HEADER ISOMERASE/DNA 03-AUG-12 4GFH
TITLE TOPOISOMERASE II-DNA-AMPPNP COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA TOPOISOMERASE 2;
COMPND 3 CHAIN: A, F;
COMPND 4 FRAGMENT: UNP RESIDUES 1-1177;
COMPND 5 SYNONYM: DNA TOPOISOMERASE II;
COMPND 6 EC: 5.99.1.3;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: DNA (5'-D(P*CP*CP*TP*AP*CP*TP*GP*CP*TP*AP*C)-3');
COMPND 10 CHAIN: B, G;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: DNA (5'-D(*CP*GP*CP*GP*GP*TP*AP*GP*CP*AP*GP*TP*AP*GP*G)-
COMPND 14 3');
COMPND 15 CHAIN: C, H;
COMPND 16 ENGINEERED: YES;
COMPND 17 MOL_ID: 4;
COMPND 18 MOLECULE: DNA (5'-D(P*GP*GP*AP*TP*GP*AP*CP*GP*AP*TP*(TSP))-3');
COMPND 19 CHAIN: D, I;
COMPND 20 ENGINEERED: YES;
COMPND 21 MOL_ID: 5;
COMPND 22 MOLECULE: DNA (5'-D(*CP*GP*CP*GP*AP*AP*TP*CP*GP*TP*CP*AP*TP*CP*C)-
COMPND 23 3');
COMPND 24 CHAIN: E, J;
COMPND 25 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: TOP2, TOR3, YNL088W, N2244;
SOURCE 7 MOL_ID: 2;
SOURCE 8 SYNTHETIC: YES;
SOURCE 9 MOL_ID: 3;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 MOL_ID: 4;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 MOL_ID: 5;
SOURCE 14 SYNTHETIC: YES
KEYWDS TOPOISOMERASE, PROTEIN-DNA COMPLEX, DNA SUPERCOILING, DNA
KEYWDS 2 REPLICATION, ATP-BINDING, DNA-BINDING, ISOMERASE, NUCLEOTIDE-
KEYWDS 3 BINDING, NUCLEUS, PHOSPHOPROTEIN, ISOMERASE-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.H.SCHMIDT,N.OSHEROFF,J.M.BERGER
REVDAT 3 31-JUL-19 4GFH 1 LINK
REVDAT 2 12-DEC-12 4GFH 1 JRNL
REVDAT 1 03-OCT-12 4GFH 0
JRNL AUTH B.H.SCHMIDT,N.OSHEROFF,J.M.BERGER
JRNL TITL STRUCTURE OF A TOPOISOMERASE II-DNA-NUCLEOTIDE COMPLEX
JRNL TITL 2 REVEALS A NEW CONTROL MECHANISM FOR ATPASE ACTIVITY.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 19 1147 2012
JRNL REFN ISSN 1545-9993
JRNL PMID 23022727
JRNL DOI 10.1038/NSMB.2388
REMARK 2
REMARK 2 RESOLUTION. 4.41 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.3_928)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 4.41
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.2
REMARK 3 NUMBER OF REFLECTIONS : 28660
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.241
REMARK 3 R VALUE (WORKING SET) : 0.239
REMARK 3 FREE R VALUE : 0.275
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060
REMARK 3 FREE R VALUE TEST SET COUNT : 1450
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 46.9880 - 9.4729 0.88 2759 154 0.2074 0.2221
REMARK 3 2 9.4729 - 7.5289 0.91 2745 147 0.1806 0.2439
REMARK 3 3 7.5289 - 6.5801 0.90 2690 165 0.2231 0.2462
REMARK 3 4 6.5801 - 5.9798 0.91 2692 144 0.2672 0.3371
REMARK 3 5 5.9798 - 5.5519 0.92 2738 146 0.2719 0.3473
REMARK 3 6 5.5519 - 5.2251 0.92 2749 142 0.2655 0.3267
REMARK 3 7 5.2251 - 4.9637 0.93 2722 145 0.2817 0.3313
REMARK 3 8 4.9637 - 4.7478 0.92 2718 148 0.2966 0.3303
REMARK 3 9 4.7478 - 4.5652 0.93 2707 141 0.3309 0.3739
REMARK 3 10 4.5652 - 4.4080 0.90 2690 118 0.3696 0.4217
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.86
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 187.6
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.540
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.390
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.33840
REMARK 3 B22 (A**2) : 2.35700
REMARK 3 B33 (A**2) : 5.98150
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 20878
REMARK 3 ANGLE : 0.842 28615
REMARK 3 CHIRALITY : 0.054 3120
REMARK 3 PLANARITY : 0.004 3269
REMARK 3 DIHEDRAL : 15.794 8059
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 7:240)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8928 21.6191 75.5921
REMARK 3 T TENSOR
REMARK 3 T11: 1.7641 T22: 1.7827
REMARK 3 T33: 0.9982 T12: -0.1245
REMARK 3 T13: -0.1774 T23: 0.3129
REMARK 3 L TENSOR
REMARK 3 L11: 2.8733 L22: 3.1520
REMARK 3 L33: 0.4172 L12: 0.8298
REMARK 3 L13: -0.0291 L23: -0.7922
REMARK 3 S TENSOR
REMARK 3 S11: 0.2541 S12: -1.3744 S13: -0.3667
REMARK 3 S21: 0.9153 S22: -0.5053 S23: -0.2056
REMARK 3 S31: -0.4221 S32: 1.0766 S33: 0.1822
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 241:408)
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3123 11.2924 50.8516
REMARK 3 T TENSOR
REMARK 3 T11: 2.0154 T22: 1.4987
REMARK 3 T33: 2.0684 T12: -0.0320
REMARK 3 T13: 0.3627 T23: 0.1269
REMARK 3 L TENSOR
REMARK 3 L11: 5.3805 L22: 5.0389
REMARK 3 L33: 4.1616 L12: 2.7833
REMARK 3 L13: 0.9807 L23: 3.3343
REMARK 3 S TENSOR
REMARK 3 S11: 0.5210 S12: -0.2556 S13: -0.3124
REMARK 3 S21: 0.1966 S22: -0.7826 S23: 0.4485
REMARK 3 S31: -0.4555 S32: -0.2077 S33: 0.2520
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 421:690)
REMARK 3 ORIGIN FOR THE GROUP (A): -12.1061 29.1108 -6.0183
REMARK 3 T TENSOR
REMARK 3 T11: 1.8610 T22: 2.0648
REMARK 3 T33: 1.9909 T12: -0.1578
REMARK 3 T13: -0.3479 T23: 0.0753
REMARK 3 L TENSOR
REMARK 3 L11: 3.9640 L22: 3.0276
REMARK 3 L33: 4.5942 L12: 2.0425
REMARK 3 L13: 1.6497 L23: 3.0631
REMARK 3 S TENSOR
REMARK 3 S11: -0.2981 S12: 0.4302 S13: 0.1071
REMARK 3 S21: -1.0645 S22: 0.3945 S23: -0.0497
REMARK 3 S31: -0.8525 S32: 0.9176 S33: -0.0179
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 691:1177)
REMARK 3 ORIGIN FOR THE GROUP (A): -48.8160 43.0617 1.7940
REMARK 3 T TENSOR
REMARK 3 T11: 1.8767 T22: 1.5481
REMARK 3 T33: 1.7032 T12: 0.0013
REMARK 3 T13: -0.1657 T23: -0.1387
REMARK 3 L TENSOR
REMARK 3 L11: 2.5738 L22: 1.2800
REMARK 3 L33: 2.9543 L12: 0.5835
REMARK 3 L13: 1.4620 L23: 1.0643
REMARK 3 S TENSOR
REMARK 3 S11: 0.0752 S12: -0.4136 S13: 0.3022
REMARK 3 S21: 0.2244 S22: -0.4450 S23: -0.0783
REMARK 3 S31: 0.2275 S32: 0.0530 S33: 0.4366
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B OR CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8927 42.6891 15.0696
REMARK 3 T TENSOR
REMARK 3 T11: 1.5071 T22: 1.8246
REMARK 3 T33: 1.8533 T12: 0.1149
REMARK 3 T13: -0.2559 T23: -0.0352
REMARK 3 L TENSOR
REMARK 3 L11: 3.6253 L22: 2.7819
REMARK 3 L33: 8.5573 L12: 2.5867
REMARK 3 L13: 4.8104 L23: 1.9509
REMARK 3 S TENSOR
REMARK 3 S11: -0.7469 S12: 0.3157 S13: 1.2027
REMARK 3 S21: -0.6636 S22: -0.6568 S23: 0.5605
REMARK 3 S31: 1.0909 S32: 0.1744 S33: 1.1875
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN C OR CHAIN E
REMARK 3 ORIGIN FOR THE GROUP (A): -24.0294 39.2623 16.5929
REMARK 3 T TENSOR
REMARK 3 T11: 2.2195 T22: 1.4538
REMARK 3 T33: 1.5332 T12: -0.2351
REMARK 3 T13: 0.2208 T23: -0.1771
REMARK 3 L TENSOR
REMARK 3 L11: 3.1495 L22: 5.2606
REMARK 3 L33: 2.6468 L12: 1.2938
REMARK 3 L13: 0.2068 L23: -3.1138
REMARK 3 S TENSOR
REMARK 3 S11: 0.5665 S12: 1.1084 S13: -0.2482
REMARK 3 S21: 1.8434 S22: 0.2031 S23: 1.9687
REMARK 3 S31: 0.4121 S32: 0.7006 S33: -0.7186
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN G OR CHAIN I
REMARK 3 ORIGIN FOR THE GROUP (A): -27.1749 -0.2455 19.4257
REMARK 3 T TENSOR
REMARK 3 T11: 1.7557 T22: 2.2403
REMARK 3 T33: 1.2271 T12: -0.0889
REMARK 3 T13: -0.3417 T23: -0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 4.8443 L22: 2.8248
REMARK 3 L33: 6.2933 L12: -3.1276
REMARK 3 L13: 4.8930 L23: -4.2877
REMARK 3 S TENSOR
REMARK 3 S11: 1.1707 S12: -0.2296 S13: 1.2729
REMARK 3 S21: -0.4032 S22: -0.9658 S23: 0.6599
REMARK 3 S31: 1.0162 S32: 1.4999 S33: -0.0949
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN H OR CHAIN J
REMARK 3 ORIGIN FOR THE GROUP (A): -25.6914 3.1352 18.2475
REMARK 3 T TENSOR
REMARK 3 T11: 2.2679 T22: 1.8144
REMARK 3 T33: 2.3839 T12: 0.2553
REMARK 3 T13: -0.0896 T23: 0.2003
REMARK 3 L TENSOR
REMARK 3 L11: 1.5709 L22: 3.2143
REMARK 3 L33: 2.4254 L12: 2.1769
REMARK 3 L13: 0.0373 L23: 0.4973
REMARK 3 S TENSOR
REMARK 3 S11: -0.1550 S12: 0.1655 S13: 0.1724
REMARK 3 S21: -0.7971 S22: 0.3129 S23: 0.2052
REMARK 3 S31: -0.6133 S32: -1.0822 S33: 0.0798
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 7:240)
REMARK 3 ORIGIN FOR THE GROUP (A): 33.3002 20.8922 50.2072
REMARK 3 T TENSOR
REMARK 3 T11: 0.9798 T22: 1.7320
REMARK 3 T33: 1.8260 T12: -0.2805
REMARK 3 T13: -0.2282 T23: 0.0860
REMARK 3 L TENSOR
REMARK 3 L11: 1.1225 L22: 3.2783
REMARK 3 L33: 1.9274 L12: 0.7442
REMARK 3 L13: -0.2461 L23: -1.5894
REMARK 3 S TENSOR
REMARK 3 S11: 0.4277 S12: -1.1111 S13: -0.4625
REMARK 3 S21: -0.1922 S22: -0.6120 S23: -0.8802
REMARK 3 S31: -0.1167 S32: 1.1460 S33: 0.1912
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 241:404)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.2142 31.3462 37.1597
REMARK 3 T TENSOR
REMARK 3 T11: 2.2196 T22: 1.4077
REMARK 3 T33: 2.0061 T12: -0.1793
REMARK 3 T13: 0.3605 T23: 0.1841
REMARK 3 L TENSOR
REMARK 3 L11: 3.6033 L22: 5.0811
REMARK 3 L33: 5.1874 L12: -2.5959
REMARK 3 L13: 1.2034 L23: -1.6864
REMARK 3 S TENSOR
REMARK 3 S11: 0.1898 S12: -0.0651 S13: -0.4335
REMARK 3 S21: -0.3233 S22: -0.4895 S23: -0.6295
REMARK 3 S31: -0.7794 S32: 0.3228 S33: 0.5547
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 421:690)
REMARK 3 ORIGIN FOR THE GROUP (A): -48.2956 13.3477 30.1698
REMARK 3 T TENSOR
REMARK 3 T11: 2.3123 T22: 2.4316
REMARK 3 T33: 2.2724 T12: 0.0921
REMARK 3 T13: -0.3874 T23: 0.0786
REMARK 3 L TENSOR
REMARK 3 L11: 3.2841 L22: 1.4558
REMARK 3 L33: 3.3358 L12: -1.4438
REMARK 3 L13: 1.7621 L23: -1.9511
REMARK 3 S TENSOR
REMARK 3 S11: -0.1747 S12: -0.7443 S13: -0.5051
REMARK 3 S21: 0.6764 S22: 0.3885 S23: 0.7421
REMARK 3 S31: -0.1051 S32: -0.3267 S33: -0.2500
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN F AND (RESSEQ 691:1177)
REMARK 3 ORIGIN FOR THE GROUP (A): -40.4565 -0.5927 -6.5379
REMARK 3 T TENSOR
REMARK 3 T11: 1.5698 T22: 1.2787
REMARK 3 T33: 1.7945 T12: 0.0776
REMARK 3 T13: -0.1930 T23: -0.0476
REMARK 3 L TENSOR
REMARK 3 L11: 3.8392 L22: 1.2971
REMARK 3 L33: 3.2055 L12: -1.6381
REMARK 3 L13: 1.7119 L23: -0.5152
REMARK 3 S TENSOR
REMARK 3 S11: 0.4004 S12: -0.0983 S13: 0.3988
REMARK 3 S21: -0.0479 S22: -0.3988 S23: -0.4245
REMARK 3 S31: 0.2191 S32: 0.3838 S33: 0.0293
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 4GFH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074116.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1159
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28660
REMARK 200 RESOLUTION RANGE HIGH (A) : 4.408
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.41
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.57
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.70300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 69.18
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% PEG 300, 100 MM TRIS (8.0), VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 291K, PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
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 84.56750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 84.60600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 84.94200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 84.60600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 84.56750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 84.94200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 300 REMARK: AS PER THE AUTHORS THE BIOLOGICAL ASSEMBLY IS A DIMER
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J
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 MET A 1
REMARK 465 SER A 2
REMARK 465 THR A 3
REMARK 465 GLU A 4
REMARK 465 PRO A 5
REMARK 465 VAL A 6
REMARK 465 GLU A 259
REMARK 465 LYS A 260
REMARK 465 LYS A 261
REMARK 465 ARG A 262
REMARK 465 GLN A 263
REMARK 465 LEU A 264
REMARK 465 ASP A 265
REMARK 465 ASN A 266
REMARK 465 GLY A 267
REMARK 465 GLU A 268
REMARK 465 ASP A 269
REMARK 465 GLY A 270
REMARK 465 ALA A 271
REMARK 465 ALA A 272
REMARK 465 LYS A 273
REMARK 465 SER A 274
REMARK 465 ASP A 275
REMARK 465 GLU A 409
REMARK 465 ASN A 410
REMARK 465 ALA A 411
REMARK 465 LEU A 412
REMARK 465 LYS A 413
REMARK 465 LYS A 414
REMARK 465 SER A 415
REMARK 465 ASP A 416
REMARK 465 GLY A 417
REMARK 465 THR A 418
REMARK 465 ARG A 419
REMARK 465 LYS A 420
REMARK 465 LYS A 603
REMARK 465 GLY A 604
REMARK 465 LEU A 605
REMARK 465 GLY A 606
REMARK 465 PRO A 1071
REMARK 465 ASN A 1072
REMARK 465 ASP A 1073
REMARK 465 GLU A 1074
REMARK 465 ILE A 1075
REMARK 465 ALA A 1076
REMARK 465 GLU A 1077
REMARK 465 GLN A 1078
REMARK 465 ILE A 1079
REMARK 465 ASN A 1080
REMARK 465 ASP A 1081
REMARK 465 VAL A 1082
REMARK 465 LYS A 1083
REMARK 465 GLY A 1084
REMARK 465 ALA A 1085
REMARK 465 THR A 1086
REMARK 465 SER A 1087
REMARK 465 ASP A 1088
REMARK 465 GLU A 1089
REMARK 465 GLU A 1090
REMARK 465 ASP A 1091
REMARK 465 GLU A 1092
REMARK 465 GLU A 1093
REMARK 465 SER A 1094
REMARK 465 SER A 1095
REMARK 465 HIS A 1096
REMARK 465 GLU A 1097
REMARK 465 ASP A 1098
REMARK 465 THR A 1099
REMARK 465 GLU A 1100
REMARK 465 ASN A 1101
REMARK 465 VAL A 1102
REMARK 465 ILE A 1103
REMARK 465 ASN A 1104
REMARK 465 GLY A 1105
REMARK 465 PRO A 1106
REMARK 465 MET F 1
REMARK 465 SER F 2
REMARK 465 THR F 3
REMARK 465 GLU F 4
REMARK 465 PRO F 5
REMARK 465 VAL F 6
REMARK 465 GLU F 259
REMARK 465 LYS F 260
REMARK 465 LYS F 261
REMARK 465 ARG F 262
REMARK 465 GLN F 263
REMARK 465 LEU F 264
REMARK 465 ASP F 265
REMARK 465 ASN F 266
REMARK 465 GLY F 267
REMARK 465 GLU F 268
REMARK 465 ASP F 269
REMARK 465 GLY F 270
REMARK 465 ALA F 271
REMARK 465 ALA F 272
REMARK 465 LYS F 273
REMARK 465 SER F 274
REMARK 465 ASP F 275
REMARK 465 ASP F 405
REMARK 465 ALA F 406
REMARK 465 ASN F 407
REMARK 465 GLU F 408
REMARK 465 GLU F 409
REMARK 465 ASN F 410
REMARK 465 ALA F 411
REMARK 465 LEU F 412
REMARK 465 LYS F 413
REMARK 465 LYS F 414
REMARK 465 SER F 415
REMARK 465 ASP F 416
REMARK 465 GLY F 417
REMARK 465 THR F 418
REMARK 465 ARG F 419
REMARK 465 LYS F 420
REMARK 465 LYS F 603
REMARK 465 GLY F 604
REMARK 465 LEU F 605
REMARK 465 GLY F 606
REMARK 465 PRO F 1071
REMARK 465 ASN F 1072
REMARK 465 ASP F 1073
REMARK 465 GLU F 1074
REMARK 465 ILE F 1075
REMARK 465 ALA F 1076
REMARK 465 GLU F 1077
REMARK 465 GLN F 1078
REMARK 465 ILE F 1079
REMARK 465 ASN F 1080
REMARK 465 ASP F 1081
REMARK 465 VAL F 1082
REMARK 465 LYS F 1083
REMARK 465 GLY F 1084
REMARK 465 ALA F 1085
REMARK 465 THR F 1086
REMARK 465 SER F 1087
REMARK 465 ASP F 1088
REMARK 465 GLU F 1089
REMARK 465 GLU F 1090
REMARK 465 ASP F 1091
REMARK 465 GLU F 1092
REMARK 465 GLU F 1093
REMARK 465 SER F 1094
REMARK 465 SER F 1095
REMARK 465 HIS F 1096
REMARK 465 GLU F 1097
REMARK 465 ASP F 1098
REMARK 465 THR F 1099
REMARK 465 GLU F 1100
REMARK 465 ASN F 1101
REMARK 465 VAL F 1102
REMARK 465 ILE F 1103
REMARK 465 ASN F 1104
REMARK 465 GLY F 1105
REMARK 465 PRO F 1106
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 DC C 1 O5'
REMARK 470 DC H 1 O5'
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 DT I 10 O3' TSP I 11 P -0.082
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 DT D 10 O4' - C1' - N1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 TSP D 11 O3' - P - O5' ANGL. DEV. = 16.7 DEGREES
REMARK 500 DC E 1 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DT I 10 C4' - C3' - O3' ANGL. DEV. = 12.8 DEGREES
REMARK 500 DT I 10 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ASP A 100 -155.25 -77.96
REMARK 500 LYS A 243 -52.14 81.80
REMARK 500 PRO A 277 -167.04 -70.20
REMARK 500 ASN A 285 -176.44 -170.02
REMARK 500 LYS A 338 11.47 85.01
REMARK 500 SER A 339 142.28 -38.21
REMARK 500 ASN A 359 65.85 36.39
REMARK 500 SER A 379 155.80 175.05
REMARK 500 THR A 437 -179.36 -68.14
REMARK 500 ARG A 507 137.08 -33.37
REMARK 500 LYS A 508 -160.37 51.62
REMARK 500 ASP A 526 -8.32 -48.95
REMARK 500 GLU A 591 -35.28 -153.48
REMARK 500 LEU A 609 121.03 -32.03
REMARK 500 LEU A 667 -37.09 -138.13
REMARK 500 GLU A 679 -55.65 -136.25
REMARK 500 SER A 755 -93.63 -103.39
REMARK 500 PHE A 767 31.66 -86.98
REMARK 500 ALA A 777 162.18 -48.59
REMARK 500 ARG A 781 -9.65 -56.25
REMARK 500 LEU A 882 43.41 77.73
REMARK 500 ASP A 938 -118.01 -97.07
REMARK 500 ASN A1042 -145.57 66.59
REMARK 500 LYS A1043 83.39 61.33
REMARK 500 ASP F 100 -155.21 -77.92
REMARK 500 LYS F 243 -52.14 81.80
REMARK 500 PRO F 277 -167.04 -70.23
REMARK 500 ASN F 285 -176.44 -170.03
REMARK 500 LYS F 338 11.47 85.06
REMARK 500 SER F 339 142.30 -38.21
REMARK 500 ASN F 359 65.85 36.36
REMARK 500 SER F 379 155.79 175.00
REMARK 500 THR F 437 -179.34 -68.12
REMARK 500 ARG F 507 137.08 -33.37
REMARK 500 LYS F 508 -160.36 51.62
REMARK 500 ASP F 526 -8.34 -48.97
REMARK 500 GLU F 591 -35.31 -153.45
REMARK 500 LEU F 609 121.02 -32.04
REMARK 500 LEU F 667 -37.11 -138.10
REMARK 500 GLU F 679 -55.66 -136.23
REMARK 500 SER F 755 -93.65 -103.33
REMARK 500 PHE F 767 31.63 -86.97
REMARK 500 ALA F 777 162.17 -48.55
REMARK 500 PTR F 782 -62.40 -92.07
REMARK 500 LEU F 882 43.36 77.77
REMARK 500 ASP F 938 -118.06 -97.10
REMARK 500 ASN F1042 -145.58 66.64
REMARK 500 LYS F1043 83.33 61.33
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 A1201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP A1202 O1B
REMARK 620 2 ANP A1202 O2G 64.5
REMARK 620 3 ANP A1202 O1A 64.0 102.4
REMARK 620 4 ASN A 70 OD1 75.0 137.3 69.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG F1201 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP F1202 O1B
REMARK 620 2 ANP F1202 O1A 64.3
REMARK 620 3 ANP F1202 O2G 60.7 101.8
REMARK 620 4 ASN F 70 OD1 73.3 71.2 130.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP F 1202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3L4J RELATED DB: PDB
REMARK 900 YEAST DNA BINDING AND CLEAVAGE CORE
REMARK 900 RELATED ID: 3L4K RELATED DB: PDB
REMARK 900 YEAST DNA BINDING AND CLEAVAGE CORE
REMARK 900 RELATED ID: 1PVG RELATED DB: PDB
REMARK 900 YEAST ATPASE
DBREF 4GFH A 1 1177 UNP P06786 TOP2_YEAST 1 1177
DBREF 4GFH F 1 1177 UNP P06786 TOP2_YEAST 1 1177
DBREF 4GFH B 1 11 PDB 4GFH 4GFH 1 11
DBREF 4GFH G 1 11 PDB 4GFH 4GFH 1 11
DBREF 4GFH C 1 15 PDB 4GFH 4GFH 1 15
DBREF 4GFH H 1 15 PDB 4GFH 4GFH 1 15
DBREF 4GFH D 1 11 PDB 4GFH 4GFH 1 11
DBREF 4GFH I 1 11 PDB 4GFH 4GFH 1 11
DBREF 4GFH E 1 15 PDB 4GFH 4GFH 1 15
DBREF 4GFH J 1 15 PDB 4GFH 4GFH 1 15
SEQRES 1 A 1177 MET SER THR GLU PRO VAL SER ALA SER ASP LYS TYR GLN
SEQRES 2 A 1177 LYS ILE SER GLN LEU GLU HIS ILE LEU LYS ARG PRO ASP
SEQRES 3 A 1177 THR TYR ILE GLY SER VAL GLU THR GLN GLU GLN LEU GLN
SEQRES 4 A 1177 TRP ILE TYR ASP GLU GLU THR ASP CYS MET ILE GLU LYS
SEQRES 5 A 1177 ASN VAL THR ILE VAL PRO GLY LEU PHE LYS ILE PHE ASP
SEQRES 6 A 1177 GLU ILE LEU VAL ASN ALA ALA ASP ASN LYS VAL ARG ASP
SEQRES 7 A 1177 PRO SER MET LYS ARG ILE ASP VAL ASN ILE HIS ALA GLU
SEQRES 8 A 1177 GLU HIS THR ILE GLU VAL LYS ASN ASP GLY LYS GLY ILE
SEQRES 9 A 1177 PRO ILE GLU ILE HIS ASN LYS GLU ASN ILE TYR ILE PRO
SEQRES 10 A 1177 GLU MET ILE PHE GLY HIS LEU LEU THR SER SER ASN TYR
SEQRES 11 A 1177 ASP ASP ASP GLU LYS LYS VAL THR GLY GLY ARG ASN GLY
SEQRES 12 A 1177 TYR GLY ALA LYS LEU CYS ASN ILE PHE SER THR GLU PHE
SEQRES 13 A 1177 ILE LEU GLU THR ALA ASP LEU ASN VAL GLY GLN LYS TYR
SEQRES 14 A 1177 VAL GLN LYS TRP GLU ASN ASN MET SER ILE CYS HIS PRO
SEQRES 15 A 1177 PRO LYS ILE THR SER TYR LYS LYS GLY PRO SER TYR THR
SEQRES 16 A 1177 LYS VAL THR PHE LYS PRO ASP LEU THR ARG PHE GLY MET
SEQRES 17 A 1177 LYS GLU LEU ASP ASN ASP ILE LEU GLY VAL MET ARG ARG
SEQRES 18 A 1177 ARG VAL TYR ASP ILE ASN GLY SER VAL ARG ASP ILE ASN
SEQRES 19 A 1177 VAL TYR LEU ASN GLY LYS SER LEU LYS ILE ARG ASN PHE
SEQRES 20 A 1177 LYS ASN TYR VAL GLU LEU TYR LEU LYS SER LEU GLU LYS
SEQRES 21 A 1177 LYS ARG GLN LEU ASP ASN GLY GLU ASP GLY ALA ALA LYS
SEQRES 22 A 1177 SER ASP ILE PRO THR ILE LEU TYR GLU ARG ILE ASN ASN
SEQRES 23 A 1177 ARG TRP GLU VAL ALA PHE ALA VAL SER ASP ILE SER PHE
SEQRES 24 A 1177 GLN GLN ILE SER PHE VAL ASN SER ILE ALA THR THR MET
SEQRES 25 A 1177 GLY GLY THR HIS VAL ASN TYR ILE THR ASP GLN ILE VAL
SEQRES 26 A 1177 LYS LYS ILE SER GLU ILE LEU LYS LYS LYS LYS LYS LYS
SEQRES 27 A 1177 SER VAL LYS SER PHE GLN ILE LYS ASN ASN MET PHE ILE
SEQRES 28 A 1177 PHE ILE ASN CYS LEU ILE GLU ASN PRO ALA PHE THR SER
SEQRES 29 A 1177 GLN THR LYS GLU GLN LEU THR THR ARG VAL LYS ASP PHE
SEQRES 30 A 1177 GLY SER ARG CYS GLU ILE PRO LEU GLU TYR ILE ASN LYS
SEQRES 31 A 1177 ILE MET LYS THR ASP LEU ALA THR ARG MET PHE GLU ILE
SEQRES 32 A 1177 ALA ASP ALA ASN GLU GLU ASN ALA LEU LYS LYS SER ASP
SEQRES 33 A 1177 GLY THR ARG LYS SER ARG ILE THR ASN TYR PRO LYS LEU
SEQRES 34 A 1177 GLU ASP ALA ASN LYS ALA GLY THR LYS GLU GLY TYR LYS
SEQRES 35 A 1177 CYS THR LEU VAL LEU THR GLU GLY ASP SER ALA LEU SER
SEQRES 36 A 1177 LEU ALA VAL ALA GLY LEU ALA VAL VAL GLY ARG ASP TYR
SEQRES 37 A 1177 TYR GLY CYS TYR PRO LEU ARG GLY LYS MET LEU ASN VAL
SEQRES 38 A 1177 ARG GLU ALA SER ALA ASP GLN ILE LEU LYS ASN ALA GLU
SEQRES 39 A 1177 ILE GLN ALA ILE LYS LYS ILE MET GLY LEU GLN HIS ARG
SEQRES 40 A 1177 LYS LYS TYR GLU ASP THR LYS SER LEU ARG TYR GLY HIS
SEQRES 41 A 1177 LEU MET ILE MET THR ASP GLN ASP HIS ASP GLY SER HIS
SEQRES 42 A 1177 ILE LYS GLY LEU ILE ILE ASN PHE LEU GLU SER SER PHE
SEQRES 43 A 1177 PRO GLY LEU LEU ASP ILE GLN GLY PHE LEU LEU GLU PHE
SEQRES 44 A 1177 ILE THR PRO ILE ILE LYS VAL SER ILE THR LYS PRO THR
SEQRES 45 A 1177 LYS ASN THR ILE ALA PHE TYR ASN MET PRO ASP TYR GLU
SEQRES 46 A 1177 LYS TRP ARG GLU GLU GLU SER HIS LYS PHE THR TRP LYS
SEQRES 47 A 1177 GLN LYS TYR TYR LYS GLY LEU GLY THR SER LEU ALA GLN
SEQRES 48 A 1177 GLU VAL ARG GLU TYR PHE SER ASN LEU ASP ARG HIS LEU
SEQRES 49 A 1177 LYS ILE PHE HIS SER LEU GLN GLY ASN ASP LYS ASP TYR
SEQRES 50 A 1177 ILE ASP LEU ALA PHE SER LYS LYS LYS ALA ASP ASP ARG
SEQRES 51 A 1177 LYS GLU TRP LEU ARG GLN TYR GLU PRO GLY THR VAL LEU
SEQRES 52 A 1177 ASP PRO THR LEU LYS GLU ILE PRO ILE SER ASP PHE ILE
SEQRES 53 A 1177 ASN LYS GLU LEU ILE LEU PHE SER LEU ALA ASP ASN ILE
SEQRES 54 A 1177 ARG SER ILE PRO ASN VAL LEU ASP GLY PHE LYS PRO GLY
SEQRES 55 A 1177 GLN ARG LYS VAL LEU TYR GLY CYS PHE LYS LYS ASN LEU
SEQRES 56 A 1177 LYS SER GLU LEU LYS VAL ALA GLN LEU ALA PRO TYR VAL
SEQRES 57 A 1177 SER GLU CYS THR ALA TYR HIS HIS GLY GLU GLN SER LEU
SEQRES 58 A 1177 ALA GLN THR ILE ILE GLY LEU ALA GLN ASN PHE VAL GLY
SEQRES 59 A 1177 SER ASN ASN ILE TYR LEU LEU LEU PRO ASN GLY ALA PHE
SEQRES 60 A 1177 GLY THR ARG ALA THR GLY GLY LYS ASP ALA ALA ALA ALA
SEQRES 61 A 1177 ARG PTR ILE TYR THR GLU LEU ASN LYS LEU THR ARG LYS
SEQRES 62 A 1177 ILE PHE HIS PRO ALA ASP ASP PRO LEU TYR LYS TYR ILE
SEQRES 63 A 1177 GLN GLU ASP GLU LYS THR VAL GLU PRO GLU TRP TYR LEU
SEQRES 64 A 1177 PRO ILE LEU PRO MET ILE LEU VAL ASN GLY ALA GLU GLY
SEQRES 65 A 1177 ILE GLY THR GLY TRP SER THR TYR ILE PRO PRO PHE ASN
SEQRES 66 A 1177 PRO LEU GLU ILE ILE LYS ASN ILE ARG HIS LEU MET ASN
SEQRES 67 A 1177 ASP GLU GLU LEU GLU GLN MET HIS PRO TRP PHE ARG GLY
SEQRES 68 A 1177 TRP THR GLY THR ILE GLU GLU ILE GLU PRO LEU ARG TYR
SEQRES 69 A 1177 ARG MET TYR GLY ARG ILE GLU GLN ILE GLY ASP ASN VAL
SEQRES 70 A 1177 LEU GLU ILE THR GLU LEU PRO ALA ARG THR TRP THR SER
SEQRES 71 A 1177 THR ILE LYS GLU TYR LEU LEU LEU GLY LEU SER GLY ASN
SEQRES 72 A 1177 ASP LYS ILE LYS PRO TRP ILE LYS ASP MET GLU GLU GLN
SEQRES 73 A 1177 HIS ASP ASP ASN ILE LYS PHE ILE ILE THR LEU SER PRO
SEQRES 74 A 1177 GLU GLU MET ALA LYS THR ARG LYS ILE GLY PHE TYR GLU
SEQRES 75 A 1177 ARG PHE LYS LEU ILE SER PRO ILE SER LEU MET ASN MET
SEQRES 76 A 1177 VAL ALA PHE ASP PRO HIS GLY LYS ILE LYS LYS TYR ASN
SEQRES 77 A 1177 SER VAL ASN GLU ILE LEU SER GLU PHE TYR TYR VAL ARG
SEQRES 78 A 1177 LEU GLU TYR TYR GLN LYS ARG LYS ASP HIS MET SER GLU
SEQRES 79 A 1177 ARG LEU GLN TRP GLU VAL GLU LYS TYR SER PHE GLN VAL
SEQRES 80 A 1177 LYS PHE ILE LYS MET ILE ILE GLU LYS GLU LEU THR VAL
SEQRES 81 A 1177 THR ASN LYS PRO ARG ASN ALA ILE ILE GLN GLU LEU GLU
SEQRES 82 A 1177 ASN LEU GLY PHE PRO ARG PHE ASN LYS GLU GLY LYS PRO
SEQRES 83 A 1177 TYR TYR GLY SER PRO ASN ASP GLU ILE ALA GLU GLN ILE
SEQRES 84 A 1177 ASN ASP VAL LYS GLY ALA THR SER ASP GLU GLU ASP GLU
SEQRES 85 A 1177 GLU SER SER HIS GLU ASP THR GLU ASN VAL ILE ASN GLY
SEQRES 86 A 1177 PRO GLU GLU LEU TYR GLY THR TYR GLU TYR LEU LEU GLY
SEQRES 87 A 1177 MET ARG ILE TRP SER LEU THR LYS GLU ARG TYR GLN LYS
SEQRES 88 A 1177 LEU LEU LYS GLN LYS GLN GLU LYS GLU THR GLU LEU GLU
SEQRES 89 A 1177 ASN LEU LEU LYS LEU SER ALA LYS ASP ILE TRP ASN THR
SEQRES 90 A 1177 ASP LEU LYS ALA PHE GLU VAL GLY TYR GLN GLU PHE LEU
SEQRES 91 A 1177 GLN ARG ASP ALA GLU ALA ARG
SEQRES 1 B 11 DC DC DT DA DC DT DG DC DT DA DC
SEQRES 1 C 15 DC DG DC DG DG DT DA DG DC DA DG DT DA
SEQRES 2 C 15 DG DG
SEQRES 1 D 11 DG DG DA DT DG DA DC DG DA DT TSP
SEQRES 1 E 15 DC DG DC DG DA DA DT DC DG DT DC DA DT
SEQRES 2 E 15 DC DC
SEQRES 1 F 1177 MET SER THR GLU PRO VAL SER ALA SER ASP LYS TYR GLN
SEQRES 2 F 1177 LYS ILE SER GLN LEU GLU HIS ILE LEU LYS ARG PRO ASP
SEQRES 3 F 1177 THR TYR ILE GLY SER VAL GLU THR GLN GLU GLN LEU GLN
SEQRES 4 F 1177 TRP ILE TYR ASP GLU GLU THR ASP CYS MET ILE GLU LYS
SEQRES 5 F 1177 ASN VAL THR ILE VAL PRO GLY LEU PHE LYS ILE PHE ASP
SEQRES 6 F 1177 GLU ILE LEU VAL ASN ALA ALA ASP ASN LYS VAL ARG ASP
SEQRES 7 F 1177 PRO SER MET LYS ARG ILE ASP VAL ASN ILE HIS ALA GLU
SEQRES 8 F 1177 GLU HIS THR ILE GLU VAL LYS ASN ASP GLY LYS GLY ILE
SEQRES 9 F 1177 PRO ILE GLU ILE HIS ASN LYS GLU ASN ILE TYR ILE PRO
SEQRES 10 F 1177 GLU MET ILE PHE GLY HIS LEU LEU THR SER SER ASN TYR
SEQRES 11 F 1177 ASP ASP ASP GLU LYS LYS VAL THR GLY GLY ARG ASN GLY
SEQRES 12 F 1177 TYR GLY ALA LYS LEU CYS ASN ILE PHE SER THR GLU PHE
SEQRES 13 F 1177 ILE LEU GLU THR ALA ASP LEU ASN VAL GLY GLN LYS TYR
SEQRES 14 F 1177 VAL GLN LYS TRP GLU ASN ASN MET SER ILE CYS HIS PRO
SEQRES 15 F 1177 PRO LYS ILE THR SER TYR LYS LYS GLY PRO SER TYR THR
SEQRES 16 F 1177 LYS VAL THR PHE LYS PRO ASP LEU THR ARG PHE GLY MET
SEQRES 17 F 1177 LYS GLU LEU ASP ASN ASP ILE LEU GLY VAL MET ARG ARG
SEQRES 18 F 1177 ARG VAL TYR ASP ILE ASN GLY SER VAL ARG ASP ILE ASN
SEQRES 19 F 1177 VAL TYR LEU ASN GLY LYS SER LEU LYS ILE ARG ASN PHE
SEQRES 20 F 1177 LYS ASN TYR VAL GLU LEU TYR LEU LYS SER LEU GLU LYS
SEQRES 21 F 1177 LYS ARG GLN LEU ASP ASN GLY GLU ASP GLY ALA ALA LYS
SEQRES 22 F 1177 SER ASP ILE PRO THR ILE LEU TYR GLU ARG ILE ASN ASN
SEQRES 23 F 1177 ARG TRP GLU VAL ALA PHE ALA VAL SER ASP ILE SER PHE
SEQRES 24 F 1177 GLN GLN ILE SER PHE VAL ASN SER ILE ALA THR THR MET
SEQRES 25 F 1177 GLY GLY THR HIS VAL ASN TYR ILE THR ASP GLN ILE VAL
SEQRES 26 F 1177 LYS LYS ILE SER GLU ILE LEU LYS LYS LYS LYS LYS LYS
SEQRES 27 F 1177 SER VAL LYS SER PHE GLN ILE LYS ASN ASN MET PHE ILE
SEQRES 28 F 1177 PHE ILE ASN CYS LEU ILE GLU ASN PRO ALA PHE THR SER
SEQRES 29 F 1177 GLN THR LYS GLU GLN LEU THR THR ARG VAL LYS ASP PHE
SEQRES 30 F 1177 GLY SER ARG CYS GLU ILE PRO LEU GLU TYR ILE ASN LYS
SEQRES 31 F 1177 ILE MET LYS THR ASP LEU ALA THR ARG MET PHE GLU ILE
SEQRES 32 F 1177 ALA ASP ALA ASN GLU GLU ASN ALA LEU LYS LYS SER ASP
SEQRES 33 F 1177 GLY THR ARG LYS SER ARG ILE THR ASN TYR PRO LYS LEU
SEQRES 34 F 1177 GLU ASP ALA ASN LYS ALA GLY THR LYS GLU GLY TYR LYS
SEQRES 35 F 1177 CYS THR LEU VAL LEU THR GLU GLY ASP SER ALA LEU SER
SEQRES 36 F 1177 LEU ALA VAL ALA GLY LEU ALA VAL VAL GLY ARG ASP TYR
SEQRES 37 F 1177 TYR GLY CYS TYR PRO LEU ARG GLY LYS MET LEU ASN VAL
SEQRES 38 F 1177 ARG GLU ALA SER ALA ASP GLN ILE LEU LYS ASN ALA GLU
SEQRES 39 F 1177 ILE GLN ALA ILE LYS LYS ILE MET GLY LEU GLN HIS ARG
SEQRES 40 F 1177 LYS LYS TYR GLU ASP THR LYS SER LEU ARG TYR GLY HIS
SEQRES 41 F 1177 LEU MET ILE MET THR ASP GLN ASP HIS ASP GLY SER HIS
SEQRES 42 F 1177 ILE LYS GLY LEU ILE ILE ASN PHE LEU GLU SER SER PHE
SEQRES 43 F 1177 PRO GLY LEU LEU ASP ILE GLN GLY PHE LEU LEU GLU PHE
SEQRES 44 F 1177 ILE THR PRO ILE ILE LYS VAL SER ILE THR LYS PRO THR
SEQRES 45 F 1177 LYS ASN THR ILE ALA PHE TYR ASN MET PRO ASP TYR GLU
SEQRES 46 F 1177 LYS TRP ARG GLU GLU GLU SER HIS LYS PHE THR TRP LYS
SEQRES 47 F 1177 GLN LYS TYR TYR LYS GLY LEU GLY THR SER LEU ALA GLN
SEQRES 48 F 1177 GLU VAL ARG GLU TYR PHE SER ASN LEU ASP ARG HIS LEU
SEQRES 49 F 1177 LYS ILE PHE HIS SER LEU GLN GLY ASN ASP LYS ASP TYR
SEQRES 50 F 1177 ILE ASP LEU ALA PHE SER LYS LYS LYS ALA ASP ASP ARG
SEQRES 51 F 1177 LYS GLU TRP LEU ARG GLN TYR GLU PRO GLY THR VAL LEU
SEQRES 52 F 1177 ASP PRO THR LEU LYS GLU ILE PRO ILE SER ASP PHE ILE
SEQRES 53 F 1177 ASN LYS GLU LEU ILE LEU PHE SER LEU ALA ASP ASN ILE
SEQRES 54 F 1177 ARG SER ILE PRO ASN VAL LEU ASP GLY PHE LYS PRO GLY
SEQRES 55 F 1177 GLN ARG LYS VAL LEU TYR GLY CYS PHE LYS LYS ASN LEU
SEQRES 56 F 1177 LYS SER GLU LEU LYS VAL ALA GLN LEU ALA PRO TYR VAL
SEQRES 57 F 1177 SER GLU CYS THR ALA TYR HIS HIS GLY GLU GLN SER LEU
SEQRES 58 F 1177 ALA GLN THR ILE ILE GLY LEU ALA GLN ASN PHE VAL GLY
SEQRES 59 F 1177 SER ASN ASN ILE TYR LEU LEU LEU PRO ASN GLY ALA PHE
SEQRES 60 F 1177 GLY THR ARG ALA THR GLY GLY LYS ASP ALA ALA ALA ALA
SEQRES 61 F 1177 ARG PTR ILE TYR THR GLU LEU ASN LYS LEU THR ARG LYS
SEQRES 62 F 1177 ILE PHE HIS PRO ALA ASP ASP PRO LEU TYR LYS TYR ILE
SEQRES 63 F 1177 GLN GLU ASP GLU LYS THR VAL GLU PRO GLU TRP TYR LEU
SEQRES 64 F 1177 PRO ILE LEU PRO MET ILE LEU VAL ASN GLY ALA GLU GLY
SEQRES 65 F 1177 ILE GLY THR GLY TRP SER THR TYR ILE PRO PRO PHE ASN
SEQRES 66 F 1177 PRO LEU GLU ILE ILE LYS ASN ILE ARG HIS LEU MET ASN
SEQRES 67 F 1177 ASP GLU GLU LEU GLU GLN MET HIS PRO TRP PHE ARG GLY
SEQRES 68 F 1177 TRP THR GLY THR ILE GLU GLU ILE GLU PRO LEU ARG TYR
SEQRES 69 F 1177 ARG MET TYR GLY ARG ILE GLU GLN ILE GLY ASP ASN VAL
SEQRES 70 F 1177 LEU GLU ILE THR GLU LEU PRO ALA ARG THR TRP THR SER
SEQRES 71 F 1177 THR ILE LYS GLU TYR LEU LEU LEU GLY LEU SER GLY ASN
SEQRES 72 F 1177 ASP LYS ILE LYS PRO TRP ILE LYS ASP MET GLU GLU GLN
SEQRES 73 F 1177 HIS ASP ASP ASN ILE LYS PHE ILE ILE THR LEU SER PRO
SEQRES 74 F 1177 GLU GLU MET ALA LYS THR ARG LYS ILE GLY PHE TYR GLU
SEQRES 75 F 1177 ARG PHE LYS LEU ILE SER PRO ILE SER LEU MET ASN MET
SEQRES 76 F 1177 VAL ALA PHE ASP PRO HIS GLY LYS ILE LYS LYS TYR ASN
SEQRES 77 F 1177 SER VAL ASN GLU ILE LEU SER GLU PHE TYR TYR VAL ARG
SEQRES 78 F 1177 LEU GLU TYR TYR GLN LYS ARG LYS ASP HIS MET SER GLU
SEQRES 79 F 1177 ARG LEU GLN TRP GLU VAL GLU LYS TYR SER PHE GLN VAL
SEQRES 80 F 1177 LYS PHE ILE LYS MET ILE ILE GLU LYS GLU LEU THR VAL
SEQRES 81 F 1177 THR ASN LYS PRO ARG ASN ALA ILE ILE GLN GLU LEU GLU
SEQRES 82 F 1177 ASN LEU GLY PHE PRO ARG PHE ASN LYS GLU GLY LYS PRO
SEQRES 83 F 1177 TYR TYR GLY SER PRO ASN ASP GLU ILE ALA GLU GLN ILE
SEQRES 84 F 1177 ASN ASP VAL LYS GLY ALA THR SER ASP GLU GLU ASP GLU
SEQRES 85 F 1177 GLU SER SER HIS GLU ASP THR GLU ASN VAL ILE ASN GLY
SEQRES 86 F 1177 PRO GLU GLU LEU TYR GLY THR TYR GLU TYR LEU LEU GLY
SEQRES 87 F 1177 MET ARG ILE TRP SER LEU THR LYS GLU ARG TYR GLN LYS
SEQRES 88 F 1177 LEU LEU LYS GLN LYS GLN GLU LYS GLU THR GLU LEU GLU
SEQRES 89 F 1177 ASN LEU LEU LYS LEU SER ALA LYS ASP ILE TRP ASN THR
SEQRES 90 F 1177 ASP LEU LYS ALA PHE GLU VAL GLY TYR GLN GLU PHE LEU
SEQRES 91 F 1177 GLN ARG ASP ALA GLU ALA ARG
SEQRES 1 G 11 DC DC DT DA DC DT DG DC DT DA DC
SEQRES 1 H 15 DC DG DC DG DG DT DA DG DC DA DG DT DA
SEQRES 2 H 15 DG DG
SEQRES 1 I 11 DG DG DA DT DG DA DC DG DA DT TSP
SEQRES 1 J 15 DC DG DC DG DA DA DT DC DG DT DC DA DT
SEQRES 2 J 15 DC DC
MODRES 4GFH PTR A 782 TYR O-PHOSPHOTYROSINE
MODRES 4GFH TSP D 11 T 3'-THIO-THYMIDINE-5'-PHOSPHATE
MODRES 4GFH PTR F 782 TYR O-PHOSPHOTYROSINE
MODRES 4GFH TSP I 11 T 3'-THIO-THYMIDINE-5'-PHOSPHATE
HET PTR A 782 16
HET TSP D 11 20
HET PTR F 782 16
HET TSP I 11 20
HET MG A1201 1
HET ANP A1202 31
HET MG F1201 1
HET ANP F1202 31
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM TSP 3'-THIO-THYMIDINE-5'-PHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR 2(C9 H12 N O6 P)
FORMUL 4 TSP 2(C10 H15 N2 O7 P S)
FORMUL 11 MG 2(MG 2+)
FORMUL 12 ANP 2(C10 H17 N6 O12 P3)
HELIX 1 1 SER A 7 TYR A 12 1 6
HELIX 2 2 SER A 16 ARG A 24 1 9
HELIX 3 3 PRO A 25 TYR A 28 5 4
HELIX 4 4 VAL A 57 ASP A 78 1 22
HELIX 5 5 TYR A 115 HIS A 123 1 9
HELIX 6 6 TYR A 144 PHE A 152 1 9
HELIX 7 7 ASP A 202 GLY A 207 1 6
HELIX 8 8 ASP A 212 VAL A 230 1 19
HELIX 9 9 ASN A 246 GLU A 252 1 7
HELIX 10 10 LEU A 253 LEU A 255 5 3
HELIX 11 11 THR A 315 LYS A 336 1 22
HELIX 12 12 LYS A 341 ASN A 347 1 7
HELIX 13 13 ARG A 373 PHE A 377 5 5
HELIX 14 14 PRO A 384 MET A 392 1 9
HELIX 15 15 THR A 394 ASP A 405 1 12
HELIX 16 16 GLY A 450 GLY A 465 1 16
HELIX 17 17 SER A 485 ASN A 492 1 8
HELIX 18 18 ASN A 492 MET A 502 1 11
HELIX 19 19 ASP A 512 LEU A 516 5 5
HELIX 20 20 ASP A 528 PHE A 546 1 19
HELIX 21 21 ASN A 580 GLU A 591 1 12
HELIX 22 22 SER A 592 PHE A 595 5 4
HELIX 23 23 LEU A 609 ASN A 619 1 11
HELIX 24 24 ASP A 634 SER A 643 1 10
HELIX 25 25 LYS A 646 TYR A 657 1 12
HELIX 26 26 ILE A 672 GLU A 679 1 8
HELIX 27 27 GLU A 679 ILE A 692 1 14
HELIX 28 28 LYS A 700 LYS A 713 1 14
HELIX 29 29 VAL A 721 THR A 732 1 12
HELIX 30 30 GLY A 737 GLN A 750 1 14
HELIX 31 31 LEU A 790 PHE A 795 1 6
HELIX 32 32 HIS A 796 ASP A 800 5 5
HELIX 33 33 ASN A 845 ASN A 858 1 14
HELIX 34 34 TRP A 908 GLY A 922 1 15
HELIX 35 35 SER A 948 GLY A 959 1 12
HELIX 36 36 GLY A 959 PHE A 964 1 6
HELIX 37 37 SER A 989 GLU A 1035 1 47
HELIX 38 38 PRO A 1044 LEU A 1055 1 12
HELIX 39 39 TYR A 1113 GLY A 1118 1 6
HELIX 40 40 ARG A 1120 LEU A 1124 5 5
HELIX 41 41 THR A 1125 LYS A 1148 1 24
HELIX 42 42 SER A 1150 ALA A 1176 1 27
HELIX 43 43 ALA F 8 TYR F 12 1 5
HELIX 44 44 SER F 16 ARG F 24 1 9
HELIX 45 45 PRO F 25 TYR F 28 5 4
HELIX 46 46 VAL F 57 ASP F 78 1 22
HELIX 47 47 TYR F 115 HIS F 123 1 9
HELIX 48 48 TYR F 144 PHE F 152 1 9
HELIX 49 49 ASP F 202 GLY F 207 1 6
HELIX 50 50 ASP F 212 VAL F 230 1 19
HELIX 51 51 ASN F 246 GLU F 252 1 7
HELIX 52 52 LEU F 253 LEU F 255 5 3
HELIX 53 53 THR F 315 LYS F 336 1 22
HELIX 54 54 LYS F 341 ASN F 347 1 7
HELIX 55 55 ARG F 373 PHE F 377 5 5
HELIX 56 56 PRO F 384 MET F 392 1 9
HELIX 57 57 THR F 394 ALA F 404 1 11
HELIX 58 58 GLY F 450 GLY F 465 1 16
HELIX 59 59 SER F 485 ASN F 492 1 8
HELIX 60 60 ASN F 492 MET F 502 1 11
HELIX 61 61 ASP F 512 LEU F 516 5 5
HELIX 62 62 ASP F 528 PHE F 546 1 19
HELIX 63 63 ASN F 580 GLU F 591 1 12
HELIX 64 64 SER F 592 PHE F 595 5 4
HELIX 65 65 LEU F 609 ASN F 619 1 11
HELIX 66 66 ASP F 634 SER F 643 1 10
HELIX 67 67 LYS F 646 TYR F 657 1 12
HELIX 68 68 ILE F 672 GLU F 679 1 8
HELIX 69 69 GLU F 679 ILE F 692 1 14
HELIX 70 70 LYS F 700 LYS F 713 1 14
HELIX 71 71 VAL F 721 THR F 732 1 12
HELIX 72 72 GLY F 737 GLN F 750 1 14
HELIX 73 73 LEU F 790 PHE F 795 1 6
HELIX 74 74 HIS F 796 ASP F 800 5 5
HELIX 75 75 ASN F 845 ASN F 858 1 14
HELIX 76 76 TRP F 908 GLY F 922 1 15
HELIX 77 77 SER F 948 GLY F 959 1 12
HELIX 78 78 GLY F 959 PHE F 964 1 6
HELIX 79 79 SER F 989 GLU F 1035 1 47
HELIX 80 80 PRO F 1044 LEU F 1055 1 12
HELIX 81 81 TYR F 1113 GLY F 1118 1 6
HELIX 82 82 ARG F 1120 LEU F 1124 5 5
HELIX 83 83 THR F 1125 LYS F 1148 1 24
HELIX 84 84 SER F 1150 ALA F 1176 1 27
SHEET 1 A 2 GLN A 13 LYS A 14 0
SHEET 2 A 2 THR F 126 SER F 127 -1 O SER F 127 N GLN A 13
SHEET 1 B 2 GLN A 35 ASP A 43 0
SHEET 2 B 2 CYS A 48 ILE A 56 -1 O CYS A 48 N ASP A 43
SHEET 1 C 3 ILE A 179 CYS A 180 0
SHEET 2 C 3 GLN A 167 GLU A 174 -1 N GLU A 174 O ILE A 179
SHEET 3 C 3 LYS A 184 SER A 187 -1 O THR A 186 N LYS A 168
SHEET 1 D 7 ILE A 179 CYS A 180 0
SHEET 2 D 7 GLN A 167 GLU A 174 -1 N GLU A 174 O ILE A 179
SHEET 3 D 7 SER A 153 ASP A 162 -1 N PHE A 156 O TRP A 173
SHEET 4 D 7 THR A 195 PRO A 201 -1 O LYS A 196 N GLU A 159
SHEET 5 D 7 THR A 94 ASN A 99 -1 N VAL A 97 O VAL A 197
SHEET 6 D 7 ARG A 83 HIS A 89 -1 N HIS A 89 O THR A 94
SHEET 7 D 7 ASN A 234 LEU A 237 1 O TYR A 236 N VAL A 86
SHEET 1 E 2 THR A 126 SER A 127 0
SHEET 2 E 2 GLN F 13 LYS F 14 -1 O GLN F 13 N SER A 127
SHEET 1 F 5 LEU A 280 ASN A 285 0
SHEET 2 F 5 TRP A 288 VAL A 294 -1 O PHE A 292 N LEU A 280
SHEET 3 F 5 MET A 349 CYS A 355 -1 O PHE A 352 N ALA A 291
SHEET 4 F 5 GLN A 300 VAL A 305 1 N PHE A 304 O CYS A 355
SHEET 5 F 5 ALA A 309 THR A 310 -1 O THR A 310 N SER A 303
SHEET 1 G 2 GLY A 313 GLY A 314 0
SHEET 2 G 2 GLN A 369 LEU A 370 1 O LEU A 370 N GLY A 313
SHEET 1 H 6 TYR A 469 LEU A 474 0
SHEET 2 H 6 THR A 444 GLU A 449 1 N THR A 444 O GLY A 470
SHEET 3 H 6 HIS A 520 MET A 524 1 O MET A 522 N LEU A 445
SHEET 4 H 6 LEU A 556 PHE A 559 1 O LEU A 557 N LEU A 521
SHEET 5 H 6 LEU A 624 HIS A 628 -1 O LYS A 625 N GLU A 558
SHEET 6 H 6 GLU A 669 PRO A 671 1 O ILE A 670 N ILE A 626
SHEET 1 I 3 THR A 575 PHE A 578 0
SHEET 2 I 3 ILE A 564 ILE A 568 -1 N VAL A 566 O ILE A 576
SHEET 3 I 3 TRP A 597 TYR A 601 -1 O LYS A 598 N SER A 567
SHEET 1 J 2 LEU A 719 LYS A 720 0
SHEET 2 J 2 TYR A 784 THR A 785 -1 O THR A 785 N LEU A 719
SHEET 1 K 2 TYR A 805 GLU A 808 0
SHEET 2 K 2 LYS A 811 PRO A 815 -1 O LYS A 811 N GLU A 808
SHEET 1 L 2 ALA A 830 ILE A 833 0
SHEET 2 L 2 SER A 838 ILE A 841 -1 O ILE A 841 N ALA A 830
SHEET 1 M 3 THR A 875 GLU A 878 0
SHEET 2 M 3 TYR A 884 TYR A 887 -1 O TYR A 887 N THR A 875
SHEET 3 M 3 ILE A 967 ILE A 970 -1 O ILE A 970 N TYR A 884
SHEET 1 N 4 ARG A 889 GLY A 894 0
SHEET 2 N 4 VAL A 897 GLU A 902 -1 O GLU A 902 N ARG A 889
SHEET 3 N 4 PHE A 943 THR A 946 -1 O ILE A 945 N LEU A 898
SHEET 4 N 4 ASP A 932 GLU A 935 -1 N GLU A 934 O ILE A 944
SHEET 1 O 2 VAL A 976 PHE A 978 0
SHEET 2 O 2 ILE A 984 LYS A 986 -1 O LYS A 985 N ALA A 977
SHEET 1 P 2 ARG A1059 PHE A1060 0
SHEET 2 P 2 PRO A1066 TYR A1067 -1 O TYR A1067 N ARG A1059
SHEET 1 Q 2 GLN F 35 ASP F 43 0
SHEET 2 Q 2 CYS F 48 ILE F 56 -1 O CYS F 48 N ASP F 43
SHEET 1 R 3 ILE F 179 CYS F 180 0
SHEET 2 R 3 GLN F 167 GLU F 174 -1 N GLU F 174 O ILE F 179
SHEET 3 R 3 LYS F 184 SER F 187 -1 O THR F 186 N LYS F 168
SHEET 1 S 7 ILE F 179 CYS F 180 0
SHEET 2 S 7 GLN F 167 GLU F 174 -1 N GLU F 174 O ILE F 179
SHEET 3 S 7 SER F 153 ASP F 162 -1 N PHE F 156 O TRP F 173
SHEET 4 S 7 THR F 195 PRO F 201 -1 O LYS F 196 N GLU F 159
SHEET 5 S 7 THR F 94 ASN F 99 -1 N VAL F 97 O VAL F 197
SHEET 6 S 7 ARG F 83 HIS F 89 -1 N HIS F 89 O THR F 94
SHEET 7 S 7 ASN F 234 LEU F 237 1 O TYR F 236 N VAL F 86
SHEET 1 T 5 LEU F 280 ASN F 285 0
SHEET 2 T 5 TRP F 288 VAL F 294 -1 O PHE F 292 N LEU F 280
SHEET 3 T 5 MET F 349 CYS F 355 -1 O PHE F 352 N ALA F 291
SHEET 4 T 5 GLN F 300 VAL F 305 1 N PHE F 304 O CYS F 355
SHEET 5 T 5 ALA F 309 THR F 310 -1 O THR F 310 N SER F 303
SHEET 1 U 2 GLY F 313 GLY F 314 0
SHEET 2 U 2 GLN F 369 LEU F 370 1 O LEU F 370 N GLY F 313
SHEET 1 V 6 TYR F 469 LEU F 474 0
SHEET 2 V 6 THR F 444 GLU F 449 1 N THR F 444 O GLY F 470
SHEET 3 V 6 HIS F 520 MET F 524 1 O MET F 522 N LEU F 445
SHEET 4 V 6 LEU F 556 PHE F 559 1 O LEU F 557 N LEU F 521
SHEET 5 V 6 LEU F 624 HIS F 628 -1 O LYS F 625 N GLU F 558
SHEET 6 V 6 GLU F 669 PRO F 671 1 O ILE F 670 N ILE F 626
SHEET 1 W 3 THR F 575 PHE F 578 0
SHEET 2 W 3 ILE F 564 ILE F 568 -1 N VAL F 566 O ILE F 576
SHEET 3 W 3 TRP F 597 TYR F 601 -1 O LYS F 598 N SER F 567
SHEET 1 X 2 LEU F 719 LYS F 720 0
SHEET 2 X 2 TYR F 784 THR F 785 -1 O THR F 785 N LEU F 719
SHEET 1 Y 2 TYR F 805 GLU F 808 0
SHEET 2 Y 2 LYS F 811 PRO F 815 -1 O LYS F 811 N GLU F 808
SHEET 1 Z 2 ALA F 830 ILE F 833 0
SHEET 2 Z 2 SER F 838 ILE F 841 -1 O ILE F 841 N ALA F 830
SHEET 1 AA 3 THR F 875 GLU F 878 0
SHEET 2 AA 3 TYR F 884 TYR F 887 -1 O TYR F 887 N THR F 875
SHEET 3 AA 3 ILE F 967 ILE F 970 -1 O ILE F 970 N TYR F 884
SHEET 1 AB 4 ARG F 889 GLY F 894 0
SHEET 2 AB 4 VAL F 897 GLU F 902 -1 O GLU F 902 N ARG F 889
SHEET 3 AB 4 PHE F 943 THR F 946 -1 O ILE F 945 N LEU F 898
SHEET 4 AB 4 ASP F 932 GLU F 935 -1 N GLU F 934 O ILE F 944
SHEET 1 AC 2 VAL F 976 PHE F 978 0
SHEET 2 AC 2 ILE F 984 LYS F 986 -1 O LYS F 985 N ALA F 977
SHEET 1 AD 2 ARG F1059 PHE F1060 0
SHEET 2 AD 2 PRO F1066 TYR F1067 -1 O TYR F1067 N ARG F1059
LINK C ARG A 781 N APTR A 782 1555 1555 1.33
LINK C APTR A 782 N ILE A 783 1555 1555 1.33
LINK O3'B DT D 10 P BTSP D 11 1555 1555 1.59
LINK C ARG F 781 N APTR F 782 1555 1555 1.33
LINK C APTR F 782 N ILE F 783 1555 1555 1.33
LINK O3'B DT I 10 P BTSP I 11 1555 1555 1.53
LINK MG MG A1201 O1B ANP A1202 1555 1555 2.21
LINK MG MG F1201 O1B ANP F1202 1555 1555 2.33
LINK MG MG F1201 O1A ANP F1202 1555 1555 2.37
LINK MG MG A1201 O2G ANP A1202 1555 1555 2.43
LINK MG MG A1201 O1A ANP A1202 1555 1555 2.49
LINK MG MG F1201 O2G ANP F1202 1555 1555 2.57
LINK OD1 ASN F 70 MG MG F1201 1555 1555 2.70
LINK OD1 ASN A 70 MG MG A1201 1555 1555 2.71
SITE 1 AC1 3 GLU A 66 ASN A 70 ANP A1202
SITE 1 AC2 23 ASN A 70 ASN A 74 ARG A 77 ASN A 99
SITE 2 AC2 23 ILE A 104 ILE A 120 PHE A 121 THR A 126
SITE 3 AC2 23 SER A 127 SER A 128 ASN A 129 GLY A 140
SITE 4 AC2 23 ARG A 141 ASN A 142 GLY A 143 TYR A 144
SITE 5 AC2 23 GLY A 145 ALA A 146 LYS A 147 THR A 195
SITE 6 AC2 23 GLN A 365 LYS A 367 MG A1201
SITE 1 AC3 3 GLU F 66 ASN F 70 ANP F1202
SITE 1 AC4 23 ASN F 70 ASN F 74 ARG F 77 ASN F 99
SITE 2 AC4 23 ILE F 104 ILE F 120 PHE F 121 THR F 126
SITE 3 AC4 23 SER F 127 SER F 128 ASN F 129 GLY F 140
SITE 4 AC4 23 ARG F 141 ASN F 142 GLY F 143 TYR F 144
SITE 5 AC4 23 GLY F 145 ALA F 146 LYS F 147 THR F 195
SITE 6 AC4 23 GLN F 365 LYS F 367 MG F1201
CRYST1 169.135 169.884 169.212 90.00 90.00 90.00 P 21 21 21 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 0.005912 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005886 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005910 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
