22 MOL_ID: 8;
COMPND 23 MOLECULE: 50S RIBOSOMAL PROTEIN L13;
COMPND 24 CHAIN: G;
COMPND 25 MOL_ID: 9;
COMPND 26 MOLECULE: 50S RIBOSOMAL PROTEIN L14;
COMPND 27 CHAIN: H;
COMPND 28 MOL_ID: 10;
COMPND 29 MOLECULE: 50S RIBOSOMAL PROTEIN L15;
COMPND 30 CHAIN: I;
COMPND 31 MOL_ID: 11;
COMPND 32 MOLECULE: 50S RIBOSOMAL PROTEIN L16;
COMPND 33 CHAIN: J;
COMPND 34 MOL_ID: 12;
COMPND 35 MOLECULE: 50S RIBOSOMAL PROTEIN L17;
COMPND 36 CHAIN: K;
COMPND 37 MOL_ID: 13;
COMPND 38 MOLECULE: 50S RIBOSOMAL PROTEIN L18;
COMPND 39 CHAIN: L;
COMPND 40 MOL_ID: 14;
COMPND 41 MOLECULE: 50S RIBOSOMAL PROTEIN L19;
COMPND 42 CHAIN: M;
COMPND 43 MOL_ID: 15;
COMPND 44 MOLECULE: 50S RIBOSOMAL PROTEIN L20;
COMPND 45 CHAIN: N;
COMPND 46 MOL_ID: 16;
COMPND 47 MOLECULE: 50S RIBOSOMAL PROTEIN L21;
COMPND 48 CHAIN: O;
COMPND 49 MOL_ID: 17;
COMPND 50 MOLECULE: 50S RIBOSOMAL PROTEIN L22;
COMPND 51 CHAIN: P;
COMPND 52 MOL_ID: 18;
COMPND 53 MOLECULE: 50S RIBOSOMAL PROTEIN L23;
COMPND 54 CHAIN: Q;
COMPND 55 MOL_ID: 19;
COMPND 56 MOLECULE: 50S RIBOSOMAL PROTEIN L24;
COMPND 57 CHAIN: R;
COMPND 58 MOL_ID: 20;
COMPND 59 MOLECULE: 50S RIBOSOMAL PROTEIN L25;
COMPND 60 CHAIN: S;
COMPND 61 SYNONYM: GENERAL STRESS PROTEIN CTC;
COMPND 62 MOL_ID: 21;
COMPND 63 MOLECULE: 50S RIBOSOMAL PROTEIN L27;
COMPND 64 CHAIN: T;
COMPND 65 MOL_ID: 22;
COMPND 66 MOLECULE: 50S RIBOSOMAL PROTEIN L28;
COMPND 67 CHAIN: U;
COMPND 68 MOL_ID: 23;
COMPND 69 MOLECULE: 50S RIBOSOMAL PROTEIN L29;
COMPND 70 CHAIN: V;
COMPND 71 MOL_ID: 24;
COMPND 72 MOLECULE: 50S RIBOSOMAL PROTEIN L30;
COMPND 73 CHAIN: W;
COMPND 74 MOL_ID: 25;
COMPND 75 MOLECULE: 50S RIBOSOMAL PROTEIN L32;
COMPND 76 CHAIN: Z;
COMPND 77 MOL_ID: 26;
COMPND 78 MOLECULE: 50S RIBOSOMAL PROTEIN L33;
COMPND 79 CHAIN: 1;
COMPND 80 MOL_ID: 27;
COMPND 81 MOLECULE: 50S RIBOSOMAL PROTEIN L34;
COMPND 82 CHAIN: 2;
COMPND 83 MOL_ID: 28;
COMPND 84 MOLECULE: 50S RIBOSOMAL PROTEIN L35;
COMPND 85 CHAIN: 3;
COMPND 86 MOL_ID: 29;
COMPND 87 MOLECULE: 23S RIBOSOMAL RNA;
COMPND 88 CHAIN: X;
COMPND 89 MOL_ID: 30;
COMPND 90 MOLECULE: 5S RIBOSOMAL RNA;
COMPND 91 CHAIN: Y
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 3 ORGANISM_TAXID: 1299;
SOURCE 4 MOL_ID: 2;
SOURCE 5 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS;
SOURCE 6 ORGANISM_TAXID: 1299;
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 PROTEIN SYNTHESIS, PEPTIDYLTRANSFERASE, RIBOZYME, RIBONUCLEOPROTEIN,
KEYWDS 2 RIBOSOME
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KAMINISHI,A.SCHEDLBAUER,B.OCHOA-LIZARRALDE,S.R.CONNELL,P.FUCINI
REVDAT 3 03-FEB-16 5DM6 1 COMPND
REVDAT 2 25-NOV-15 5DM6 1 JRNL
REVDAT 1 11-NOV-15 5DM6 0
JRNL AUTH T.KAMINISHI,A.SCHEDLBAUER,A.FABBRETTI,L.BRANDI,
JRNL AUTH 2 B.OCHOA-LIZARRALDE,C.G.HE,P.MILON,S.R.CONNELL,C.O.GUALERZI,
JRNL AUTH 3 P.FUCINI
JRNL TITL CRYSTALLOGRAPHIC CHARACTERIZATION OF THE RIBOSOMAL BINDING
JRNL TITL 2 SITE AND MOLECULAR MECHANISM OF ACTION OF HYGROMYCIN A.
JRNL REF NUCLEIC ACIDS RES. V. 43 10015 2015
JRNL REFN ESSN 1362-4962
JRNL PMID 26464437
JRNL DOI 10.1093/NAR/GKV975
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 58.96
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 528529
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.235
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.670
REMARK 3 FREE R VALUE TEST SET COUNT : 24666
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 58.9728 - 9.0007 1.00 17648 832 0.1968 0.2152
REMARK 3 2 9.0007 - 7.1481 1.00 17100 959 0.1891 0.2244
REMARK 3 3 7.1481 - 6.2457 1.00 17082 873 0.1843 0.2272
REMARK 3 4 6.2457 - 5.6751 1.00 16994 896 0.1856 0.2294
REMARK 3 5 5.6751 - 5.2686 1.00 16999 855 0.1882 0.2254
REMARK 3 6 5.2686 - 4.9582 1.00 16908 898 0.1954 0.2388
REMARK 3 7 4.9582 - 4.7100 1.00 16950 851 0.2006 0.2503
REMARK 3 8 4.7100 - 4.5050 1.00 16854 881 0.2051 0.2539
REMARK 3 9 4.5050 - 4.3316 1.00 16941 836 0.2142 0.2666
REMARK 3 10 4.3316 - 4.1822 1.00 16842 864 0.2181 0.2569
REMARK 3 11 4.1822 - 4.0515 1.00 16791 868 0.2257 0.2762
REMARK 3 12 4.0515 - 3.9357 1.00 16838 867 0.2311 0.2795
REMARK 3 13 3.9357 - 3.8321 1.00 16865 836 0.2400 0.2706
REMARK 3 14 3.8321 - 3.7386 1.00 16917 822 0.2484 0.2889
REMARK 3 15 3.7386 - 3.6536 1.00 16679 928 0.2635 0.3066
REMARK 3 16 3.6536 - 3.5759 1.00 16782 884 0.2726 0.3171
REMARK 3 17 3.5759 - 3.5044 1.00 16832 845 0.2899 0.3286
REMARK 3 18 3.5044 - 3.4383 1.00 16790 809 0.3059 0.3558
REMARK 3 19 3.4383 - 3.3769 1.00 16776 882 0.3237 0.3666
REMARK 3 20 3.3769 - 3.3196 1.00 16750 876 0.3271 0.3466
REMARK 3 21 3.3196 - 3.2661 1.00 16774 831 0.3392 0.3747
REMARK 3 22 3.2661 - 3.2158 1.00 16797 845 0.3500 0.3723
REMARK 3 23 3.2158 - 3.1685 1.00 16813 790 0.3590 0.4063
REMARK 3 24 3.1685 - 3.1239 1.00 16771 808 0.3725 0.3925
REMARK 3 25 3.1239 - 3.0817 0.99 16710 778 0.3922 0.4236
REMARK 3 26 3.0817 - 3.0417 0.99 16691 722 0.4196 0.4248
REMARK 3 27 3.0417 - 3.0037 0.98 16620 718 0.4487 0.4760
REMARK 3 28 3.0037 - 2.9675 0.98 16452 744 0.4640 0.4451
REMARK 3 29 2.9675 - 2.9330 0.96 16212 580 0.4659 0.4103
REMARK 3 30 2.9330 - 2.9000 0.91 15685 488 0.4684 0.4678
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.500
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.580
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 91.89
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 125.6
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.018 98492
REMARK 3 ANGLE : 1.514 147899
REMARK 3 CHIRALITY : 0.059 18615
REMARK 3 PLANARITY : 0.007 7735
REMARK 3 DIHEDRAL : 17.212 45493
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5DM6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-15.
REMARK 100 THE DEPOSITION ID IS D_1000213114.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-11
REMARK 200 TEMPERATURE (KELVIN) : 90
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 531662
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 58.960
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 21.90
REMARK 200 R MERGE (I) : 0.24100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.3800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 22.40
REMARK 200 R MERGE FOR SHELL (I) : 7.86200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.710
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, SODIUM HYDROXIDE, MAGNESIUM
REMARK 280 CHLORIDE, AMMONIUM CHLORIDE, 2-MERCAPTOETHANOL, SPERMIDINE, 2-
REMARK 280 ETHYL-1, 3-HEXANEDIOL, ETHANOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 292K
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 84.95000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 205.38000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 348.06000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 84.95000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 205.38000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 348.06000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 84.95000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 205.38000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 348.06000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 84.95000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 205.38000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 348.06000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 30-MERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 153910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 488290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1362.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 0, A, B, C, D, E, F, G, H, I,
REMARK 350 AND CHAINS: J, K, L, M, N, O, P, Q, R,
REMARK 350 AND CHAINS: S, T, U, V, W, Z, 1, 2, 3, X,
REMARK 350 AND CHAINS: Y
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 G X 0
REMARK 465 A X 243A
REMARK 465 C X 243B
REMARK 465 C X 243C
REMARK 465 G X 243D
REMARK 465 A X 243E
REMARK 465 A X 243F
REMARK 465 A X 243G
REMARK 465 C X 243H
REMARK 465 G X 243I
REMARK 465 C X 243J
REMARK 465 U X 243K
REMARK 465 U X 243L
REMARK 465 G X 243M
REMARK 465 C X 243N
REMARK 465 G X 243O
REMARK 465 U X 243P
REMARK 465 U X 243Q
REMARK 465 U X 243R
REMARK 465 C X 243S
REMARK 465 G X 243T
REMARK 465 G X 243U
REMARK 465 G X 243V
REMARK 465 G X 243W
REMARK 465 U X 243X
REMARK 465 U X 243Y
REMARK 465 G X 243Z
REMARK 465 U X 244A
REMARK 465 A X 244B
REMARK 465 G X 244C
REMARK 465 G X 244D
REMARK 465 A X 244E
REMARK 465 C X 244F
REMARK 465 C X 244G
REMARK 465 A X 244H
REMARK 465 G X 244I
REMARK 465 U X 244J
REMARK 465 U X 244K
REMARK 465 U X 244L
REMARK 465 U X 244M
REMARK 465 U X 244N
REMARK 465 A X 244O
REMARK 465 A X 244P
REMARK 465 G X 244Q
REMARK 465 A X 244R
REMARK 465 U X 244S
REMARK 465 U X 244T
REMARK 465 C X 244U
REMARK 465 A X 244V
REMARK 465 A X 244W
REMARK 465 C X 244X
REMARK 465 C X 244Y
REMARK 465 C X 244Z
REMARK 465 C X 245A
REMARK 465 C X 350A
REMARK 465 G X 350B
REMARK 465 G X 350C
REMARK 465 U X 350D
REMARK 465 U X 350E
REMARK 465 G X 350F
REMARK 465 A X 350G
REMARK 465 C X 350H
REMARK 465 U X 350I
REMARK 465 G X 350J
REMARK 465 U X 350K
REMARK 465 A X 350L
REMARK 465 C X 350M
REMARK 465 U X 350N
REMARK 465 G X 350O
REMARK 465 G X 350P
REMARK 465 C X 350Q
REMARK 465 A X 350R
REMARK 465 C X 350S
REMARK 465 C X 350T
REMARK 465 U X 350U
REMARK 465 G X 350V
REMARK 465 A X 350W
REMARK 465 G X 350X
REMARK 465 U X 350Y
REMARK 465 G X 880
REMARK 465 G X 881
REMARK 465 G X 882
REMARK 465 G X 883
REMARK 465 G X 884
REMARK 465 C X 885
REMARK 465 C X 886
REMARK 465 U X 887
REMARK 465 A X 888
REMARK 465 C X 889
REMARK 465 C X 890
REMARK 465 A X 891
REMARK 465 G X 892
REMARK 465 C X 893
REMARK 465 U X 894
REMARK 465 U X 895
REMARK 465 A X 896
REMARK 465 C X 897
REMARK 465 C X 898
REMARK 465 C X 2903
REMARK 465 U X 2904
REMARK 465 C X 2905
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 OP2 C X 1670 MG MG X 6022 1.54
REMARK 500 OP2 A X 2518 MG MG X 6033 1.54
REMARK 500 OP1 G X 2429 MG MG X 6092 1.62
REMARK 500 OP1 U X 826 MG MG X 6092 1.67
REMARK 500 ND2 ASN H 41 O2' A X 2674 1.91
REMARK 500 OG1 THR 3 34 OP1 C X 2420 1.98
REMARK 500 OP1 A Y 17 O2' U Y 110 1.98
REMARK 500 OP1 A X 578 O2' U X 1255 2.01
REMARK 500 NZ LYS 3 29 OP2 U X 2419 2.03
REMARK 500 O2' C X 635 OP1 U X 639 2.03
REMARK 500 OG1 THR L 65 OP1 G Y 52 2.04
REMARK 500 NZ LYS K 9 OP2 G X 2002 2.04
REMARK 500 O2' G X 1418 O4 U X 1578 2.05
REMARK 500 NZ LYS R 96 OP1 C X 297 2.08
REMARK 500 O PRO B 62 O2' U X 2786 2.08
REMARK 500 OG1 THR K 36 OP1 G X 1278 2.09
REMARK 500 O2' G X 612 N6 A X 615 2.11
REMARK 500 NH2 ARG 3 13 OP2 G X 222 2.11
REMARK 500 O GLN S 105 NE2 GLN S 109 2.12
REMARK 500 ND1 HIS L 37 OP1 C Y 30 2.12
REMARK 500 OG SER T 10 OP2 G X 2277 2.13
REMARK 500 OD1 ASP C 154 OG1 THR C 157 2.14
REMARK 500 O ASN 3 33 N GLY 3 35 2.15
REMARK 500 N3 A X 309 O2' G X 329 2.15
REMARK 500 O2' G X 1071 OP2 G X 1089 2.15
REMARK 500 OP1 A X 2564 O2' G X 2648 2.16
REMARK 500 O THR 2 43 N SER 2 45 2.16
REMARK 500 NH2 ARG Z 19 OP1 G X 1264 2.16
REMARK 500 O2' C X 413 O2' U X 1880 2.17
REMARK 500 O2' U X 2522 OP1 U X 2647 2.17
REMARK 500 O2' C X 1462 O2' A X 2702 2.17
REMARK 500 NZ LYS P 15 O2' A X 502 2.17
REMARK 500 NZ LYS E 172 OP2 G X 2529 2.17
REMARK 500 OP2 U X 1926 N1 G X 1929 2.17
REMARK 500 O2' G X 1266 O6 G X 2012 2.17
REMARK 500 N6 A X 2320 O2' A X 2333 2.17
REMARK 500 O TRP C 136 ND2 ASN C 140 2.18
REMARK 500 O MET C 106 OG SER C 110 2.18
REMARK 500 N2 G X 1042 O2 U X 1113 2.18
REMARK 500 O2' C X 1428 OP2 A X 1569 2.18
REMARK 500 O GLN Z 35 N HIS Z 37 2.18
REMARK 500 O2' U X 994 OP1 A X 996 2.19
REMARK 500 O LYS U 33 O2' C X 2395 2.19
REMARK 500 NZ LYS B 109 OP1 C X 2723 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 A X 492 N3 A X 492 C4 -0.038
REMARK 500 A X 761 N3 A X 761 C4 0.036
REMARK 500 A X 761 C4 A X 761 C5 0.044
REMARK 500 A X 761 C6 A X 761 N1 0.056
REMARK 500 C X1638 N1 C X1638 C6 -0.041
REMARK 500 C X1660 N3 C X1660 C4 -0.042
REMARK 500 G X1661 C4 G X1661 C5 -0.045
REMARK 500 G X1661 C6 G X1661 N1 -0.047
REMARK 500 C X1999 N3 C X1999 C4 -0.049
REMARK 500 G X2012 C8 G X2012 N9 -0.042
REMARK 500 G X2509 C6 G X2509 N1 -0.043
REMARK 500 C X2510 N3 C X2510 C4 -0.042
REMARK 500 G X2879 C4 G X2879 C5 0.044
REMARK 500 G X2879 C8 G X2879 N9 0.045
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 PRO A 121 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 PRO B 86 C - N - CA ANGL. DEV. = 10.4 DEGREES
REMARK 500 PRO B 86 C - N - CD ANGL. DEV. = -13.4 DEGREES
REMARK 500 PRO B 126 C - N - CA ANGL. DEV. = 10.2 DEGREES
REMARK 500 PRO C 18 C - N - CA ANGL. DEV. = 9.7 DEGREES
REMARK 500 PRO E 112 C - N - CA ANGL. DEV. = 12.6 DEGREES
REMARK 500 PRO J 40 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 PRO J 71 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 ARG N 28 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 PRO P 61 C - N - CA ANGL. DEV. = -15.0 DEGREES
REMARK 500 PRO 2 7 C - N - CA ANGL. DEV. = 10.9 DEGREES
REMARK 500 C X 20 N3 - C4 - N4 ANGL. DEV. = 4.5 DEGREES
REMARK 500 G X 23 O5' - P - OP1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 U X 25 C6 - N1 - C2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 G X 26 O3' - P - OP1 ANGL. DEV. = 11.6 DEGREES
REMARK 500 G X 27 O5' - P - OP1 ANGL. DEV. = -7.4 DEGREES
REMARK 500 G X 30 C8 - N9 - C4 ANGL. DEV. = -3.0 DEGREES
REMARK 500 G X 30 N9 - C4 - C5 ANGL. DEV. = 2.4 DEGREES
REMARK 500 C X 170 C5 - C6 - N1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 C X 170 C2 - N1 - C1' ANGL. DEV. = 7.1 DEGREES
REMARK 500 G X 220 O5' - P - OP1 ANGL. DEV. = -5.4 DEGREES
REMARK 500 G X 224 O3' - P - OP1 ANGL. DEV. = 7.1 DEGREES
REMARK 500 G X 327 C8 - N9 - C4 ANGL. DEV. = -2.9 DEGREES
REMARK 500 G X 338 N3 - C4 - C5 ANGL. DEV. = -3.1 DEGREES
REMARK 500 C X 445 O5' - P - OP2 ANGL. DEV. = -6.8 DEGREES
REMARK 500 G X 452 N3 - C4 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 A X 472 O4' - C1' - N9 ANGL. DEV. = 5.8 DEGREES
REMARK 500 A X 472 C2 - N3 - C4 ANGL. DEV. = -3.9 DEGREES
REMARK 500 U X 475 O3' - P - OP2 ANGL. DEV. = 8.8 DEGREES
REMARK 500 C X 486 N1 - C2 - O2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 C X 486 N3 - C2 - O2 ANGL. DEV. = 4.5 DEGREES
REMARK 500 G X 488 O3' - P - OP2 ANGL. DEV. = 7.8 DEGREES
REMARK 500 A X 492 C6 - N1 - C2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 A X 492 N1 - C2 - N3 ANGL. DEV. = 3.9 DEGREES
REMARK 500 G X 498 N1 - C6 - O6 ANGL. DEV. = 5.9 DEGREES
REMARK 500 G X 498 C5 - C6 - O6 ANGL. DEV. = -4.9 DEGREES
REMARK 500 G X 512 O4' - C1' - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 A X 513 O5' - P - OP1 ANGL. DEV. = -5.9 DEGREES
REMARK 500 A X 513 O5' - P - OP2 ANGL. DEV. = 9.8 DEGREES
REMARK 500 C X 516 C6 - N1 - C2 ANGL. DEV. = -2.5 DEGREES
REMARK 500 C X 531 C4 - C5 - C6 ANGL. DEV. = 3.2 DEGREES
REMARK 500 C X 531 C5 - C6 - N1 ANGL. DEV. = -3.8 DEGREES
REMARK 500 U X 568 O5' - P - OP2 ANGL. DEV. = -10.0 DEGREES
REMARK 500 A X 571 N1 - C6 - N6 ANGL. DEV. = 3.9 DEGREES
REMARK 500 G X 573 O5' - P - OP1 ANGL. DEV. = -9.0 DEGREES
REMARK 500 C X 581 O3' - P - OP2 ANGL. DEV. = 7.4 DEGREES
REMARK 500 G X 583 O3' - P - OP2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 A X 586 O5' - P - OP2 ANGL. DEV. = -7.7 DEGREES
REMARK 500 U X 588 C6 - N1 - C2 ANGL. DEV. = 4.0 DEGREES
REMARK 500 U X 598 C5 - C6 - N1 ANGL. DEV. = -3.5 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 483 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 0 6 -24.62 -152.39
REMARK 500 SER 0 17 -123.91 -74.89
REMARK 500 LEU 0 28 70.43 -56.92
REMARK 500 ALA 0 29 -22.10 -173.56
REMARK 500 THR 0 30 78.66 -49.39
REMARK 500 ALA 0 31 -88.60 -114.80
REMARK 500 LYS 0 32 -91.33 -132.74
REMARK 500 PHE 0 33 -138.98 -80.32
REMARK 500 ILE 0 45 -90.31 -61.93
REMARK 500 GLN 0 52 38.33 -148.58
REMARK 500 PRO 0 61 -74.25 -63.37
REMARK 500 HIS 0 62 -134.25 -73.75
REMARK 500 ARG 0 66 -151.08 -135.52
REMARK 500 SER 0 67 -139.18 -132.77
REMARK 500 THR 0 74 -166.75 -119.32
REMARK 500 LYS 0 75 123.20 -175.97
REMARK 500 ALA 0 84 38.44 -98.61
REMARK 500 ALA 0 85 -71.00 -139.15
REMARK 500 ALA 0 87 -125.99 -78.11
REMARK 500 VAL 0 89 67.76 35.74
REMARK 500 SER 0 92 -143.55 -124.11
REMARK 500 ALA 0 100 -16.82 -160.91
REMARK 500 PHE 0 103 69.85 -151.79
REMARK 500 MET 0 104 66.65 -107.57
REMARK 500 ASP 0 107 -120.55 -114.45
REMARK 500 ALA 0 108 94.94 -57.88
REMARK 500 VAL 0 109 86.60 -69.70
REMARK 500 LEU 0 123 42.11 -96.95
REMARK 500 LEU 0 126 -74.74 -120.20
REMARK 500 PRO 0 136 15.73 -69.56
REMARK 500 LYS 0 137 -9.29 -144.04
REMARK 500 SER 0 138 -107.41 -73.07
REMARK 500 ASP 0 144 54.64 -98.61
REMARK 500 VAL 0 145 62.43 -110.94
REMARK 500 ALA 0 146 -31.10 -167.08
REMARK 500 LYS 0 153 -65.16 -101.96
REMARK 500 ARG 0 156 102.30 -57.58
REMARK 500 ILE 0 157 -104.14 -62.68
REMARK 500 GLU 0 158 144.71 68.32
REMARK 500 ASP 0 162 -164.20 -123.87
REMARK 500 SER 0 175 37.44 -87.44
REMARK 500 PHE 0 176 -140.79 -132.42
REMARK 500 GLU 0 177 -154.55 -119.55
REMARK 500 ASN 0 180 -7.38 -144.63
REMARK 500 GLN 0 186 32.78 -98.69
REMARK 500 ALA 0 187 11.79 -146.77
REMARK 500 ALA 0 191 12.56 -165.35
REMARK 500 LYS 0 201 -157.39 -125.40
REMARK 500 VAL 0 203 108.72 65.44
REMARK 500 SER 0 207 -143.17 -165.65
REMARK 500
REMARK 500 THIS ENTRY HAS 492 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 ALA B 73 PRO B 74 -147.46
REMARK 500 ALA B 85 PRO B 86 -137.47
REMARK 500 GLY B 178 GLU B 179 148.41
REMARK 500 VAL C 187 ILE C 188 -145.53
REMARK 500 ASP G 37 GLU G 38 -148.26
REMARK 500 HIS Z 37 GLY Z 38 148.30
REMARK 500 TYR Z 52 ASP Z 53 149.24
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 X6051 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY B 110 O
REMARK 620 2 A X2821 OP2 79.0
REMARK 620 3 G X2822 OP2 71.5 79.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6037 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 14 OP2
REMARK 620 2 G X 15 OP2 90.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6168 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 31 OP1
REMARK 620 2 C X1239 OP1 68.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6058 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 165F OP1
REMARK 620 2 U X2243 OP1 71.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6109 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 169 OP1
REMARK 620 2 C X 170 OP2 87.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6139 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 382 OP2
REMARK 620 2 G X 386 OP1 122.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6014 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 450 O6
REMARK 620 2 C X 453 OP1 85.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6089 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 526 OP1
REMARK 620 2 C X 527 OP1 99.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6065 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 530 O6
REMARK 620 2 U X2022 OP1 91.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6021 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 531 OP2
REMARK 620 2 C X2036 OP1 174.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6117 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X 568 O4
REMARK 620 2 A X 973 OP2 96.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6035 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 570 O6
REMARK 620 2 A X2448 OP1 158.8
REMARK 620 3 C X2499 OP1 75.4 104.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6016 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X 576 OP1
REMARK 620 2 A X2503 OP1 89.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6084 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 730 OP2
REMARK 620 2 C X 731 OP2 74.0
REMARK 620 3 A X 761 OP1 105.3 95.3
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6041 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X 740 OP2
REMARK 620 2 A X1783 OP1 138.4
REMARK 620 3 A X1784 OP1 91.2 129.5
REMARK 620 4 A X1784 OP2 109.3 91.5 55.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6004 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 751 OP1
REMARK 620 2 A X1614 OP1 156.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6054 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 783 OP2
REMARK 620 2 A X 784 OP2 96.8
REMARK 620 3 A X2589 OP1 101.0 93.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6059 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 784 OP1
REMARK 620 2 G X2588 OP1 87.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6011 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X 787 OP1
REMARK 620 2 C X 790 OP2 134.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6166 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 818 OP2
REMARK 620 2 G X1187 O6 90.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6094 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X 944 O3'
REMARK 620 2 A X 945 OP2 56.6
REMARK 620 3 G X 946 OP1 123.6 91.5
REMARK 620 4 G X 946 OP2 83.4 96.8 53.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6028 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X 948 OP1
REMARK 620 2 U X 962 OP1 93.3
REMARK 620 3 U X 963 OP2 115.2 137.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6026 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X 990 OP2
REMARK 620 2 C X 991 OP2 76.9
REMARK 620 3 G X1186 OP2 150.1 73.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6070 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1009 OP2
REMARK 620 2 A X1010 OP2 102.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6015 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1265 OP2
REMARK 620 2 U X2615 OP1 95.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6018 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1268 OP1
REMARK 620 2 C X2006 OP1 92.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6029 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1269 OP2
REMARK 620 2 A X2005 OP1 115.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X1271 OP2
REMARK 620 2 A X1272 OP1 70.4
REMARK 620 3 G X1647 OP1 154.7 107.3
REMARK 620 4 C X1648 OP1 91.8 160.7 92.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6062 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X1298 OP2
REMARK 620 2 U X1639 OP2 168.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6102 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X1314 OP1
REMARK 620 2 C X1315 OP2 75.7
REMARK 620 3 G X1332 OP1 93.8 155.9
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6155 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1342 OP2
REMARK 620 2 U X1602 O4 92.6
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6103 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1378 O2'
REMARK 620 2 U X1379 OP2 71.4
REMARK 620 3 G X1380 OP2 86.7 69.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6181 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1439 OP2
REMARK 620 2 U X1440 O4 98.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6032 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X1455 OP2
REMARK 620 2 G X1456 OP2 94.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6079 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1603 OP1
REMARK 620 2 C X1604 OP2 94.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6009 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1664 OP1
REMARK 620 2 A X1665 OP2 88.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6022 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1669 OP2
REMARK 620 2 U X1671 O4 70.2
REMARK 620 3 G X2550 OP1 65.5 106.2
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6025 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X1780 OP1
REMARK 620 2 C X1782 OP1 87.7
REMARK 620 3 A X1783 OP2 164.3 77.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6019 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X2035 OP1
REMARK 620 2 G X2035 OP2 52.5
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6017 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X2056 OP2
REMARK 620 2 A X2057 OP2 89.8
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6008 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X2061 OP2
REMARK 620 2 G X2502 OP2 101.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6151 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X2248 OP2
REMARK 620 2 U X2249 O4 99.7
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6076 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2268 OP1
REMARK 620 2 A X2269 OP1 92.0
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6092 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X2427 OP1
REMARK 620 2 G X2428 OP1 73.1
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6077 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X2431 OP2
REMARK 620 2 A X2432 OP2 86.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6071 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2448 OP2
REMARK 620 2 C X2498 OP2 81.0
REMARK 620 3 C X2499 OP2 67.4 56.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6020 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 C X2573 OP1
REMARK 620 2 G X2574 OP1 81.7
REMARK 620 3 C X2575 OP2 83.9 96.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6012 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X2576 OP1
REMARK 620 2 A X2577 OP1 91.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6050 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X2582 OP2
REMARK 620 2 G X2583 OP2 83.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6048 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 U X2615 OP2
REMARK 620 2 C X2616 OP2 76.2
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6042 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 G X2682 OP2
REMARK 620 2 A X2721 OP1 161.3
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6044 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2711 OP1
REMARK 620 2 A X2712A OP1 68.4
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG X6007 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 A X2711 OP2
REMARK 620 2 A X2712A OP2 105.4
REMARK 620 3 G X2714 OP2 95.8 132.3
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG M 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6004
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6006
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6007
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6008
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6009
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6011
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6012
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6013
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6014
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6015
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6016
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6017
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6018
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6019
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6020
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6021
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6022
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6023
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6024
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6025
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6026
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6028
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6029
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6031
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6032
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6033
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6034
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6035
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6037
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6038
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6039
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6040
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6041
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6042
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6044
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6045
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6046
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6047
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6048
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6049
REMARK 800
REMARK 800 SITE_IDENTIFIER: AG9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6050
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6051
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6052
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6053
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6054
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6057
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6058
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6059
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6060
REMARK 800
REMARK 800 SITE_IDENTIFIER: AH9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6061
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6062
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6064
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6065
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6067
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6069
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6070
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6071
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6072
REMARK 800
REMARK 800 SITE_IDENTIFIER: AI9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6073
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6075
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6076
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6077
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6078
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6079
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6081
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6084
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6085
REMARK 800
REMARK 800 SITE_IDENTIFIER: AJ9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6088
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6089
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6090
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6092
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6093
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6094
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6099
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AK9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6108
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6109
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6110
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6111
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6112
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6113
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6114
REMARK 800
REMARK 800 SITE_IDENTIFIER: AL9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6115
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6116
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6117
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6119
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6121
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6123
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6125
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6127
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6128
REMARK 800
REMARK 800 SITE_IDENTIFIER: AM9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6129
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6134
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6135
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6137
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6139
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6140
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6141
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6144
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6145
REMARK 800
REMARK 800 SITE_IDENTIFIER: AN9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6151
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6153
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6155
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6156
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6157
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6160
REMARK 800
REMARK 800 SITE_IDENTIFIER: AO9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6166
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6168
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6169
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6172
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6177
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6179
REMARK 800
REMARK 800 SITE_IDENTIFIER: AP9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6180
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6181
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6185
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6186
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6189
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 6192
REMARK 800
REMARK 800 SITE_IDENTIFIER: AQ6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Y 202
DBREF 5DM6 0 1 224 UNP Q9RSS8 RL1_DEIRA 6 229
DBREF 5DM6 A 2 275 UNP Q9RXJ9 RL2_DEIRA 2 275
DBREF 5DM6 B 1 205 UNP Q9RXK2 RL3_DEIRA 1 205
DBREF 5DM6 C 2 198 UNP Q9RXK1 RL4_DEIRA 2 198
DBREF 5DM6 D 3 179 UNP Q9RXJ0 RL5_DEIRA 3 179
DBREF 5DM6 E 5 175 UNP Q9RSL3 RL6_DEIRA 5 175
DBREF 5DM6 F 4 144 UNP Q9RSS7 RL11_DEIRA 4 144
DBREF 5DM6 G 30 171 UNP Q9RXY1 RL13_DEIRA 30 171
DBREF 5DM6 H 1 134 UNP Q9RXJ2 RL14_DEIRA 1 134
DBREF 5DM6 I 4 144 UNP Q9RSK9 RL15_DEIRA 4 144
DBREF 5DM6 J 6 141 UNP Q9RXJ5 RL16_DEIRA 5 140
DBREF 5DM6 K 3 115 UNP Q9RSJ5 RL17_DEIRA 3 115
DBREF 5DM6 L 8 111 UNP Q9RSL2 RL18_DEIRA 8 111
DBREF 5DM6 M 2 106 UNP Q9RWB4 RL19_DEIRA 2 106
DBREF 5DM6 N 2 118 UNP Q9RSW7 RL20_DEIRA 2 118
DBREF 5DM6 O 5 98 UNP Q9RY64 RL21_DEIRA 5 98
DBREF 5DM6 P 8 134 UNP Q9RXJ7 RL22_DEIRA 8 134
DBREF 5DM6 Q 2 94 UNP Q9RXK0 RL23_DEIRA 2 94
DBREF 5DM6 R 4 113 UNP Q9RXJ1 RL24_DEIRA 4 113
DBREF 5DM6 S 1 175 UNP Q9RX88 RL25_DEIRA 1 175
DBREF 5DM6 T 2 85 UNP Q9RY65 RL27_DEIRA 2 85
DBREF 5DM6 U 8 79 UNP Q9RRG8 RL28_DEIRA 8 79
DBREF 5DM6 V 1 66 UNP Q9RXJ4 RL29_DEIRA 1 66
DBREF 5DM6 W 1 55 UNP Q9RSL0 RL30_DEIRA 1 55
DBREF 5DM6 Z 3 59 UNP P49228 RL32_DEIRA 3 59
DBREF 5DM6 1 0 53 PDB 5DM6 5DM6 0 53
DBREF 5DM6 2 1 47 UNP Q9RSH2 RL34_DEIRA 1 47
DBREF 5DM6 3 2 66 UNP Q9RSW6 RL35_DEIRA 2 66
DBREF1 5DM6 X 0 2905 GB AE000513.1
DBREF2 5DM6 X 11612676 2587938 2585058
DBREF1 5DM6 Y 2 123 GB AE000513.1
DBREF2 5DM6 Y 11612676 254393 254514
SEQADV 5DM6 LYS A 7 UNP Q9RXJ9 ARG 7 CONFLICT
SEQADV 5DM6 ALA A 25 UNP Q9RXJ9 THR 25 CONFLICT
SEQADV 5DM6 LEU A 270 UNP Q9RXJ9 ILE 270 CONFLICT
SEQADV 5DM6 MET F 1 UNP Q9RSS7 EXPRESSION TAG
SEQADV 5DM6 ARG F 2 UNP Q9RSS7 EXPRESSION TAG
SEQADV 5DM6 ARG F 3 UNP Q9RSS7 EXPRESSION TAG
SEQADV 5DM6 LYS L 26 UNP Q9RSL2 ARG 26 CONFLICT
SEQADV 5DM6 GLY M 107 UNP Q9RWB4 EXPRESSION TAG
SEQADV 5DM6 LYS M 108 UNP Q9RWB4 EXPRESSION TAG
SEQADV 5DM6 ALA M 109 UNP Q9RWB4 EXPRESSION TAG
SEQADV 5DM6 ALA M 110 UNP Q9RWB4 EXPRESSION TAG
SEQADV 5DM6 ILE U 67 UNP Q9RRG8 LEU 67 CONFLICT
SEQADV 5DM6 U X 1510 GB 11612676 UNK 86412 CONFLICT
SEQRES 1 0 224 LYS ARG TYR ARG ALA LEU GLU GLY LYS VAL ASP ARG ASN
SEQRES 2 0 224 LYS GLN TYR SER ILE ASP GLU ALA ALA ALA LEU VAL LYS
SEQRES 3 0 224 GLU LEU ALA THR ALA LYS PHE ASP GLU THR VAL GLU VAL
SEQRES 4 0 224 HIS PHE ARG LEU GLY ILE ASP PRO ARG LYS SER ASP GLN
SEQRES 5 0 224 ASN VAL ARG GLY THR VAL ALA LEU PRO HIS GLY THR GLY
SEQRES 6 0 224 ARG SER VAL ARG VAL ALA VAL ILE THR LYS GLY GLU ASN
SEQRES 7 0 224 VAL GLN ALA ALA GLU ALA ALA GLY ALA ASP VAL VAL GLY
SEQRES 8 0 224 SER ASP GLU LEU ILE GLU ARG ILE ALA GLY GLY PHE MET
SEQRES 9 0 224 ASP PHE ASP ALA VAL VAL ALA THR PRO ASP MET MET ALA
SEQRES 10 0 224 GLN ILE GLY GLN LYS LEU ALA ARG LEU LEU GLY PRO ARG
SEQRES 11 0 224 GLY LEU LEU PRO ASN PRO LYS SER GLY THR VAL GLY ALA
SEQRES 12 0 224 ASP VAL ALA GLY MET VAL ARG GLY LEU LYS ALA GLY ARG
SEQRES 13 0 224 ILE GLU PHE ARG ASN ASP LYS THR GLY VAL VAL HIS ALA
SEQRES 14 0 224 PRO ILE GLY LYS ALA SER PHE GLU SER GLY ASN LEU SER
SEQRES 15 0 224 ALA ASN TYR GLN ALA LEU ILE SER ALA LEU GLU GLY ALA
SEQRES 16 0 224 LYS PRO GLY THR ALA LYS GLY VAL PHE LEU ARG SER ALA
SEQRES 17 0 224 TYR LEU THR THR THR MET GLY PRO SER ILE PRO LEU ALA
SEQRES 18 0 224 LEU GLY GLY
SEQRES 1 A 274 ALA VAL LYS LYS TYR LYS PRO TYR THR PRO SER ARG ARG
SEQRES 2 A 274 GLN MET THR THR ALA ASP PHE SER GLY LEU ALA 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 LEU VAL THR ARG ARG
SEQRES 22 A 274 LYS
SEQRES 1 B 205 MET LYS GLY ILE LEU GLY THR LYS ILE GLY MET THR GLN
SEQRES 2 B 205 ILE TRP LYS ASN ASP ARG ALA ILE PRO VAL THR VAL VAL
SEQRES 3 B 205 LEU ALA GLY PRO CYS PRO ILE VAL GLN ARG LYS THR ALA
SEQRES 4 B 205 GLN THR ASP GLY TYR GLU ALA VAL GLN ILE GLY TYR ALA
SEQRES 5 B 205 PRO LYS ALA GLU ARG LYS VAL ASN LYS PRO MET GLN GLY
SEQRES 6 B 205 HIS PHE ALA LYS ALA GLY VAL ALA PRO THR ARG ILE LEU
SEQRES 7 B 205 ARG GLU PHE ARG GLY PHE ALA PRO ASP GLY ASP SER VAL
SEQRES 8 B 205 ASN VAL ASP ILE PHE ALA GLU GLY GLU LYS ILE ASP ALA
SEQRES 9 B 205 THR GLY THR SER LYS GLY LYS GLY THR GLN GLY VAL MET
SEQRES 10 B 205 LYS ARG TRP ASN PHE ALA GLY GLY PRO ALA SER HIS GLY
SEQRES 11 B 205 SER LYS LYS TRP HIS ARG ARG PRO GLY SER ILE GLY GLN
SEQRES 12 B 205 ARG LYS THR PRO GLY ARG VAL TYR LYS GLY LYS ARG MET
SEQRES 13 B 205 ALA GLY HIS MET GLY MET GLU ARG VAL THR VAL GLN ASN
SEQRES 14 B 205 LEU GLU VAL VAL GLU ILE ARG ALA GLY GLU ASN LEU ILE
SEQRES 15 B 205 LEU VAL LYS GLY ALA ILE PRO GLY ALA ASN GLY GLY LEU
SEQRES 16 B 205 VAL VAL LEU ARG SER ALA ALA LYS ALA SER
SEQRES 1 C 197 ALA GLN ILE ASN VAL ILE GLY GLN ASN GLY GLY ARG THR
SEQRES 2 C 197 ILE GLU LEU PRO LEU PRO GLU VAL ASN SER GLY VAL LEU
SEQRES 3 C 197 HIS GLU VAL VAL THR TRP GLN LEU ALA SER ARG ARG ARG
SEQRES 4 C 197 GLY THR ALA SER THR ARG THR ARG ALA GLN VAL SER LYS
SEQRES 5 C 197 THR GLY ARG LYS MET TYR GLY GLN LYS GLY THR GLY ASN
SEQRES 6 C 197 ALA ARG HIS GLY ASP ARG SER VAL PRO THR PHE VAL GLY
SEQRES 7 C 197 GLY GLY VAL ALA PHE GLY PRO LYS PRO ARG SER TYR ASP
SEQRES 8 C 197 TYR THR LEU PRO ARG GLN VAL ARG GLN LEU GLY LEU ALA
SEQRES 9 C 197 MET ALA ILE ALA SER ARG GLN GLU GLY GLY LYS LEU VAL
SEQRES 10 C 197 ALA VAL ASP GLY PHE ASP ILE ALA ASP ALA LYS THR LYS
SEQRES 11 C 197 ASN PHE ILE SER TRP ALA LYS GLN ASN GLY LEU ASP GLY
SEQRES 12 C 197 THR GLU LYS VAL LEU LEU VAL THR ASP ASP GLU ASN THR
SEQRES 13 C 197 ARG ARG ALA ALA ARG ASN VAL SER TRP VAL SER VAL LEU
SEQRES 14 C 197 PRO VAL ALA GLY VAL ASN VAL TYR ASP ILE LEU ARG HIS
SEQRES 15 C 197 ASP ARG LEU VAL ILE ASP ALA ALA ALA LEU GLU ILE VAL
SEQRES 16 C 197 GLU GLU
SEQRES 1 D 177 GLN LEU LYS THR LYS TYR ASN ASP GLN VAL ARG PRO ALA
SEQRES 2 D 177 LEU MET GLN GLN PHE GLY TYR SER SER VAL MET ALA VAL
SEQRES 3 D 177 PRO ARG ILE GLU LYS ILE VAL VAL ASN GLU GLY LEU GLY
SEQRES 4 D 177 SER SER LYS GLU ASP SER LYS ALA ILE ASP LYS ALA ALA
SEQRES 5 D 177 LYS GLU LEU ALA LEU ILE THR LEU GLN LYS PRO ILE ILE
SEQRES 6 D 177 THR LYS ALA LYS LYS SER ILE SER ASN PHE LYS LEU ARG
SEQRES 7 D 177 GLN GLY MET PRO VAL GLY ILE LYS VAL THR LEU ARG GLY
SEQRES 8 D 177 GLU ARG MET TYR VAL PHE LEU GLU LYS LEU ILE ASN ILE
SEQRES 9 D 177 GLY LEU PRO ARG ILE ARG ASP PHE ARG GLY ILE ASN PRO
SEQRES 10 D 177 ASN ALA PHE ASP GLY ARG GLY ASN TYR ASN LEU GLY ILE
SEQRES 11 D 177 LYS GLU GLN LEU ILE PHE PRO GLU ILE THR TYR ASP MET
SEQRES 12 D 177 VAL ASP LYS THR ARG GLY MET ASP ILE THR ILE VAL THR
SEQRES 13 D 177 THR ALA LYS THR ASP GLU GLU ALA ARG ALA LEU LEU GLN
SEQRES 14 D 177 SER MET GLY LEU PRO PHE ARG LYS
SEQRES 1 E 171 GLY LYS GLN PRO ILE ALA VAL PRO SER GLY VAL THR VAL
SEQRES 2 E 171 ASN ALA GLN ASP GLY VAL PHE LYS VAL LYS GLY PRO LYS
SEQRES 3 E 171 GLY GLU LEU THR VAL PRO TYR ASN THR GLU LEU THR VAL
SEQRES 4 E 171 ARG GLN ASP GLY ASP GLN LEU LEU VAL GLU ARG PRO SER
SEQRES 5 E 171 ASP ALA GLN LYS HIS ARG ALA LEU HIS GLY LEU THR ARG
SEQRES 6 E 171 THR LEU VAL ALA ASN ALA VAL LYS GLY VAL SER ASP GLY
SEQRES 7 E 171 TYR THR ILE ASN LEU GLU LEU ARG GLY VAL GLY PHE ARG
SEQRES 8 E 171 ALA LYS LEU THR GLY LYS ALA LEU GLU MET ASN ILE GLY
SEQRES 9 E 171 TYR SER HIS PRO VAL ILE ILE GLU PRO PRO ALA GLY VAL
SEQRES 10 E 171 THR PHE ALA VAL PRO GLU PRO THR ARG ILE ASP VAL SER
SEQRES 11 E 171 GLY ILE ASP LYS GLN LEU VAL GLY GLN VAL ALA ALA ASN
SEQRES 12 E 171 VAL ARG LYS VAL ARG LYS PRO ASP ALA TYR HIS GLY LYS
SEQRES 13 E 171 GLY VAL ARG PHE VAL GLY GLU GLN ILE ALA LEU LYS ALA
SEQRES 14 E 171 GLY LYS
SEQRES 1 F 144 MET ARG ARG 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 142 LYS THR TYR ILE PRO LYS ASN ASP GLU GLN ASN TRP VAL
SEQRES 2 G 142 VAL VAL ASP ALA SER GLY VAL PRO LEU GLY ARG LEU ALA
SEQRES 3 G 142 THR LEU ILE ALA SER ARG ILE ARG GLY LYS HIS ARG PRO
SEQRES 4 G 142 ASP PHE THR PRO ASN MET ILE GLN GLY ASP PHE VAL VAL
SEQRES 5 G 142 VAL ILE ASN ALA ALA GLN VAL ALA LEU THR GLY LYS LYS
SEQRES 6 G 142 LEU ASP ASP LYS VAL TYR THR ARG TYR THR GLY TYR GLN
SEQRES 7 G 142 GLY GLY LEU LYS THR GLU THR ALA ARG GLU ALA LEU SER
SEQRES 8 G 142 LYS HIS PRO GLU ARG VAL ILE GLU HIS ALA VAL PHE GLY
SEQRES 9 G 142 MET LEU PRO LYS GLY ARG GLN GLY ARG ALA MET HIS THR
SEQRES 10 G 142 ARG LEU LYS VAL TYR ALA GLY GLU THR HIS PRO HIS SER
SEQRES 11 G 142 ALA GLN LYS PRO GLN VAL LEU LYS THR GLN PRO LEU
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 141 HIS ASP LEU LYS PRO THR PRO GLY SER ARG LYS ASP ARG
SEQRES 2 I 141 LYS ARG VAL GLY ARG GLY PRO GLY GLY THR ASP LYS THR
SEQRES 3 I 141 ALA GLY ARG GLY HIS LYS GLY GLN LYS SER ARG SER GLY
SEQRES 4 I 141 ALA GLY LYS GLY ALA PHE PHE GLU GLY GLY ARG SER ARG
SEQRES 5 I 141 LEU ILE ALA ARG LEU PRO LYS ARG GLY PHE ASN ASN VAL
SEQRES 6 I 141 GLY THR THR TYR GLU VAL VAL LYS LEU SER GLN LEU GLN
SEQRES 7 I 141 ASP LEU GLU ASP THR THR PHE ASP ARG ASP THR LEU GLU
SEQRES 8 I 141 ALA TYR ARG LEU VAL ARG ARG LYS ASN ARG PRO VAL LYS
SEQRES 9 I 141 LEU LEU ALA SER GLY GLU ILE SER ARG ALA VAL THR VAL
SEQRES 10 I 141 HIS VAL ASP ALA ALA SER ALA ALA ALA ILE LYS ALA VAL
SEQRES 11 I 141 GLU ALA ALA GLY GLY ARG VAL VAL LEU PRO GLU
SEQRES 1 J 136 LYS ARG THR LYS PHE ARG LYS GLN PHE ARG GLY ARG MET
SEQRES 2 J 136 THR GLY ASP ALA LYS GLY GLY ASP TYR VAL ALA PHE GLY
SEQRES 3 J 136 ASP TYR GLY LEU ILE ALA MET GLU PRO ALA TRP ILE LYS
SEQRES 4 J 136 SER ASN GLN ILE GLU ALA CYS ARG ILE VAL MET SER ARG
SEQRES 5 J 136 HIS PHE ARG ARG GLY GLY LYS ILE TYR ILE ARG ILE PHE
SEQRES 6 J 136 PRO ASP LYS PRO VAL THR LYS LYS PRO ALA GLU THR ARG
SEQRES 7 J 136 MET GLY LYS GLY LYS GLY ALA VAL GLU TYR TRP VAL SER
SEQRES 8 J 136 VAL VAL LYS PRO GLY ARG VAL MET PHE GLU VAL ALA GLY
SEQRES 9 J 136 VAL THR GLU GLU GLN ALA LYS GLU ALA PHE ARG LEU ALA
SEQRES 10 J 136 GLY HIS LYS LEU PRO ILE GLN THR LYS MET VAL LYS ARG
SEQRES 11 J 136 GLU VAL TYR ASP GLU ALA
SEQRES 1 K 113 HIS GLY LYS ALA GLY ARG LYS LEU ASN ARG ASN SER SER
SEQRES 2 K 113 ALA ARG VAL ALA LEU ALA ARG ALA GLN ALA THR ALA LEU
SEQRES 3 K 113 LEU ARG GLU GLY ARG ILE GLN THR THR LEU THR LYS ALA
SEQRES 4 K 113 LYS GLU LEU ARG PRO PHE VAL GLU GLN LEU ILE THR THR
SEQRES 5 K 113 ALA LYS GLY GLY ASP LEU HIS SER ARG ARG LEU VAL ALA
SEQRES 6 K 113 GLN ASP ILE HIS ASP LYS ASP VAL VAL ARG LYS VAL MET
SEQRES 7 K 113 ASP GLU VAL ALA PRO LYS TYR ALA GLU ARG PRO GLY GLY
SEQRES 8 K 113 TYR THR ARG ILE LEU ARG VAL GLY THR ARG ARG GLY ASP
SEQRES 9 K 113 GLY VAL THR MET ALA LEU ILE GLU LEU
SEQRES 1 L 104 ARG ARG LYS LEU ARG THR ARG ARG LYS VAL ARG THR THR
SEQRES 2 L 104 THR ALA ALA SER GLY LYS LEU ARG LEU SER VAL TYR ARG
SEQRES 3 L 104 SER SER LYS HIS ILE TYR ALA GLN ILE ILE ASP ASP SER
SEQRES 4 L 104 ARG GLY GLN THR LEU ALA ALA ALA SER SER ALA ALA LEU
SEQRES 5 L 104 LYS SER GLY ASN LYS THR ASP THR ALA ALA ALA VAL GLY
SEQRES 6 L 104 LYS ALA LEU ALA ALA ALA ALA ALA GLU LYS GLY ILE LYS
SEQRES 7 L 104 GLN VAL VAL PHE ASP ARG GLY SER TYR LYS TYR HIS GLY
SEQRES 8 L 104 ARG VAL LYS ALA LEU ALA ASP ALA ALA ARG GLU GLY GLY
SEQRES 1 M 109 GLN THR HIS ILE LYS ILE ASN ARG GLY GLU LEU LEU ARG
SEQRES 2 M 109 GLY ILE GLU GLN ASP HIS THR ARG GLN LEU PRO ASP PHE
SEQRES 3 M 109 ARG PRO GLY ASP THR VAL ARG VAL ASP THR LYS VAL ARG
SEQRES 4 M 109 GLU GLY ASN ARG THR ARG SER GLN ALA PHE GLU GLY VAL
SEQRES 5 M 109 VAL ILE ALA ILE ASN GLY SER GLY SER ARG LYS SER PHE
SEQRES 6 M 109 THR VAL ARG LYS ILE SER PHE GLY GLU GLY VAL GLU ARG
SEQRES 7 M 109 VAL PHE PRO PHE ALA SER PRO LEU VAL ASN GLN VAL THR
SEQRES 8 M 109 ILE VAL GLU ARG GLY LYS VAL ARG ARG ALA LYS LEU TYR
SEQRES 9 M 109 TYR GLY LYS ALA ALA
SEQRES 1 N 117 PRO ARG ALA LYS THR GLY ILE VAL ARG ARG ARG ARG HIS
SEQRES 2 N 117 LYS LYS VAL LEU LYS ARG ALA LYS GLY PHE TRP GLY SER
SEQRES 3 N 117 ARG SER LYS GLN TYR ARG ASN ALA PHE GLN THR LEU LEU
SEQRES 4 N 117 ASN ALA ALA THR TYR GLU TYR ARG ASP ARG ARG ASN LYS
SEQRES 5 N 117 LYS ARG ASP PHE ARG ARG LEU TRP ILE GLN ARG ILE ASN
SEQRES 6 N 117 ALA GLY ALA ARG LEU HIS GLY MET ASN TYR SER THR PHE
SEQRES 7 N 117 ILE ASN GLY LEU LYS ARG ALA ASN ILE ASP LEU ASN ARG
SEQRES 8 N 117 LYS VAL LEU ALA ASP ILE ALA ALA ARG GLU PRO GLU ALA
SEQRES 9 N 117 PHE LYS ALA LEU VAL ASP ALA SER ARG ASN ALA ARG GLN
SEQRES 1 O 94 ILE GLN THR GLY GLY LYS GLN TYR ARG VAL SER GLU GLY
SEQRES 2 O 94 ASP VAL ILE ARG VAL GLU SER LEU GLN GLY GLU ALA GLY
SEQRES 3 O 94 ASP LYS VAL GLU LEU LYS ALA LEU PHE VAL GLY GLY GLU
SEQRES 4 O 94 GLN THR VAL PHE GLY GLU ASP ALA GLY LYS TYR THR VAL
SEQRES 5 O 94 GLN ALA GLU VAL VAL GLU HIS GLY ARG GLY LYS LYS ILE
SEQRES 6 O 94 TYR ILE ARG LYS TYR LYS SER GLY VAL GLN TYR ARG ARG
SEQRES 7 O 94 ARG THR GLY HIS ARG GLN ASN PHE THR ALA ILE LYS ILE
SEQRES 8 O 94 LEU GLY ILE
SEQRES 1 P 127 PHE ARG ASN LYS LYS GLN ARG LYS GLN GLN VAL LYS LEU
SEQRES 2 P 127 ARG LYS PRO GLY PHE ALA VAL ALA LYS TYR VAL ARG MET
SEQRES 3 P 127 SER PRO ARG LYS VAL ARG LEU VAL VAL ASP VAL ILE ARG
SEQRES 4 P 127 GLY LYS SER VAL GLN ASP ALA GLU ASP LEU LEU ARG PHE
SEQRES 5 P 127 ILE PRO ARG SER ALA SER GLU PRO VAL ALA LYS VAL LEU
SEQRES 6 P 127 ASN SER ALA LYS ALA ASN ALA LEU HIS ASN ASP GLU MET
SEQRES 7 P 127 LEU GLU ASP ARG LEU PHE VAL LYS GLU ALA TYR VAL ASP
SEQRES 8 P 127 ALA GLY PRO THR LEU LYS ARG LEU ILE PRO ARG ALA ARG
SEQRES 9 P 127 GLY SER ALA ASN ILE ILE LYS LYS ARG THR SER HIS ILE
SEQRES 10 P 127 THR ILE ILE VAL ALA GLU LYS GLY ASN LYS
SEQRES 1 Q 93 SER HIS TYR ASP ILE LEU GLN ALA PRO VAL ILE SER GLU
SEQRES 2 Q 93 LYS ALA TYR SER ALA MET GLU ARG GLY VAL TYR SER PHE
SEQRES 3 Q 93 TRP VAL SER PRO LYS ALA THR LYS THR GLU ILE LYS ASP
SEQRES 4 Q 93 ALA ILE GLN GLN ALA PHE GLY VAL ARG VAL ILE GLY ILE
SEQRES 5 Q 93 SER THR MET ASN VAL PRO GLY LYS ARG LYS ARG VAL GLY
SEQRES 6 Q 93 ARG PHE ILE GLY GLN ARG ASN ASP ARG LYS LYS ALA ILE
SEQRES 7 Q 93 VAL ARG LEU ALA GLU GLY GLN SER ILE GLU ALA LEU ALA
SEQRES 8 Q 93 GLY GLN
SEQRES 1 R 110 PRO SER ALA GLY SER HIS HIS ASN ASP LYS LEU HIS PHE
SEQRES 2 R 110 LYS LYS GLY ASP THR VAL ILE VAL LEU SER GLY LYS HIS
SEQRES 3 R 110 LYS GLY GLN THR GLY LYS VAL LEU LEU ALA LEU PRO ARG
SEQRES 4 R 110 ASP GLN LYS VAL VAL VAL GLU GLY VAL ASN VAL ILE THR
SEQRES 5 R 110 LYS ASN VAL LYS PRO SER MET THR ASN PRO GLN GLY GLY
SEQRES 6 R 110 GLN GLU GLN ARG GLU LEU ALA LEU HIS ALA SER LYS VAL
SEQRES 7 R 110 ALA LEU VAL ASP PRO GLU THR GLY LYS ALA THR ARG VAL
SEQRES 8 R 110 ARG LYS GLN ILE VAL ASP GLY LYS LYS VAL ARG VAL ALA
SEQRES 9 R 110 VAL ALA SER GLY LYS THR
SEQRES 1 S 175 MET GLU LEU THR ALA LYS PRO ARG THR PRO LYS GLN LYS
SEQRES 2 S 175 LEU ASP GLU SER MET ILE ALA ALA VAL ALA TYR ASN LYS
SEQRES 3 S 175 GLU ASN ASN VAL SER PHE ALA LEU ASP ARG LYS ALA PHE
SEQRES 4 S 175 ASP ARG ALA PHE ARG GLN GLN SER THR THR GLY LEU PHE
SEQRES 5 S 175 ASP ILE THR VAL GLU GLY GLY GLU THR PHE PRO ALA LEU
SEQRES 6 S 175 VAL LYS ALA VAL GLN MET ASP LYS ARG LYS ARG ALA PRO
SEQRES 7 S 175 ILE HIS VAL ASP PHE TYR MET VAL THR TYR GLY GLU PRO
SEQRES 8 S 175 VAL GLU VAL SER VAL PRO VAL HIS THR THR GLY ARG SER
SEQRES 9 S 175 GLN GLY GLU VAL GLN GLY GLY LEU VAL ASP ILE VAL VAL
SEQRES 10 S 175 HIS ASN LEU GLN ILE VAL ALA PRO GLY PRO ARG ARG ILE
SEQRES 11 S 175 PRO GLN GLU LEU VAL VAL ASP VAL THR LYS MET ASN ILE
SEQRES 12 S 175 GLY ASP HIS ILE THR ALA GLY ASP ILE LYS LEU PRO GLU
SEQRES 13 S 175 GLY CYS THR LEU ALA ALA ASP PRO GLU LEU THR VAL VAL
SEQRES 14 S 175 SER VAL LEU PRO PRO ARG
SEQRES 1 T 84 ALA HIS LYS LYS GLY VAL GLY SER SER LYS ASN GLY ARG
SEQRES 2 T 84 ASP SER ASN PRO LYS TYR LEU GLY VAL LYS LYS PHE GLY
SEQRES 3 T 84 GLY GLU VAL VAL LYS ALA GLY ASN ILE LEU VAL ARG GLN
SEQRES 4 T 84 ARG GLY THR LYS PHE LYS ALA GLY GLN GLY VAL GLY MET
SEQRES 5 T 84 GLY ARG ASP HIS THR LEU PHE ALA LEU SER ASP GLY LYS
SEQRES 6 T 84 VAL VAL PHE ILE ASN LYS GLY LYS GLY ALA ARG PHE ILE
SEQRES 7 T 84 SER ILE GLU ALA ALA GLN
SEQRES 1 U 72 THR GLY LYS LYS ASN LEU VAL VAL ASN SER VAL ILE ARG
SEQRES 2 U 72 ARG GLY LYS ALA ARG ALA ASP GLY GLY VAL GLY ARG LYS
SEQRES 3 U 72 THR THR GLY ILE THR LYS ARG VAL GLN ARG ALA ASN LEU
SEQRES 4 U 72 HIS LYS LYS ALA ILE ARG GLU ASN GLY GLN VAL LYS THR
SEQRES 5 U 72 VAL TRP LEU SER ALA ASN ALA ILE ARG THR LEU SER LYS
SEQRES 6 U 72 GLY PRO TYR LYS GLY ILE GLU
SEQRES 1 V 66 MET LYS PRO SER GLU MET ARG ASN LEU GLN ALA THR ASP
SEQRES 2 V 66 PHE ALA LYS GLU ILE ASP ALA ARG LYS LYS GLU LEU MET
SEQRES 3 V 66 GLU LEU ARG PHE GLN ALA ALA ALA GLY GLN LEU ALA GLN
SEQRES 4 V 66 PRO HIS ARG VAL ARG GLN LEU ARG ARG GLU VAL ALA GLN
SEQRES 5 V 66 LEU ASN THR VAL LYS ALA GLU LEU ALA ARG LYS GLY GLU
SEQRES 6 V 66 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 57 LYS HIS PRO VAL PRO LYS LYS LYS THR SER LYS SER LYS
SEQRES 2 Z 57 ARG ASP MET ARG ARG SER HIS HIS ALA LEU THR ALA PRO
SEQRES 3 Z 57 ASN LEU THR GLU CYS PRO GLN CYS HIS GLY LYS LYS LEU
SEQRES 4 Z 57 SER HIS HIS ILE CYS PRO ASN CYS GLY TYR TYR ASP GLY
SEQRES 5 Z 57 ARG GLN VAL LEU ALA
SEQRES 1 1 54 ALA ALA ALA GLY ALA ALA PRO ARG ILE ILE VAL LYS MET
SEQRES 2 1 54 GLU SER SER ALA GLY THR GLY PHE TYR TYR THR THR THR
SEQRES 3 1 54 LYS ASN ARG ARG ASN THR GLN ALA LYS LEU GLU LEU LYS
SEQRES 4 1 54 LYS TYR ASP PRO VAL ALA ALA HIS VAL VAL PHE ALA ALA
SEQRES 5 1 54 ALA ALA
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 65 PRO LYS MET LYS THR HIS LYS MET ALA LYS ARG ARG ILE
SEQRES 2 3 65 LYS ILE THR GLY THR GLY LYS VAL MET ALA PHE LYS SER
SEQRES 3 3 65 GLY LYS ARG HIS GLN ASN THR GLY LYS SER GLY ASP GLU
SEQRES 4 3 65 ILE ARG GLY LYS GLY LYS GLY PHE VAL LEU ALA LYS ALA
SEQRES 5 3 65 GLU TRP ALA ARG MET LYS LEU MET LEU PRO ARG GLY LYS
SEQRES 1 X 2881 G G G U C A A G A U A G U
SEQRES 2 X 2881 A A G G G U C C A C G G U
SEQRES 3 X 2881 G G A U G C C C U G G C G
SEQRES 4 X 2881 C U G G A G C C G A U G A
SEQRES 5 X 2881 A G G A C G C G A U U A C
SEQRES 6 X 2881 C U G C G A A A A G C C C
SEQRES 7 X 2881 C G A C G A G C U G G A G
SEQRES 8 X 2881 A U A C G C U U U G A C U
SEQRES 9 X 2881 C G G G G A U G U C C G A
SEQRES 10 X 2881 A U G G G G A A A C C C A
SEQRES 11 X 2881 C C U C G U A A G A G G U
SEQRES 12 X 2881 A U C C G C A A G G A U G
SEQRES 13 X 2881 G G A A C U C A G G G A A
SEQRES 14 X 2881 C U G A A A C A U C U C A
SEQRES 15 X 2881 G U A C C U G A A G G A G
SEQRES 16 X 2881 A A G A A A G A G A A U U
SEQRES 17 X 2881 C G A U U C C G U U A G U
SEQRES 18 X 2881 A G C G G C G A G C G A A
SEQRES 19 X 2881 C C C G G A U C A G C C C
SEQRES 20 X 2881 A A A C C G A A A C G C U
SEQRES 21 X 2881 U G C G U U U C G G G G U
SEQRES 22 X 2881 U G U A G G A C C A G U U
SEQRES 23 X 2881 U U U A A G A U U C A A C
SEQRES 24 X 2881 C C C U C A A G C C G A A
SEQRES 25 X 2881 G U G G C U G G A A A G C
SEQRES 26 X 2881 U A C A C C U C A G A A G
SEQRES 27 X 2881 G U G A G A G U C C U G U
SEQRES 28 X 2881 A G G C G A A C G A G C G
SEQRES 29 X 2881 G U U G A C U G U A C U G
SEQRES 30 X 2881 G C A C C U G A G U A G G
SEQRES 31 X 2881 U C G U U G U U C G U G A
SEQRES 32 X 2881 A A C G A U G A C U G A A
SEQRES 33 X 2881 U C C G C G C G G A C C A
SEQRES 34 X 2881 C C G C G C A A G G C U A
SEQRES 35 X 2881 A A U A C U C C C A G U G
SEQRES 36 X 2881 A C C G A U A G C G C A U
SEQRES 37 X 2881 A G U A C C G U G A G G G
SEQRES 38 X 2881 A A A G G U G A A A A G A
SEQRES 39 X 2881 A C C C C G G G A G G G G
SEQRES 40 X 2881 A G U G A A A G A G A A C
SEQRES 41 X 2881 C U G A A A C C G U G G A
SEQRES 42 X 2881 C U U A C A A G C A G U C
SEQRES 43 X 2881 A U G G C A C C U U A U G
SEQRES 44 X 2881 C G U G U U A U G G C G U
SEQRES 45 X 2881 G C C U A U U G A A G C A
SEQRES 46 X 2881 U G A G C C G G C G A C U
SEQRES 47 X 2881 U A G A C C U G A C G U G
SEQRES 48 X 2881 C G A G C U U A A G U U G
SEQRES 49 X 2881 A A A A A C G G A G G C G
SEQRES 50 X 2881 G A G C G A A A G C G A G
SEQRES 51 X 2881 U C C G A A U A G G G C G
SEQRES 52 X 2881 G C A U U A G U A C G U C
SEQRES 53 X 2881 G G G C U A G A C U C G A
SEQRES 54 X 2881 A A C C A G G U G A G C U
SEQRES 55 X 2881 A A G C A U G A C C A G G
SEQRES 56 X 2881 U U G A A A C C C C C G U
SEQRES 57 X 2881 G A C A G G G G G C G G A
SEQRES 58 X 2881 G G A C C G A A C C G G U
SEQRES 59 X 2881 G C C U G C U G A A A C A
SEQRES 60 X 2881 G U C U C G G A U G A G U
SEQRES 61 X 2881 U G U G U U U A G G A G U
SEQRES 62 X 2881 G A A A A G C U A A C C G
SEQRES 63 X 2881 A A C C U G G A G A U A G
SEQRES 64 X 2881 C U A G U U C U C C C C G
SEQRES 65 X 2881 A A A U G U A U U G A G G
SEQRES 66 X 2881 U A C A G C C U C G G A U
SEQRES 67 X 2881 G U U G A C C A U G U C C
SEQRES 68 X 2881 U G U A G A G C A C U C A
SEQRES 69 X 2881 C A A G G C U A G G G G G
SEQRES 70 X 2881 C C U A C C A G C U U A C
SEQRES 71 X 2881 C A A A C C U U A U G A A
SEQRES 72 X 2881 A C U C C G A A G G G G C
SEQRES 73 X 2881 A C G C G U U U A G U C C
SEQRES 74 X 2881 G G G A G U G A G G C U G
SEQRES 75 X 2881 C G A G A G C U A A C U U
SEQRES 76 X 2881 C C G U A G C C G A G A G
SEQRES 77 X 2881 G G A A A C A A C C C A G
SEQRES 78 X 2881 A C C A U C A G C U A A G
SEQRES 79 X 2881 G U C C C U A A A U G A U
SEQRES 80 X 2881 C G C U C A G U G G U U A
SEQRES 81 X 2881 A G G A U G U G U C G U C
SEQRES 82 X 2881 G C A U A G A C A G C C A
SEQRES 83 X 2881 G G A G G U U G G C U U A
SEQRES 84 X 2881 G A A G C A G C C A C C C
SEQRES 85 X 2881 U U C A A A G A G U G C G
SEQRES 86 X 2881 U A A U A G C U C A C U G
SEQRES 87 X 2881 G U C G A G U G A C G A U
SEQRES 88 X 2881 G C G C C G A A A A U G A
SEQRES 89 X 2881 U C G G G G C U C A A G U
SEQRES 90 X 2881 G A U C U A C C G A A G C
SEQRES 91 X 2881 U A U G G A U U C A A C U
SEQRES 92 X 2881 C G C G A A G C G A G U U
SEQRES 93 X 2881 G U C U G G U A G G G G A
SEQRES 94 X 2881 G C G U U C A G U C C G C
SEQRES 95 X 2881 G G A G A A G C C A U A C
SEQRES 96 X 2881 C G G A A G G A G U G G U
SEQRES 97 X 2881 G G A G C C G A C U G A A
SEQRES 98 X 2881 G U G C G G A U G C C G G
SEQRES 99 X 2881 C A U G A G U A A C G A U
SEQRES 100 X 2881 A A A A G A A G U G A G A
SEQRES 101 X 2881 A U C U U C U U C G C C G
SEQRES 102 X 2881 U A A G G A C A A G G G U
SEQRES 103 X 2881 U C C U G G G G A A G G G
SEQRES 104 X 2881 U C G U C C G C C C A G G
SEQRES 105 X 2881 G A A A G U C G G G A C C
SEQRES 106 X 2881 U A A G G U G A G G C C G
SEQRES 107 X 2881 A A C G G C G C A G C C G
SEQRES 108 X 2881 A U G G A C A G C A G G U
SEQRES 109 X 2881 C A A G A U U C C U G C A
SEQRES 110 X 2881 C C G A U C A U G U G G A
SEQRES 111 X 2881 G U G A U G G A G G G A C
SEQRES 112 X 2881 G C A U U A C G C U A U C
SEQRES 113 X 2881 C A A U G C C A A G C U A
SEQRES 114 X 2881 U G G C U A U G C U G G U
SEQRES 115 X 2881 U G G U A C G C U C A A G
SEQRES 116 X 2881 G G C G A U C G G G U C A
SEQRES 117 X 2881 G A A A A U C U A C C G G
SEQRES 118 X 2881 U C A C A U G C C U C A G
SEQRES 119 X 2881 A C G U A U C G G G A G C
SEQRES 120 X 2881 U U C C U C G G A A G C G
SEQRES 121 X 2881 A A G U U G G A A A C G C
SEQRES 122 X 2881 G A C G G U G C C A A G A
SEQRES 123 X 2881 A A A G C U U C U A A A C
SEQRES 124 X 2881 G U U G A A A C A U G A U
SEQRES 125 X 2881 U G C C C G U A C C G C A
SEQRES 126 X 2881 A A C C G A C A C A G G U
SEQRES 127 X 2881 G U C C G A G U G U C A A
SEQRES 128 X 2881 U G C A C U A A G G C G C
SEQRES 129 X 2881 G C G A G A G A A C C C U
SEQRES 130 X 2881 C G U U A A G G A A C U U
SEQRES 131 X 2881 U G C A A U C U C A C C C
SEQRES 132 X 2881 C G U A A C U U C G G A A
SEQRES 133 X 2881 G A A G G G G U C C C C A
SEQRES 134 X 2881 C G C U U C G C G U G G G
SEQRES 135 X 2881 G C G C A G U G A A U A G
SEQRES 136 X 2881 G C C C A G G C G A C U G
SEQRES 137 X 2881 U U U A C C A A A A U C A
SEQRES 138 X 2881 C A G C A C U C U G C C A
SEQRES 139 X 2881 A C A C G A A C A G U G G
SEQRES 140 X 2881 A C G U A U A G G G U G U
SEQRES 141 X 2881 G A C G C C U G C C C G G
SEQRES 142 X 2881 U G C C G G A A G G U C A
SEQRES 143 X 2881 A G U G G A G C G G U G C
SEQRES 144 X 2881 A A G C U G C G A A A U G
SEQRES 145 X 2881 A A G C C C C G G U G A A
SEQRES 146 X 2881 C G G C G G C C G U A A C
SEQRES 147 X 2881 U A U A A C G G U C C U A
SEQRES 148 X 2881 A G G U A G C G A A A U U
SEQRES 149 X 2881 C C U U G U C G G G U A A
SEQRES 150 X 2881 G U U C C G A C C U G C A
SEQRES 151 X 2881 C G A A A G G C G U A A C
SEQRES 152 X 2881 G A U C U G G G C G C U G
SEQRES 153 X 2881 U C U C A A C G A G G G A
SEQRES 154 X 2881 C U C G G U G A A A U U G
SEQRES 155 X 2881 A A U U G G C U G U A A A
SEQRES 156 X 2881 G A U G C G G C C U A C C
SEQRES 157 X 2881 C G U A G C A G G A C G A
SEQRES 158 X 2881 A A A G A C C C C G U G G
SEQRES 159 X 2881 A G C U U U A C U A U A G
SEQRES 160 X 2881 U C U G G C A U U G G G A
SEQRES 161 X 2881 U U C G G G U U U C U C U
SEQRES 162 X 2881 G C G U A G G A U A G G U
SEQRES 163 X 2881 G G G A G C C U G C G A A
SEQRES 164 X 2881 A C U G G C C U U U U G G
SEQRES 165 X 2881 G G U C G G U G G A G G C
SEQRES 166 X 2881 A A C G G U G A A A U A C
SEQRES 167 X 2881 C A C C C U G A G A A A C
SEQRES 168 X 2881 U U G G A U U U C U A A C
SEQRES 169 X 2881 C U G A A A A A U C A C U
SEQRES 170 X 2881 U U C G G G G A C C G U G
SEQRES 171 X 2881 C U U G G C G G G U A G U
SEQRES 172 X 2881 U U G A C U G G G G C G G
SEQRES 173 X 2881 U C G C C U C C C A A A A
SEQRES 174 X 2881 U G U A A C G G A G G C G
SEQRES 175 X 2881 C C C A A A G G U C A C C
SEQRES 176 X 2881 U C A A G A C G G U U G G
SEQRES 177 X 2881 A A A U C G U C U G U A G
SEQRES 178 X 2881 A G C G C A A A G G U A G
SEQRES 179 X 2881 A A G G U G G C U U G A C
SEQRES 180 X 2881 U G C G A G A C U G A C A
SEQRES 181 X 2881 C G U C G A G C A G G G A
SEQRES 182 X 2881 G G A A A C U C G G G C U
SEQRES 183 X 2881 U A G U G A A C C G G U G
SEQRES 184 X 2881 G U A C C G U G U G G A A
SEQRES 185 X 2881 G G G C C A U C G A U C A
SEQRES 186 X 2881 A C G G A U A A A A G U U
SEQRES 187 X 2881 A C C C C G G G G A U A A
SEQRES 188 X 2881 C A G G C U G A U C U C C
SEQRES 189 X 2881 C C C G A G A G U C C A U
SEQRES 190 X 2881 A U C G G C G G G G A G G
SEQRES 191 X 2881 U U U G G C A C C U C G A
SEQRES 192 X 2881 U G U C G G C U C G U C G
SEQRES 193 X 2881 C A U C C U G G G G C U G
SEQRES 194 X 2881 A A G A A G G U C C C A A
SEQRES 195 X 2881 G G G U U G G G C U G U U
SEQRES 196 X 2881 C G C C C A U U A A A G C
SEQRES 197 X 2881 G G C A C G C G A G C U G
SEQRES 198 X 2881 G G U U C A G A A C G U C
SEQRES 199 X 2881 G U G A G A C A G U U C G
SEQRES 200 X 2881 G U C U C U A U C C G C U
SEQRES 201 X 2881 A C G G G C G C A G G A G
SEQRES 202 X 2881 A A U U G A G G G G A G U
SEQRES 203 X 2881 U G C U C C U A G U A C G
SEQRES 204 X 2881 A G A G G A C C G G A G U
SEQRES 205 X 2881 G A A C G G A C C G C U G
SEQRES 206 X 2881 G U C U C C C U G C U G U
SEQRES 207 X 2881 C G U A C C A A C G G C A
SEQRES 208 X 2881 C A U G C A G G G U A G C
SEQRES 209 X 2881 U A U G U C C G G A A C G
SEQRES 210 X 2881 G A U A A C C G C U G A A
SEQRES 211 X 2881 A G C A U C U A A G C G G
SEQRES 212 X 2881 G A A G C C A G C C C C A
SEQRES 213 X 2881 A G A U G A G U U C U C C
SEQRES 214 X 2881 C A C U G U U U A U C A G
SEQRES 215 X 2881 G U A A G A C U C C C G G
SEQRES 216 X 2881 A A G A C C A C C G G G U
SEQRES 217 X 2881 U A A G A G G C C A G G C
SEQRES 218 X 2881 G U G C A C G C A U A G C
SEQRES 219 X 2881 A A U G U G U U C A G C G
SEQRES 220 X 2881 G A C U G G U G C U C A U
SEQRES 221 X 2881 C A G U C G A G G U C U U
SEQRES 222 X 2881 G A C C A C U C
SEQRES 1 Y 122 C A C C C C C G U G C C C
SEQRES 2 Y 122 A U A G C A C U G U G G A
SEQRES 3 Y 122 A C C A C C C C A C C C C
SEQRES 4 Y 122 A U G C C G A A C U G G G
SEQRES 5 Y 122 U C G U G A A A C A C A G
SEQRES 6 Y 122 C A G C G C C A A U G A U
SEQRES 7 Y 122 A C U C G G A C C G C A G
SEQRES 8 Y 122 G G U C C C G G A A A A G
SEQRES 9 Y 122 U C G G U C A G C G C G G
SEQRES 10 Y 122 G G G U U
HET MG M 201 1
HET MG X6001 1
HET MG X6002 1
HET MG X6003 1
HET MG X6004 1
HET MG X6005 1
HET MG X6006 1
HET MG X6007 1
HET MG X6008 1
HET MG X6009 1
HET MG X6010 1
HET MG X6011 1
HET MG X6012 1
HET MG X6013 1
HET MG X6014 1
HET MG X6015 1
HET MG X6016 1
HET MG X6017 1
HET MG X6018 1
HET MG X6019 1
HET MG X6020 1
HET MG X6021 1
HET MG X6022 1
HET MG X6023 1
HET MG X6024 1
HET MG X6025 1
HET MG X6026 1
HET MG X6027 1
HET MG X6028 1
HET MG X6029 1
HET MG X6030 1
HET MG X6031 1
HET MG X6032 1
HET MG X6033 1
HET MG X6034 1
HET MG X6035 1
HET MG X6036 1
HET MG X6037 1
HET MG X6038 1
HET MG X6039 1
HET MG X6040 1
HET MG X6041 1
HET MG X6042 1
HET MG X6043 1
HET MG X6044 1
HET MG X6045 1
HET MG X6046 1
HET MG X6047 1
HET MG X6048 1
HET MG X6049 1
HET MG X6050 1
HET MG X6051 1
HET MG X6052 1
HET MG X6053 1
HET MG X6054 1
HET MG X6055 1
HET MG X6056 1
HET MG X6057 1
HET MG X6058 1
HET MG X6059 1
HET MG X6060 1
HET MG X6061 1
HET MG X6062 1
HET MG X6063 1
HET MG X6064 1
HET MG X6065 1
HET MG X6066 1
HET MG X6067 1
HET MG X6068 1
HET MG X6069 1
HET MG X6070 1
HET MG X6071 1
HET MG X6072 1
HET MG X6073 1
HET MG X6074 1
HET MG X6075 1
HET MG X6076 1
HET MG X6077 1
HET MG X6078 1
HET MG X6079 1
HET MG X6080 1
HET MG X6081 1
HET MG X6082 1
HET MG X6083 1
HET MG X6084 1
HET MG X6085 1
HET MG X6086 1
HET MG X6087 1
HET MG X6088 1
HET MG X6089 1
HET MG X6090 1
HET MG X6091 1
HET MG X6092 1
HET MG X6093 1
HET MG X6094 1
HET MG X6095 1
HET MG X6096 1
HET MG X6097 1
HET MG X6098 1
HET MG X6099 1
HET MG X6100 1
HET MG X6101 1
HET MG X6102 1
HET MG X6103 1
HET MG X6104 1
HET MG X6105 1
HET MG X6106 1
HET MG X6107 1
HET MG X6108 1
HET MG X6109 1
HET MG X6110 1
HET MG X6111 1
HET MG X6112 1
HET MG X6113 1
HET MG X6114 1
HET MG X6115 1
HET MG X6116 1
HET MG X6117 1
HET MG X6118 1
HET MG X6119 1
HET MG X6120 1
HET MG X6121 1
HET MG X6122 1
HET MG X6123 1
HET MG X6124 1
HET MG X6125 1
HET MG X6126 1
HET MG X6127 1
HET MG X6128 1
HET MG X6129 1
HET MG X6130 1
HET MG X6131 1
HET MG X6132 1
HET MG X6133 1
HET MG X6134 1
HET MG X6135 1
HET MG X6136 1
HET MG X6137 1
HET MG X6138 1
HET MG X6139 1
HET MG X6140 1
HET MG X6141 1
HET MG X6142 1
HET MG X6143 1
HET MG X6144 1
HET MG X6145 1
HET MG X6146 1
HET MG X6147 1
HET MG X6148 1
HET MG X6149 1
HET MG X6150 1
HET MG X6151 1
HET MG X6152 1
HET MG X6153 1
HET MG X6154 1
HET MG X6155 1
HET MG X6156 1
HET MG X6157 1
HET MG X6158 1
HET MG X6159 1
HET MG X6160 1
HET MG X6161 1
HET MG X6162 1
HET MG X6163 1
HET MG X6164 1
HET MG X6165 1
HET MG X6166 1
HET MG X6167 1
HET MG X6168 1
HET MG X6169 1
HET MG X6170 1
HET MG X6171 1
HET MG X6172 1
HET MG X6173 1
HET MG X6174 1
HET MG X6175 1
HET MG X6176 1
HET MG X6177 1
HET MG X6178 1
HET MG X6179 1
HET MG X6180 1
HET MG X6181 1
HET MG X6182 1
HET MG X6183 1
HET MG X6184 1
HET MG X6185 1
HET MG X6186 1
HET MG X6187 1
HET MG X6188 1
HET MG X6189 1
HET MG X6190 1
HET MG X6191 1
HET MG X6192 1
HET MG Y 201 1
HET MG Y 202 1
HET MG Y 203 1
HET MG Y 204 1
HET MG Y 205 1
HETNAM MG MAGNESIUM ION
FORMUL 31 MG 198(MG 2+)
HELIX 1 AA1 ASP 0 93 ILE 0 99 1 7
HELIX 2 AA2 MET 0 116 LYS 0 122 1 7
HELIX 3 AA3 LEU 0 127 GLY 0 131 5 5
HELIX 4 AA4 THR A 10 ARG A 14 5 5
HELIX 5 AA5 LYS A 68 SER A 73 5 6
HELIX 6 AA6 ALA A 199 ILE A 204 5 6
HELIX 7 AA7 LYS A 208 LEU A 215 1 8
HELIX 8 AA8 ARG A 222 MET A 226 5 5
HELIX 9 AA9 ASN A 227 HIS A 231 5 5
HELIX 10 AB1 LYS A 264 ARG A 268 5 5
HELIX 11 AB2 THR B 38 GLY B 43 1 6
HELIX 12 AB3 ALA B 55 VAL B 59 5 5
HELIX 13 AB4 ASN B 60 ALA B 70 1 11
HELIX 14 AB5 VAL B 91 PHE B 96 1 6
HELIX 15 AB6 GLY B 115 ASN B 121 1 7
HELIX 16 AB7 ASN C 23 SER C 37 1 15
HELIX 17 AB8 PRO C 96 GLU C 113 1 18
HELIX 18 AB9 LYS C 129 ASN C 140 1 12
HELIX 19 AC1 ASP C 154 ARG C 162 1 9
HELIX 20 AC2 ASN C 176 HIS C 183 1 8
HELIX 21 AC3 LEU D 4 GLY D 21 1 18
HELIX 22 AC4 ASP D 46 LEU D 62 1 17
HELIX 23 AC5 ARG D 92 GLY D 107 1 16
HELIX 24 AC6 THR D 142 VAL D 146 5 5
HELIX 25 AC7 THR D 162 MET D 173 1 12
HELIX 26 AC8 GLN E 59 SER E 80 1 22
HELIX 27 AC9 ASP E 137 VAL E 151 1 15
HELIX 28 AD1 ALA F 40 GLN F 44 5 5
HELIX 29 AD2 SER F 119 THR F 126 1 8
HELIX 30 AD3 PRO G 50 GLY G 64 1 15
HELIX 31 AD4 ASN G 84 VAL G 88 5 5
HELIX 32 AD5 LYS G 93 LYS G 98 1 6
HELIX 33 AD6 ALA G 115 HIS G 122 1 8
HELIX 34 AD7 PRO G 123 MET G 134 1 12
HELIX 35 AD8 GLY G 138 THR G 146 1 9
HELIX 36 AD9 HIS G 158 LYS G 162 5 5
HELIX 37 AE1 ARG H 116 ARG H 121 1 6
HELIX 38 AE2 PHE H 123 ALA H 130 1 8
HELIX 39 AE3 ARG I 55 LEU I 60 1 6
HELIX 40 AE4 LEU I 77 GLN I 81 1 5
HELIX 41 AE5 ASP I 91 LEU I 98 1 8
HELIX 42 AE6 SER I 126 ALA I 135 1 10
HELIX 43 AE7 SER J 45 ARG J 60 1 16
HELIX 44 AE8 THR J 111 LYS J 125 1 15
HELIX 45 AE9 ASN K 13 GLU K 31 1 19
HELIX 46 AF1 LEU K 38 LYS K 56 1 19
HELIX 47 AF2 ASP K 59 ILE K 70 1 12
HELIX 48 AF3 ASP K 72 GLU K 82 1 11
HELIX 49 AF4 GLU K 82 ALA K 88 1 7
HELIX 50 AF5 ARG L 9 THR L 19 1 11
HELIX 51 AF6 THR L 67 GLY L 83 1 17
HELIX 52 AF7 GLY L 98 GLY L 110 1 13
HELIX 53 AF8 ASN M 8 ASP M 19 1 12
HELIX 54 AF9 SER M 60 ARG M 63 5 4
HELIX 55 AG1 LEU M 104 ALA M 109 5 6
HELIX 56 AG2 ILE N 8 ALA N 21 1 14
HELIX 57 AG3 TRP N 25 LYS N 30 5 6
HELIX 58 AG4 GLN N 31 HIS N 72 1 42
HELIX 59 AG5 ASN N 75 ALA N 86 1 12
HELIX 60 AG6 ASN N 91 GLU N 102 1 12
HELIX 61 AG7 GLU N 102 GLN N 118 1 17
HELIX 62 AG8 GLY O 48 TYR O 54 1 7
HELIX 63 AG9 ASN P 10 VAL P 18 1 9
HELIX 64 AH1 SER P 34 ARG P 46 1 13
HELIX 65 AH2 VAL P 50 LEU P 57 1 8
HELIX 66 AH3 ARG P 58 ILE P 60 5 3
HELIX 67 AH4 ALA P 64 LEU P 80 1 17
HELIX 68 AH5 HIS Q 3 ILE Q 6 1 4
HELIX 69 AH6 SER Q 13 ARG Q 22 1 10
HELIX 70 AH7 THR Q 34 GLY Q 47 1 14
HELIX 71 AH8 ILE Q 88 GLY Q 93 1 6
HELIX 72 AH9 SER R 5 ASN R 11 5 7
HELIX 73 AI1 SER R 79 VAL R 81 5 3
HELIX 74 AI2 ARG S 36 SER S 47 1 12
HELIX 75 AI3 SER U 63 GLY U 73 1 11
HELIX 76 AI4 PRO V 3 ASN V 8 1 6
HELIX 77 AI5 GLN V 10 GLY V 35 1 26
HELIX 78 AI6 GLN V 39 GLY V 64 1 26
HELIX 79 AI7 PRO W 13 LEU W 23 1 11
HELIX 80 AI8 VAL W 40 VAL W 47 1 8
HELIX 81 AI9 SER Z 12 ARG Z 20 1 9
HELIX 82 AJ1 ASN 2 8 GLY 2 17 1 10
HELIX 83 AJ2 GLY 2 17 LYS 2 23 1 7
HELIX 84 AJ3 THR 2 24 GLY 2 38 1 15
HELIX 85 AJ4 THR 2 43 GLU 2 47 5 5
HELIX 86 AJ5 HIS 3 7 LYS 3 11 5 5
HELIX 87 AJ6 SER 3 37 GLY 3 45 1 9
HELIX 88 AJ7 GLU 3 54 LEU 3 62 1 9
SHEET 1 AA1 2 VAL A 3 LYS A 4 0
SHEET 2 AA1 2 THR A 18 ALA A 19 -1 O THR A 18 N LYS A 4
SHEET 1 AA2 2 THR A 34 LEU A 37 0
SHEET 2 AA2 2 ARG A 60 ARG A 63 -1 O TYR A 62 N GLU A 35
SHEET 1 AA3 4 LYS A 102 LEU A 106 0
SHEET 2 AA3 4 ILE A 92 TYR A 97 -1 N ALA A 93 O ILE A 105
SHEET 3 AA3 4 ASN A 76 GLU A 83 -1 N LYS A 78 O HIS A 96
SHEET 4 AA3 4 THR A 116 ASN A 118 -1 O VAL A 117 N ALA A 77
SHEET 1 AA4 4 ALA A 130 PRO A 132 0
SHEET 2 AA4 4 TYR A 190 ILE A 193 -1 O ALA A 191 N LEU A 131
SHEET 3 AA4 4 VAL A 141 HIS A 143 -1 N HIS A 143 O THR A 192
SHEET 4 AA4 4 VAL A 163 GLN A 164 -1 O VAL A 163 N VAL A 142
SHEET 1 AA5 4 GLY A 167 LYS A 168 0
SHEET 2 AA5 4 TYR A 172 ARG A 176 -1 O ILE A 174 N GLY A 167
SHEET 3 AA5 4 LEU A 182 HIS A 186 -1 O ARG A 183 N VAL A 175
SHEET 4 AA5 4 LEU A 270 THR A 272 -1 O VAL A 271 N LEU A 182
SHEET 1 AA6 7 GLY B 3 LYS B 16 0
SHEET 2 AA6 7 ARG B 19 LEU B 27 -1 O VAL B 25 N GLY B 10
SHEET 3 AA6 7 LEU B 181 LYS B 185 -1 O ILE B 182 N VAL B 26
SHEET 4 AA6 7 ARG B 164 ARG B 176 -1 N ARG B 176 O LEU B 181
SHEET 5 AA6 7 LYS B 101 THR B 107 -1 N ILE B 102 O LEU B 170
SHEET 6 AA6 7 GLY B 194 ARG B 199 -1 O VAL B 197 N THR B 105
SHEET 7 AA6 7 GLY B 3 LYS B 16 -1 N GLY B 6 O VAL B 196
SHEET 1 AA7 3 GLN B 35 LYS B 37 0
SHEET 2 AA7 3 ALA B 46 GLY B 50 -1 O GLN B 48 N GLN B 35
SHEET 3 AA7 3 LEU B 78 ARG B 82 -1 O ARG B 79 N ILE B 49
SHEET 1 AA8 2 GLY B 112 GLN B 114 0
SHEET 2 AA8 2 GLY B 158 MET B 160 -1 O GLY B 158 N GLN B 114
SHEET 1 AA9 4 LEU C 117 VAL C 120 0
SHEET 2 AA9 4 ARG C 185 ALA C 190 1 O ASP C 189 N VAL C 120
SHEET 3 AA9 4 VAL C 148 THR C 152 1 N LEU C 149 O VAL C 187
SHEET 4 AA9 4 VAL C 167 PRO C 171 1 O LEU C 170 N LEU C 150
SHEET 1 AB1 2 ILE D 31 GLU D 32 0
SHEET 2 AB1 2 VAL D 157 THR D 158 -1 O VAL D 157 N GLU D 32
SHEET 1 AB2 4 ILE D 66 LYS D 69 0
SHEET 2 AB2 4 PRO D 84 VAL D 89 -1 O LYS D 88 N ILE D 66
SHEET 3 AB2 4 VAL D 36 ASN D 37 -1 N VAL D 36 O VAL D 89
SHEET 4 AB2 4 ASP D 153 ILE D 154 -1 O ASP D 153 N ASN D 37
SHEET 1 AB3 2 VAL E 43 GLN E 45 0
SHEET 2 AB3 2 LEU E 50 VAL E 52 -1 O LEU E 51 N ARG E 44
SHEET 1 AB4 4 VAL E 121 ALA E 124 0
SHEET 2 AB4 4 ARG E 130 GLY E 135 -1 O SER E 134 N THR E 122
SHEET 3 AB4 4 TYR E 83 ARG E 90 -1 N TYR E 83 O GLY E 135
SHEET 4 AB4 4 GLY E 161 PHE E 164 -1 O ARG E 163 N GLU E 88
SHEET 1 AB5 3 LEU E 98 THR E 99 0
SHEET 2 AB5 3 ALA E 102 MET E 105 -1 O ALA E 102 N THR E 99
SHEET 3 AB5 3 VAL E 113 ILE E 115 -1 O ILE E 115 N LEU E 103
SHEET 1 AB6 3 GLY F 6 LYS F 9 0
SHEET 2 AB6 3 VAL F 55 ILE F 59 -1 O ILE F 59 N GLY F 6
SHEET 3 AB6 3 THR F 66 THR F 69 -1 O THR F 66 N THR F 58
SHEET 1 AB7 3 TRP G 41 ASP G 45 0
SHEET 2 AB7 3 PHE G 79 ILE G 83 1 O VAL G 81 N VAL G 44
SHEET 3 AB7 3 LEU G 148 VAL G 150 1 O LYS G 149 N VAL G 82
SHEET 1 AB8 2 VAL G 99 ARG G 102 0
SHEET 2 AB8 2 LYS G 111 THR G 114 -1 O LYS G 111 N ARG G 102
SHEET 1 AB9 6 ARG H 7 VAL H 10 0
SHEET 2 AB9 6 ALA H 16 ARG H 23 -1 O ILE H 19 N LEU H 8
SHEET 3 AB9 6 ILE H 50 ALA H 58 -1 O LYS H 56 N GLU H 18
SHEET 4 AB9 6 ALA H 72 ARG H 76 -1 O ALA H 72 N ILE H 51
SHEET 5 AB9 6 ALA H 95 ILE H 98 -1 O ALA H 95 N ARG H 76
SHEET 6 AB9 6 ARG H 7 VAL H 10 1 N ASP H 9 O ALA H 96
SHEET 1 AC1 7 ILE H 81 LYS H 82 0
SHEET 2 AC1 7 THR H 88 PHE H 91 -1 O ILE H 89 N ILE H 81
SHEET 3 AC1 7 GLU M 75 PRO M 82 -1 O GLU M 78 N ARG H 90
SHEET 4 AC1 7 SER M 65 SER M 72 -1 N LYS M 70 O VAL M 77
SHEET 5 AC1 7 THR M 45 ASN M 58 -1 N ILE M 55 O THR M 67
SHEET 6 AC1 7 THR M 32 ARG M 40 -1 N VAL M 35 O PHE M 50
SHEET 7 AC1 7 VAL M 88 GLU M 95 -1 O GLN M 90 N ASP M 36
SHEET 1 AC2 3 GLU I 73 LYS I 76 0
SHEET 2 AC2 3 VAL I 106 LEU I 109 1 O LYS I 107 N GLU I 73
SHEET 3 AC2 3 ALA I 124 ALA I 125 1 O ALA I 124 N LEU I 108
SHEET 1 AC3 2 VAL I 120 HIS I 121 0
SHEET 2 AC3 2 VAL I 140 VAL I 141 1 O VAL I 141 N VAL I 120
SHEET 1 AC4 4 LYS J 64 ILE J 67 0
SHEET 2 AC4 4 VAL J 103 ALA J 108 -1 O GLU J 106 N TYR J 66
SHEET 3 AC4 4 TYR J 33 ALA J 37 -1 N TYR J 33 O VAL J 107
SHEET 4 AC4 4 THR J 130 VAL J 133 -1 O LYS J 131 N ILE J 36
SHEET 1 AC5 3 ILE J 43 LYS J 44 0
SHEET 2 AC5 3 TYR J 93 SER J 96 -1 O SER J 96 N ILE J 43
SHEET 3 AC5 3 LYS J 73 VAL J 75 -1 N LYS J 73 O VAL J 95
SHEET 1 AC6 3 ARG K 33 THR K 37 0
SHEET 2 AC6 3 THR K 109 GLU K 114 -1 O ALA K 111 N THR K 36
SHEET 3 AC6 3 ARG K 96 THR K 102 -1 N LEU K 98 O LEU K 112
SHEET 1 AC7 4 GLN L 49 THR L 50 0
SHEET 2 AC7 4 ILE L 42 ASP L 44 -1 N ASP L 44 O GLN L 49
SHEET 3 AC7 4 ARG L 28 LEU L 29 -1 N ARG L 28 O ILE L 43
SHEET 4 AC7 4 VAL L 88 PHE L 89 1 O VAL L 88 N LEU L 29
SHEET 1 AC8 2 GLN O 6 THR O 7 0
SHEET 2 AC8 2 LYS O 10 GLN O 11 -1 O LYS O 10 N THR O 7
SHEET 1 AC9 4 ARG O 21 GLU O 23 0
SHEET 2 AC9 4 ASN O 89 ILE O 95 -1 O THR O 91 N VAL O 22
SHEET 3 AC9 4 THR O 55 ARG O 65 -1 N VAL O 61 O ALA O 92
SHEET 4 AC9 4 LYS O 32 LYS O 36 -1 N VAL O 33 O ALA O 58
SHEET 1 AD1 2 ILE O 69 LYS O 75 0
SHEET 2 AD1 2 TYR O 80 HIS O 86 -1 O THR O 84 N ILE O 71
SHEET 1 AD2 3 PHE P 25 VAL P 31 0
SHEET 2 AD2 3 SER P 122 GLU P 130 -1 O SER P 122 N VAL P 31
SHEET 3 AD2 3 LEU P 90 ALA P 99 -1 N ASP P 98 O HIS P 123
SHEET 1 AD3 2 LEU P 103 PRO P 108 0
SHEET 2 AD3 2 ALA P 114 LYS P 119 -1 O ILE P 117 N ARG P 105
SHEET 1 AD4 4 LEU Q 7 PRO Q 10 0
SHEET 2 AD4 4 VAL Q 24 VAL Q 29 -1 O TRP Q 28 N ALA Q 9
SHEET 3 AD4 4 ARG Q 75 LEU Q 82 -1 O VAL Q 80 N TYR Q 25
SHEET 4 AD4 4 VAL Q 50 VAL Q 58 -1 N SER Q 54 O ILE Q 79
SHEET 1 AD5 2 ARG Q 62 VAL Q 65 0
SHEET 2 AD5 2 PHE Q 68 GLN Q 71 -1 O GLY Q 70 N LYS Q 63
SHEET 1 AD6 4 THR R 21 ILE R 23 0
SHEET 2 AD6 4 THR R 33 LEU R 40 -1 O GLY R 34 N VAL R 22
SHEET 3 AD6 4 LYS R 45 VAL R 48 -1 O VAL R 47 N LEU R 38
SHEET 4 AD6 4 LEU R 76 HIS R 77 -1 O LEU R 76 N VAL R 46
SHEET 1 AD7 2 VAL R 53 LYS R 56 0
SHEET 2 AD7 2 GLN R 69 ARG R 72 -1 O ARG R 72 N VAL R 53
SHEET 1 AD8 2 ARG R 95 VAL R 99 0
SHEET 2 AD8 2 LYS R 103 ALA R 107 -1 O ARG R 105 N GLN R 97
SHEET 1 AD9 5 ASN S 29 ASP S 35 0
SHEET 2 AD9 5 MET S 18 TYR S 24 -1 N ALA S 23 O VAL S 30
SHEET 3 AD9 5 ALA S 77 MET S 85 1 O PHE S 83 N VAL S 22
SHEET 4 AD9 5 THR S 61 ASP S 72 -1 N LEU S 65 O TYR S 84
SHEET 5 AD9 5 PHE S 52 THR S 55 -1 N ILE S 54 O PHE S 62
SHEET 1 AE1 3 VAL S 94 PRO S 97 0
SHEET 2 AE1 3 ASN S 119 VAL S 123 -1 O ILE S 122 N VAL S 94
SHEET 3 AE1 3 THR S 159 LEU S 160 -1 O THR S 159 N VAL S 123
SHEET 1 AE2 2 LEU S 112 ASP S 114 0
SHEET 2 AE2 2 SER S 170 LEU S 172 -1 O SER S 170 N ASP S 114
SHEET 1 AE3 2 ILE S 147 THR S 148 0
SHEET 2 AE3 2 THR S 167 VAL S 168 -1 O VAL S 168 N ILE S 147
SHEET 1 AE4 4 GLY T 22 VAL T 23 0
SHEET 2 AE4 4 ILE T 36 ARG T 39 -1 O ARG T 39 N GLY T 22
SHEET 3 AE4 4 LEU T 59 ALA T 61 -1 O LEU T 59 N LEU T 37
SHEET 4 AE4 4 VAL T 51 MET T 53 -1 N GLY T 52 O PHE T 60
SHEET 1 AE5 3 LYS T 46 ALA T 47 0
SHEET 2 AE5 3 ARG T 77 GLU T 82 1 O ARG T 77 N LYS T 46
SHEET 3 AE5 3 LYS T 66 ASN T 71 -1 N ILE T 70 O PHE T 78
SHEET 1 AE6 3 SER W 31 GLU W 33 0
SHEET 2 AE6 3 LYS W 2 LEU W 5 -1 N ILE W 3 O ARG W 32
SHEET 3 AE6 3 LEU W 51 VAL W 53 -1 O GLU W 52 N LYS W 4
SHEET 1 AE7 2 THR Z 31 GLU Z 32 0
SHEET 2 AE7 2 LYS Z 39 LYS Z 40 -1 O LYS Z 40 N THR Z 31
SHEET 1 AE8 4 TYR 1 21 LYS 1 26 0
SHEET 2 AE8 4 ILE 1 8 SER 1 14 -1 N VAL 1 10 O THR 1 24
SHEET 3 AE8 4 PHE 1 49 ALA 1 52 -1 O ALA 1 50 N GLU 1 13
SHEET 4 AE8 4 GLU 1 36 LEU 1 37 -1 N LEU 1 37 O PHE 1 49
SHEET 1 AE9 3 LYS 3 15 ILE 3 16 0
SHEET 2 AE9 3 VAL 3 22 ALA 3 24 -1 O MET 3 23 N LYS 3 15
SHEET 3 AE9 3 PHE 3 48 VAL 3 49 -1 O PHE 3 48 N ALA 3 24
SSBOND 1 CYS Z 33 CYS Z 46 1555 1555 2.06
SSBOND 2 CYS Z 36 CYS Z 49 1555 1555 2.06
LINK O GLY B 110 MG MG X6051 1555 1555 2.62
LINK OP2 A X 14 MG MG X6037 1555 1555 1.75
LINK OP2 G X 15 MG MG X6037 1555 1555 2.47
LINK OP1 C X 31 MG MG X6168 1555 1555 2.32
LINK OP1 A X 72 MG MG X6148 1555 1555 2.04
LINK OP2 U X 120 MG MG X6125 1555 1555 2.28
LINK OP1 C X 165F MG MG X6058 1555 1555 2.02
LINK OP1 A X 169 MG MG X6109 1555 1555 1.95
LINK OP2 C X 170 MG MG X6109 1555 1555 2.08
LINK OP1 C X 221 MG MG X6072 1555 1555 1.85
LINK O4 U X 380 MG MG X6108 1555 1555 2.40
LINK OP2 G X 382 MG MG X6139 1555 1555 1.89
LINK OP1 G X 386 MG MG X6139 1555 1555 2.49
LINK OP2 G X 393 MG MG X6137 1555 1555 1.90
LINK O6 G X 450 MG MG X6014 1555 1555 1.98
LINK OP1 C X 453 MG MG X6014 1555 1555 2.04
LINK OP1 A X 526 MG MG X6089 1555 1555 1.86
LINK OP1 C X 527 MG MG X6089 1555 1555 2.09
LINK O2 C X 527 MG MG X6111 1555 1555 2.11
LINK O6 G X 530 MG MG X6065 1555 1555 2.02
LINK OP2 C X 531 MG MG X6021 1555 1555 2.93
LINK OP2 G X 563 MG MG X6045 1555 1555 2.14
LINK OP1 A X 567 MG MG X6013 1555 1555 2.02
LINK O4 U X 568 MG MG X6117 1555 1555 2.28
LINK O6 G X 570 MG MG X6035 1555 1555 2.33
LINK OP1 C X 574 MG MG X6101 1555 1555 2.11
LINK OP2 C X 574 MG MG X6040 1555 1555 2.19
LINK OP1 U X 576 MG MG X6016 1555 1555 2.07
LINK OP2 C X 671 MG MG X6121 1555 1555 2.38
LINK OP2 A X 730 MG MG X6084 1555 1555 2.28
LINK OP2 C X 731 MG MG X6084 1555 1555 1.79
LINK OP1 G X 739 MG MG X6149 1555 1555 2.16
LINK OP2 U X 740 MG MG X6041 1555 1555 1.83
LINK OP1 A X 751 MG MG X6004 1555 1555 1.92
LINK OP1 A X 761 MG MG X6084 1555 1555 2.10
LINK OP2 A X 783 MG MG X6054 1555 1555 1.87
LINK OP1 A X 784 MG MG X6059 1555 1555 2.01
LINK OP2 A X 784 MG MG X6054 1555 1555 2.99
LINK OP2 G X 785 MG MG X6069 1555 1555 2.13
LINK OP1 U X 787 MG MG X6011 1555 1555 2.36
LINK OP2 C X 790 MG MG X6011 1555 1555 2.07
LINK OP1 A X 800 MG MG X6064 1555 1555 2.03
LINK OP1 A X 802 MG MG X6093 1555 1555 2.22
LINK OP1 U X 810 MG MG X6024 1555 1555 1.87
LINK OP2 G X 818 MG MG X6166 1555 1555 2.42
LINK OP1 G X 823 MG MG X6075 1555 1555 2.27
LINK OP2 G X 848 MG MG X6090 1555 1555 2.41
LINK OP2 G X 862 MG MG X6116 1555 1555 2.16
LINK O3' G X 944 MG MG X6094 1555 1555 2.94
LINK OP1 A X 945 MG MG X6060 1555 1555 1.81
LINK OP2 A X 945 MG MG X6094 1555 1555 1.89
LINK OP1 G X 946 MG MG X6094 1555 1555 2.64
LINK OP2 G X 946 MG MG X6094 1555 1555 2.91
LINK OP1 C X 948 MG MG X6028 1555 1555 2.58
LINK OP1 U X 962 MG MG X6028 1555 1555 1.92
LINK OP1 U X 963 MG MG X6114 1555 1555 1.91
LINK OP2 U X 963 MG MG X6028 1555 1555 1.90
LINK OP2 A X 973 MG MG X6117 1555 1555 1.88
LINK OP2 A X 975 MG MG X6134 1555 1555 1.71
LINK OP1 A X 981 MG MG X6129 1555 1555 1.76
LINK OP2 A X 990 MG MG X6026 1555 1555 2.00
LINK OP2 C X 991 MG MG X6026 1555 1555 2.33
LINK OP2 A X1009 MG MG X6070 1555 1555 2.28
LINK OP2 A X1010 MG MG X6070 1555 1555 2.00
LINK OP2 A X1156 MG MG X6039 1555 1555 2.60
LINK OP2 G X1186 MG MG X6026 1555 1555 1.76
LINK OP2 G X1187 MG MG X6185 1555 1555 1.82
LINK O6 G X1187 MG MG X6166 1555 1555 2.28
LINK OP1 C X1239 MG MG X6168 1555 1555 2.93
LINK OP1 G X1253 MG MG X6135 1555 1555 2.72
LINK OP2 A X1265 MG MG X6015 1555 1555 2.62
LINK OP1 U X1267 MG MG X6047 1555 1555 1.89
LINK OP1 A X1268 MG MG X6018 1555 1555 2.03
LINK OP2 A X1269 MG MG X6029 1555 1555 2.12
LINK OP2 G X1271 MG MG X6002 1555 1555 1.91
LINK OP1 A X1272 MG MG X6002 1555 1555 2.58
LINK OP2 C X1298 MG MG X6062 1555 1555 2.15
LINK OP2 G X1303 MG MG X6144 1555 1555 2.70
LINK OP1 C X1314 MG MG X6102 1555 1555 2.34
LINK OP2 C X1315 MG MG X6102 1555 1555 2.75
LINK OP2 C X1327 MG MG X6003 1555 1555 2.08
LINK OP1 G X1332 MG MG X6102 1555 1555 1.71
LINK OP2 C X1335 MG MG X6115 1555 1555 2.28
LINK OP2 A X1342 MG MG X6155 1555 1555 1.92
LINK OP1 C X1345 MG MG X6127 1555 1555 2.12
LINK OP2 G X1347 MG MG X6113 1555 1555 2.25
LINK OP1 U X1352 MG MG X6123 1555 1555 1.76
LINK O2' A X1378 MG MG X6103 1555 1555 2.05
LINK OP2 U X1379 MG MG X6103 1555 1555 2.04
LINK OP2 G X1380 MG MG X6103 1555 1555 2.38
LINK OP2 A X1439 MG MG X6181 1555 1555 1.99
LINK O4 U X1440 MG MG X6181 1555 1555 2.03
LINK OP2 U X1444 MG MG X6085 1555 1555 2.25
LINK OP2 G X1455 MG MG X6032 1555 1555 2.00
LINK OP2 G X1456 MG MG X6032 1555 1555 2.15
LINK OP1 U X1602 MG MG X6153 1555 1555 2.28
LINK O4 U X1602 MG MG X6155 1555 1555 2.33
LINK OP1 A X1603 MG MG X6079 1555 1555 2.01
LINK OP2 C X1604 MG MG X6079 1555 1555 1.74
LINK OP1 A X1614 MG MG X6004 1555 1555 2.10
LINK OP1 A X1626 MG MG X6052 1555 1555 2.12
LINK OP2 C X1636 MG MG X6112 1555 1555 2.27
LINK OP1 U X1639 MG MG X6099 1555 1555 2.29
LINK OP2 U X1639 MG MG X6062 1555 1555 2.34
LINK OP1 G X1647 MG MG X6002 1555 1555 2.00
LINK OP2 G X1647 MG MG X6031 1555 1555 1.95
LINK OP1 C X1648 MG MG X6002 1555 1555 2.27
LINK OP1 A X1664 MG MG X6009 1555 1555 2.78
LINK OP2 A X1664 MG MG X6001 1555 1555 2.10
LINK OP2 A X1665 MG MG X6009 1555 1555 2.29
LINK OP2 A X1669 MG MG X6022 1555 1555 2.58
LINK O4 U X1671 MG MG X6022 1555 1555 2.73
LINK OP2 A X1676 MG MG X6053 1555 1555 2.39
LINK OP1 C X1774 MG MG X6057 1555 1555 2.09
LINK OP2 G X1776 MG MG X6049 1555 1555 2.10
LINK OP1 A X1780 MG MG X6025 1555 1555 1.87
LINK OP1 C X1782 MG MG X6025 1555 1555 2.20
LINK OP1 A X1783 MG MG X6041 1555 1555 2.46
LINK OP2 A X1783 MG MG X6025 1555 1555 2.10
LINK OP1 A X1784 MG MG X6041 1555 1555 2.70
LINK OP2 A X1784 MG MG X6041 1555 1555 2.88
LINK OP1 G X1828 MG MG X6140 1555 1555 2.08
LINK OP2 A X1890 MG MG X6163 1555 1555 1.91
LINK OP2 A X1997 MG MG X6006 1555 1555 1.88
LINK OP1 A X2005 MG MG X6029 1555 1555 1.92
LINK OP1 C X2006 MG MG X6018 1555 1555 2.09
LINK OP1 U X2017 MG MG X6061 1555 1555 2.32
LINK OP1 U X2022 MG MG X6065 1555 1555 1.99
LINK OP2 C X2025 MG MG X6034 1555 1555 2.13
LINK OP2 U X2028 MG MG X6119 1555 1555 2.86
LINK OP1 G X2035 MG MG X6019 1555 1555 2.50
LINK OP2 G X2035 MG MG X6019 1555 1555 2.95
LINK OP1 C X2036 MG MG X6021 1555 1555 2.17
LINK OP1 A X2042 MG MG X6088 1555 1555 2.05
LINK OP2 G X2056 MG MG X6017 1555 1555 1.96
LINK OP2 A X2057 MG MG X6017 1555 1555 2.51
LINK OP2 G X2061 MG MG X6008 1555 1555 2.20
LINK OP1 A X2062 MG MG X6038 1555 1555 2.30
LINK OP1 U X2074 MG MG X6023 1555 1555 1.92
LINK O4 U X2084 MG MG X6186 1555 1555 2.11
LINK OP1 U X2243 MG MG X6058 1555 1555 2.58
LINK OP2 C X2248 MG MG X6151 1555 1555 2.25
LINK O4 U X2249 MG MG X6151 1555 1555 1.72
LINK OP1 A X2268 MG MG X6076 1555 1555 2.19
LINK OP1 A X2269 MG MG X6076 1555 1555 2.46
LINK OP1 C X2427 MG MG X6092 1555 1555 2.36
LINK OP1 G X2428 MG MG X6092 1555 1555 2.24
LINK OP2 U X2431 MG MG X6077 1555 1555 2.22
LINK OP2 A X2432 MG MG X6077 1555 1555 1.92
LINK OP1 A X2448 MG MG X6035 1555 1555 2.85
LINK OP2 A X2448 MG MG X6071 1555 1555 2.94
LINK OP1 C X2452 MG MG X6081 1555 1555 2.22
LINK OP2 C X2461 MG MG X6145 1555 1555 2.43
LINK OP2 A X2471 MG MG X6110 1555 1555 2.36
LINK OP1 U X2492 MG MG X6169 1555 1555 2.01
LINK OP2 C X2498 MG MG X6071 1555 1555 2.24
LINK OP1 C X2499 MG MG X6035 1555 1555 2.32
LINK OP2 C X2499 MG MG X6071 1555 1555 2.74
LINK OP2 G X2502 MG MG X6008 1555 1555 2.17
LINK OP1 A X2503 MG MG X6016 1555 1555 2.13
LINK OP1 G X2550 MG MG X6022 1555 1555 2.82
LINK OP1 C X2573 MG MG X6020 1555 1555 2.29
LINK OP1 G X2574 MG MG X6020 1555 1555 1.94
LINK OP2 C X2575 MG MG X6020 1555 1555 2.16
LINK OP1 G X2576 MG MG X6012 1555 1555 1.94
LINK OP1 A X2577 MG MG X6012 1555 1555 1.83
LINK OP2 G X2582 MG MG X6050 1555 1555 2.00
LINK OP2 G X2583 MG MG X6050 1555 1555 2.13
LINK OP1 G X2588 MG MG X6059 1555 1555 1.85
LINK OP2 G X2588 MG MG X6073 1555 1555 2.17
LINK OP1 A X2589 MG MG X6054 1555 1555 1.82
LINK OP1 A X2598 MG MG X6078 1555 1555 1.96
LINK OP1 U X2615 MG MG X6015 1555 1555 1.84
LINK OP2 U X2615 MG MG X6048 1555 1555 2.59
LINK OP2 C X2616 MG MG X6048 1555 1555 2.39
LINK OP2 A X2639 MG MG X6046 1555 1555 2.38
LINK OP2 G X2643 MG MG X6160 1555 1555 2.30
LINK OP2 G X2655 MG MG X6157 1555 1555 2.58
LINK OP2 G X2682 MG MG X6042 1555 1555 2.14
LINK OP2 A X2705 MG MG X6067 1555 1555 2.18
LINK OP1 A X2711 MG MG X6044 1555 1555 2.16
LINK OP2 A X2711 MG MG X6007 1555 1555 2.18
LINK OP1 A X2712A MG MG X6044 1555 1555 1.79
LINK OP2 A X2712A MG MG X6007 1555 1555 1.93
LINK OP2 G X2714 MG MG X6007 1555 1555 1.96
LINK OP1 A X2721 MG MG X6042 1555 1555 2.27
LINK OP2 A X2821 MG MG X6051 1555 1555 1.72
LINK OP2 G X2822 MG MG X6051 1555 1555 2.40
LINK OP2 A Y 101 MG MG Y 202 1555 1555 2.35
CISPEP 1 GLY 0 215 PRO 0 216 0 -4.20
CISPEP 2 THR B 146 PRO B 147 0 3.08
CISPEP 3 LEU C 19 PRO C 20 0 -11.04
CISPEP 4 GLY C 114 GLY C 115 0 -4.64
CISPEP 5 ILE C 188 ASP C 189 0 -12.03
CISPEP 6 GLY G 92 LYS G 93 0 -2.86
CISPEP 7 GLY I 24 GLY I 25 0 0.88
CISPEP 8 LYS I 45 GLY I 46 0 -4.28
CISPEP 9 GLY J 24 GLY J 25 0 2.85
CISPEP 10 ARG J 61 GLY J 62 0 -3.80
CISPEP 11 MET R 62 THR R 63 0 3.22
CISPEP 12 ASP R 100 GLY R 101 0 17.57
CISPEP 13 GLY R 111 LYS R 112 0 9.47
CISPEP 14 GLY T 6 VAL T 7 0 -12.86
CISPEP 15 SER U 17 VAL U 18 0 24.27
CISPEP 16 GLY V 35 GLN V 36 0 0.12
CISPEP 17 GLY 3 35 LYS 3 36 0 -6.99
CISPEP 18 LYS 3 36 SER 3 37 0 -11.04
SITE 1 AC1 1 ASN M 58
SITE 1 AC2 1 A X1664
SITE 1 AC3 4 G X1271 A X1272 G X1647 C X1648
SITE 1 AC4 1 C X1327
SITE 1 AC5 3 A X 750 A X 751 A X1614
SITE 1 AC6 2 C X1996 A X1997
SITE 1 AC7 4 A X2711 C X2712 A X2712A G X2714
SITE 1 AC8 3 G X2061 C X2501 G X2502
SITE 1 AC9 2 A X1664 A X1665
SITE 1 AD1 2 U X 787 C X 790
SITE 1 AD2 2 G X2576 A X2577
SITE 1 AD3 1 A X 567
SITE 1 AD4 2 G X 450 C X 453
SITE 1 AD5 2 A X1265 U X2615
SITE 1 AD6 2 U X 576 A X2503
SITE 1 AD7 2 G X2056 A X2057
SITE 1 AD8 3 U X1267 A X1268 C X2006
SITE 1 AD9 1 G X2035
SITE 1 AE1 3 C X2573 G X2574 C X2575
SITE 1 AE2 2 C X 531 C X2036
SITE 1 AE3 4 A X1669 C X1670 U X1671 G X2550
SITE 1 AE4 1 U X2074
SITE 1 AE5 2 U X 810 G X1253
SITE 1 AE6 3 A X1780 C X1782 A X1783
SITE 1 AE7 3 A X 990 C X 991 G X1186
SITE 1 AE8 3 C X 948 U X 962 U X 963
SITE 1 AE9 2 A X1269 A X2005
SITE 1 AF1 2 C X1646 G X1647
SITE 1 AF2 3 U X1454 G X1455 G X1456
SITE 1 AF3 1 A X2518
SITE 1 AF4 1 C X2025
SITE 1 AF5 3 G X 570 A X2448 C X2499
SITE 1 AF6 2 A X 14 G X 15
SITE 1 AF7 1 A X2062
SITE 1 AF8 1 A X1156
SITE 1 AF9 1 C X 574
SITE 1 AG1 3 U X 740 A X1783 A X1784
SITE 1 AG2 2 G X2682 A X2721
SITE 1 AG3 3 C X2710 A X2711 A X2712A
SITE 1 AG4 1 G X 563
SITE 1 AG5 2 A X2639 G X2640
SITE 1 AG6 1 U X1267
SITE 1 AG7 2 U X2615 C X2616
SITE 1 AG8 1 G X1776
SITE 1 AG9 4 G X2581 G X2582 G X2583 U X2584
SITE 1 AH1 4 GLY B 110 A X2820 A X2821 G X2822
SITE 1 AH2 1 A X1626
SITE 1 AH3 1 A X1676
SITE 1 AH4 3 A X 783 A X 784 A X2589
SITE 1 AH5 1 C X1774
SITE 1 AH6 3 C X 165F U X 165G U X2243
SITE 1 AH7 2 A X 784 G X2588
SITE 1 AH8 1 A X 945
SITE 1 AH9 1 U X2017
SITE 1 AI1 2 C X1298 U X1639
SITE 1 AI2 1 A X 800
SITE 1 AI3 2 G X 530 U X2022
SITE 1 AI4 1 A X2705
SITE 1 AI5 2 G X 785 G X 792
SITE 1 AI6 2 A X1009 A X1010
SITE 1 AI7 5 G X2447 A X2448 A X2497 C X2498
SITE 2 AI7 5 C X2499
SITE 1 AI8 1 C X 221
SITE 1 AI9 1 G X2588
SITE 1 AJ1 2 U X 822 G X 823
SITE 1 AJ2 2 A X2268 A X2269
SITE 1 AJ3 2 U X2431 A X2432
SITE 1 AJ4 3 ALA A 242 G X2597 A X2598
SITE 1 AJ5 3 A X1395 A X1603 C X1604
SITE 1 AJ6 1 C X2452
SITE 1 AJ7 3 A X 730 C X 731 A X 761
SITE 1 AJ8 1 U X1444
SITE 1 AJ9 1 A X2042
SITE 1 AK1 2 A X 526 C X 527
SITE 1 AK2 1 G X 848
SITE 1 AK3 4 U X 826 C X2427 G X2428 G X2429
SITE 1 AK4 1 A X 802
SITE 1 AK5 3 G X 944 A X 945 G X 946
SITE 1 AK6 1 U X1639
SITE 1 AK7 1 A X1701
SITE 1 AK8 1 C X 574
SITE 1 AK9 3 C X1314 C X1315 G X1332
SITE 1 AL1 3 A X1378 U X1379 G X1380
SITE 1 AL2 1 U X 380
SITE 1 AL3 3 A X 167 A X 169 C X 170
SITE 1 AL4 1 A X2471
SITE 1 AL5 1 C X 527
SITE 1 AL6 1 C X1636
SITE 1 AL7 1 G X1347
SITE 1 AL8 1 U X 963
SITE 1 AL9 1 C X1335
SITE 1 AM1 1 G X 862
SITE 1 AM2 2 U X 568 A X 973
SITE 1 AM3 1 U X2028
SITE 1 AM4 2 A X 670 C X 671
SITE 1 AM5 1 U X1352
SITE 1 AM6 2 A X 119 U X 120
SITE 1 AM7 2 C X1345 G X1346
SITE 1 AM8 1 U X2546
SITE 1 AM9 1 A X 981
SITE 1 AN1 1 A X 975
SITE 1 AN2 1 G X1253
SITE 1 AN3 1 G X 393
SITE 1 AN4 2 G X 382 G X 386
SITE 1 AN5 1 G X1828
SITE 1 AN6 1 U X1183
SITE 1 AN7 1 G X1303
SITE 1 AN8 1 C X2461
SITE 1 AN9 1 A X 72
SITE 1 AO1 3 G X 738 G X 739 U X1779
SITE 1 AO2 1 G X2763
SITE 1 AO3 2 C X2248 U X2249
SITE 1 AO4 1 U X1602
SITE 1 AO5 2 A X1342 U X1602
SITE 1 AO6 1 G X1283
SITE 1 AO7 2 U X2653 G X2655
SITE 1 AO8 1 G X2643
SITE 1 AO9 1 A X 984
SITE 1 AP1 1 A X1890
SITE 1 AP2 1 A X1641
SITE 1 AP3 2 G X 818 G X1187
SITE 1 AP4 2 C X 31 C X1239
SITE 1 AP5 1 U X2492
SITE 1 AP6 1 G X 159
SITE 1 AP7 2 A X1001 G X1002
SITE 1 AP8 1 G X2624
SITE 1 AP9 1 A X 835
SITE 1 AQ1 2 A X1439 U X1440
SITE 1 AQ2 1 G X1187
SITE 1 AQ3 1 U X2084
SITE 1 AQ4 1 G X2255
SITE 1 AQ5 1 G X 80
SITE 1 AQ6 1 A Y 101
CRYST1 169.900 410.760 696.120 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 0.005886 0.000000 0.000000 0.00000
SCALE2 0.000000 0.002435 0.000000 0.00000
SCALE3 0.000000 0.000000 0.001437 0.00000
(ATOM LINES ARE NOT SHOWN.)
END