HEADER REPLICATION ACTIVATOR/DNA 23-MAR-11 3R8F
TITLE REPLICATION INITIATOR DNAA BOUND TO AMPPCP AND SINGLE-STRANDED DNA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDUES 76-399;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: 5'-D(P*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*AP*A)-3';
COMPND 8 CHAIN: E;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS;
SOURCE 3 ORGANISM_TAXID: 63363;
SOURCE 4 STRAIN: VF5;
SOURCE 5 GENE: AQ_322, DNAA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS AAA+ ATPASE, REPLICATION INITIATOR, DNA BINDING, REPLICATION
KEYWDS 2 ACTIVATOR-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.E.DUDERSTADT,K.CHUANG,J.M.BERGER
REVDAT 5 09-SEP-15 3R8F 1 TITLE
REVDAT 4 28-MAR-12 3R8F 1 JRNL
REVDAT 3 22-FEB-12 3R8F 1 HET HETATM HETNAM HETSYN
REVDAT 3 2 1 REMARK
REVDAT 2 19-OCT-11 3R8F 1 JRNL
REVDAT 1 28-SEP-11 3R8F 0
JRNL AUTH K.E.DUDERSTADT,K.CHUANG,J.M.BERGER
JRNL TITL DNA STRETCHING BY BACTERIAL INITIATORS PROMOTES REPLICATION
JRNL TITL 2 ORIGIN OPENING.
JRNL REF NATURE V. 478 209 2011
JRNL REFN ISSN 0028-0836
JRNL PMID 21964332
JRNL DOI 10.1038/NATURE10455
REMARK 2
REMARK 2 RESOLUTION. 3.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5
REMARK 3 NUMBER OF REFLECTIONS : 32803
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.250
REMARK 3 R VALUE (WORKING SET) : 0.249
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1663
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 43.4907 - 7.6926 0.96 2704 133 0.2179 0.2132
REMARK 3 2 7.6926 - 6.1113 0.98 2634 138 0.2785 0.3035
REMARK 3 3 6.1113 - 5.3403 0.99 2610 150 0.2848 0.3437
REMARK 3 4 5.3403 - 4.8528 0.99 2605 151 0.2069 0.2459
REMARK 3 5 4.8528 - 4.5053 0.99 2600 133 0.2035 0.2304
REMARK 3 6 4.5053 - 4.2399 0.99 2606 145 0.2262 0.2231
REMARK 3 7 4.2399 - 4.0277 1.00 2596 150 0.2270 0.2507
REMARK 3 8 4.0277 - 3.8525 1.00 2598 138 0.2719 0.3157
REMARK 3 9 3.8525 - 3.7043 1.00 2587 125 0.2733 0.2896
REMARK 3 10 3.7043 - 3.5765 1.00 2589 146 0.2783 0.2847
REMARK 3 11 3.5765 - 3.4648 1.00 2573 124 0.3293 0.3180
REMARK 3 12 3.4648 - 3.3660 0.94 2438 130 0.3823 0.4161
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 : 0.31
REMARK 3 B_SOL : 66.67
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.460
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.720
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 85.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.18040
REMARK 3 B22 (A**2) : 20.58500
REMARK 3 B33 (A**2) : -14.40460
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 : 0.009 11529
REMARK 3 ANGLE : 0.864 14840
REMARK 3 CHIRALITY : 0.043 1648
REMARK 3 PLANARITY : 0.003 1812
REMARK 3 DIHEDRAL : 18.557 4397
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 77:241
REMARK 3 ORIGIN FOR THE GROUP (A): -14.6757 -16.3973 19.6790
REMARK 3 T TENSOR
REMARK 3 T11: 0.3701 T22: 0.3710
REMARK 3 T33: 0.3382 T12: 0.0811
REMARK 3 T13: -0.0096 T23: -0.0930
REMARK 3 L TENSOR
REMARK 3 L11: 2.1393 L22: 0.4722
REMARK 3 L33: 3.5563 L12: 0.8747
REMARK 3 L13: -1.0151 L23: 0.9902
REMARK 3 S TENSOR
REMARK 3 S11: -0.1180 S12: 0.1314 S13: 0.0687
REMARK 3 S21: 0.0426 S22: -0.1731 S23: 0.1148
REMARK 3 S31: 0.0075 S32: -0.1450 S33: -0.0010
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain B and resseq 77:241
REMARK 3 ORIGIN FOR THE GROUP (A): -32.1692 -2.1246 38.9260
REMARK 3 T TENSOR
REMARK 3 T11: 0.4641 T22: 0.4578
REMARK 3 T33: 0.4839 T12: 0.0768
REMARK 3 T13: -0.0509 T23: -0.1861
REMARK 3 L TENSOR
REMARK 3 L11: 0.9257 L22: 1.2143
REMARK 3 L33: 3.9970 L12: 1.3978
REMARK 3 L13: 0.2035 L23: 1.0032
REMARK 3 S TENSOR
REMARK 3 S11: 0.0711 S12: -0.0748 S13: 0.1333
REMARK 3 S21: 0.1542 S22: -0.1934 S23: 0.1188
REMARK 3 S31: 0.1878 S32: 0.0808 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain C and resseq 77:241
REMARK 3 ORIGIN FOR THE GROUP (A): -30.7053 11.8644 64.9840
REMARK 3 T TENSOR
REMARK 3 T11: 0.5288 T22: 0.4717
REMARK 3 T33: 0.5118 T12: -0.0605
REMARK 3 T13: -0.0061 T23: -0.1805
REMARK 3 L TENSOR
REMARK 3 L11: 2.9989 L22: 1.0709
REMARK 3 L33: 1.5975 L12: 1.9348
REMARK 3 L13: 1.2925 L23: 0.6769
REMARK 3 S TENSOR
REMARK 3 S11: 0.1704 S12: -0.0680 S13: 0.0578
REMARK 3 S21: 0.1012 S22: -0.2259 S23: 0.0264
REMARK 3 S31: -0.0726 S32: 0.0475 S33: 0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain D and resseq 77:241
REMARK 3 ORIGIN FOR THE GROUP (A): -11.2169 26.1137 82.3417
REMARK 3 T TENSOR
REMARK 3 T11: 0.3624 T22: 0.4275
REMARK 3 T33: 0.4076 T12: -0.0556
REMARK 3 T13: 0.0501 T23: -0.0346
REMARK 3 L TENSOR
REMARK 3 L11: 3.4186 L22: 0.6692
REMARK 3 L33: 2.0363 L12: 0.8104
REMARK 3 L13: -0.8330 L23: -1.2202
REMARK 3 S TENSOR
REMARK 3 S11: -0.2894 S12: -0.0578 S13: -0.1884
REMARK 3 S21: 0.0397 S22: -0.0456 S23: -0.1791
REMARK 3 S31: -0.0063 S32: -0.1389 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain A and resseq 242:290
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4129 -35.3195 -0.6690
REMARK 3 T TENSOR
REMARK 3 T11: 0.4661 T22: 0.7174
REMARK 3 T33: 0.6651 T12: 0.0598
REMARK 3 T13: 0.0348 T23: -0.3649
REMARK 3 L TENSOR
REMARK 3 L11: 0.7483 L22: 0.9002
REMARK 3 L33: 0.2699 L12: -0.7457
REMARK 3 L13: -0.2643 L23: 0.5283
REMARK 3 S TENSOR
REMARK 3 S11: 0.1740 S12: 0.3600 S13: -0.6917
REMARK 3 S21: 0.0622 S22: -0.1903 S23: -0.0955
REMARK 3 S31: -0.3332 S32: -0.5269 S33: -0.0000
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain B and resseq 242:290
REMARK 3 ORIGIN FOR THE GROUP (A): -40.6837 -20.6572 18.3254
REMARK 3 T TENSOR
REMARK 3 T11: 0.4938 T22: 0.6812
REMARK 3 T33: 0.6075 T12: -0.0498
REMARK 3 T13: 0.0167 T23: -0.3887
REMARK 3 L TENSOR
REMARK 3 L11: 1.2756 L22: 0.7532
REMARK 3 L33: 0.8708 L12: -0.6550
REMARK 3 L13: -0.1347 L23: 0.7408
REMARK 3 S TENSOR
REMARK 3 S11: -0.5914 S12: 0.0122 S13: -0.0311
REMARK 3 S21: -0.1745 S22: -0.0584 S23: 0.0070
REMARK 3 S31: 0.2652 S32: 0.0676 S33: -0.0012
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain C and resseq 242:290
REMARK 3 ORIGIN FOR THE GROUP (A): -51.1465 -6.7552 56.5918
REMARK 3 T TENSOR
REMARK 3 T11: 0.6447 T22: 0.7024
REMARK 3 T33: 0.8355 T12: -0.1750
REMARK 3 T13: 0.1798 T23: -0.4604
REMARK 3 L TENSOR
REMARK 3 L11: 0.7153 L22: 0.5794
REMARK 3 L33: 0.7056 L12: 0.6056
REMARK 3 L13: -0.0053 L23: 0.1170
REMARK 3 S TENSOR
REMARK 3 S11: 0.2503 S12: 0.6179 S13: -0.0271
REMARK 3 S21: -0.0205 S22: -0.6151 S23: 0.2241
REMARK 3 S31: 0.2876 S32: -0.4439 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain D and resseq 242:290
REMARK 3 ORIGIN FOR THE GROUP (A): -31.3556 7.1571 90.8350
REMARK 3 T TENSOR
REMARK 3 T11: 0.6387 T22: 0.7067
REMARK 3 T33: 0.5328 T12: -0.2912
REMARK 3 T13: 0.0042 T23: 0.0610
REMARK 3 L TENSOR
REMARK 3 L11: 0.8808 L22: 1.2567
REMARK 3 L33: 0.6307 L12: 1.1841
REMARK 3 L13: 0.2263 L23: 0.1357
REMARK 3 S TENSOR
REMARK 3 S11: 0.0253 S12: -0.1643 S13: 0.2782
REMARK 3 S21: -0.6309 S22: -0.0141 S23: 0.4643
REMARK 3 S31: 0.4594 S32: -1.1570 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain A and resseq 291:399
REMARK 3 ORIGIN FOR THE GROUP (A): -9.5168 -57.4281 16.3206
REMARK 3 T TENSOR
REMARK 3 T11: 0.1196 T22: 0.0972
REMARK 3 T33: 0.6063 T12: -0.0135
REMARK 3 T13: -0.0120 T23: -0.3072
REMARK 3 L TENSOR
REMARK 3 L11: 1.7722 L22: 2.1181
REMARK 3 L33: 3.6346 L12: 0.0437
REMARK 3 L13: 0.0237 L23: -2.0551
REMARK 3 S TENSOR
REMARK 3 S11: 0.6636 S12: -0.1458 S13: -0.1295
REMARK 3 S21: -0.4947 S22: -1.1891 S23: -0.3239
REMARK 3 S31: 0.4967 S32: 1.6215 S33: -0.2676
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain B and resseq 291:399
REMARK 3 ORIGIN FOR THE GROUP (A): -30.7741 -43.0580 32.2968
REMARK 3 T TENSOR
REMARK 3 T11: 0.8161 T22: 0.7502
REMARK 3 T33: 0.9783 T12: -0.1608
REMARK 3 T13: 0.2466 T23: -0.0436
REMARK 3 L TENSOR
REMARK 3 L11: 1.4233 L22: 0.7000
REMARK 3 L33: 0.7986 L12: 0.7110
REMARK 3 L13: -0.3664 L23: -0.5746
REMARK 3 S TENSOR
REMARK 3 S11: 0.3915 S12: -0.2321 S13: -0.4996
REMARK 3 S21: -0.3403 S22: -0.9482 S23: -0.1713
REMARK 3 S31: -0.6090 S32: 0.4811 S33: -0.0150
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain C and resseq 291:399
REMARK 3 ORIGIN FOR THE GROUP (A): -34.1015 -29.0465 58.9862
REMARK 3 T TENSOR
REMARK 3 T11: 1.7577 T22: 0.6546
REMARK 3 T33: 1.0636 T12: -0.3142
REMARK 3 T13: 0.1354 T23: 0.0171
REMARK 3 L TENSOR
REMARK 3 L11: 0.0339 L22: 0.1015
REMARK 3 L33: 0.7181 L12: 0.0556
REMARK 3 L13: 0.1699 L23: 0.1090
REMARK 3 S TENSOR
REMARK 3 S11: 0.2314 S12: 0.2514 S13: 0.3019
REMARK 3 S21: 0.2215 S22: -1.0286 S23: 0.1554
REMARK 3 S31: 0.4221 S32: -0.6550 S33: -0.0219
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain D and resseq 291:399
REMARK 3 ORIGIN FOR THE GROUP (A): -17.3476 -14.8751 80.4037
REMARK 3 T TENSOR
REMARK 3 T11: 1.3809 T22: 0.8531
REMARK 3 T33: 1.0923 T12: -0.1256
REMARK 3 T13: -0.0934 T23: 0.0778
REMARK 3 L TENSOR
REMARK 3 L11: 0.8919 L22: 0.2722
REMARK 3 L33: 0.0169 L12: -0.9275
REMARK 3 L13: 0.3077 L23: -0.0898
REMARK 3 S TENSOR
REMARK 3 S11: 0.2032 S12: -0.2571 S13: 0.7898
REMARK 3 S21: -0.2252 S22: -0.3069 S23: 0.3274
REMARK 3 S31: 0.7809 S32: -0.2687 S33: -0.0000
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : 1
REMARK 3 NCS GROUP : 1
REMARK 3 NCS OPERATOR : 1
REMARK 3 REFERENCE SELECTION: CHAIN B AND NOT RESSEQ 255:265
REMARK 3 SELECTION : CHAIN A AND NOT RESSEQ 255:265
REMARK 3 ATOM PAIRS NUMBER : 2552
REMARK 3 RMSD : 0.059
REMARK 3 NCS OPERATOR : 2
REMARK 3 REFERENCE SELECTION: CHAIN B AND NOT RESSEQ 255:265
REMARK 3 SELECTION : CHAIN C AND NOT RESSEQ 255:265
REMARK 3 ATOM PAIRS NUMBER : 2552
REMARK 3 RMSD : 0.056
REMARK 3 NCS OPERATOR : 3
REMARK 3 REFERENCE SELECTION: CHAIN B AND NOT RESSEQ 255:265
REMARK 3 SELECTION : CHAIN D AND NOT RESSEQ 255:265
REMARK 3 ATOM PAIRS NUMBER : 2552
REMARK 3 RMSD : 0.063
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3R8F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-11.
REMARK 100 THE RCSB ID CODE IS RCSB064619.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
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 : 32862
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.350
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 (%) : 98.9
REMARK 200 DATA REDUNDANCY : 3.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.47
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.61200
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: PHENIX (PHENIX.AUTOMR)
REMARK 200 STARTING MODEL: PDB ENTRY 2HCB
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-35 MM SODIUM CACODYLATE, PH 6.5,
REMARK 280 26% 1,2-PROPANEDIOL, 1-2% PEG2000 MME, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 291K
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 49.89850
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 100.63300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 57.10950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 100.63300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 49.89850
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 57.10950
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 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: PENTAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 LYS A 76
REMARK 465 ARG A 328
REMARK 465 LYS A 378
REMARK 465 LYS A 379
REMARK 465 ASP A 380
REMARK 465 LYS B 76
REMARK 465 ARG B 328
REMARK 465 LYS B 378
REMARK 465 LYS B 379
REMARK 465 ASP B 380
REMARK 465 LYS C 76
REMARK 465 ARG C 328
REMARK 465 LYS C 378
REMARK 465 LYS C 379
REMARK 465 ASP C 380
REMARK 465 LYS D 76
REMARK 465 ARG D 328
REMARK 465 LYS D 378
REMARK 465 LYS D 379
REMARK 465 ASP D 380
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 CA GLY B 124 O2A ACP B 700 2.11
REMARK 500 O2' ACP B 700 O HOH B 9 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU A 292 OD1 ASN B 258 4545 1.78
REMARK 500 OE1 GLU A 292 OE2 GLU B 260 4545 2.11
REMARK 500 OD1 ASN A 258 CB LYS B 263 4545 2.14
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 SER A 146 141.34 -170.78
REMARK 500 PRO A 217 -35.58 -37.16
REMARK 500 PHE A 311 -52.73 -125.25
REMARK 500 LYS A 330 0.62 83.80
REMARK 500 ASP A 362 -4.60 85.92
REMARK 500 SER B 146 141.37 -170.78
REMARK 500 PRO B 217 -35.68 -37.05
REMARK 500 LEU B 261 3.68 82.51
REMARK 500 PHE B 311 -52.76 -125.21
REMARK 500 LYS B 330 0.60 83.81
REMARK 500 ASP B 362 -4.62 85.94
REMARK 500 SER C 146 141.34 -170.77
REMARK 500 PRO C 217 -35.58 -37.12
REMARK 500 PHE C 311 -52.81 -125.17
REMARK 500 LYS C 330 0.54 83.88
REMARK 500 ASP C 362 -4.67 85.94
REMARK 500 SER D 146 141.33 -170.80
REMARK 500 PRO D 217 -35.66 -37.08
REMARK 500 PHE D 311 -52.81 -125.23
REMARK 500 LYS D 330 0.62 83.77
REMARK 500 ASP D 362 -4.60 85.94
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 D 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 126 OG1
REMARK 620 2 ACP D 700 O3G 105.5
REMARK 620 3 ACP D 700 O1B 55.2 60.0
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 126 OG1
REMARK 620 2 ACP C 700 O3G 104.1
REMARK 620 3 ACP C 700 O1B 57.2 60.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 126 OG1
REMARK 620 2 ACP B 700 O1G 100.7
REMARK 620 3 ACP B 700 O1B 59.8 57.1
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 401 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 126 OG1
REMARK 620 2 ACP A 700 O3G 99.7
REMARK 620 3 ACP A 700 O2B 55.4 56.0
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 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP A 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP C 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACP D 700
DBREF 3R8F A 76 399 UNP O66659 DNAA_AQUAE 76 399
DBREF 3R8F B 76 399 UNP O66659 DNAA_AQUAE 76 399
DBREF 3R8F C 76 399 UNP O66659 DNAA_AQUAE 76 399
DBREF 3R8F D 76 399 UNP O66659 DNAA_AQUAE 76 399
DBREF 3R8F E 1 12 PDB 3R8F 3R8F 1 12
SEQRES 1 A 324 LYS ASP PHE LEU ASN PRO LYS TYR THR LEU GLU ASN PHE
SEQRES 2 A 324 ILE VAL GLY GLU GLY ASN ARG LEU ALA TYR GLU VAL VAL
SEQRES 3 A 324 LYS GLU ALA LEU GLU ASN LEU GLY SER LEU TYR ASN PRO
SEQRES 4 A 324 ILE PHE ILE TYR GLY SER VAL GLY THR GLY LYS THR HIS
SEQRES 5 A 324 LEU LEU GLN ALA ALA GLY ASN GLU ALA LYS LYS ARG GLY
SEQRES 6 A 324 TYR ARG VAL ILE TYR SER SER ALA ASP ASP PHE ALA GLN
SEQRES 7 A 324 ALA MET VAL GLU HIS LEU LYS LYS GLY THR ILE ASN GLU
SEQRES 8 A 324 PHE ARG ASN MET TYR LYS SER VAL ASP LEU LEU LEU LEU
SEQRES 9 A 324 ASP ASP VAL GLN PHE LEU SER GLY LYS GLU ARG THR GLN
SEQRES 10 A 324 ILE GLU PHE PHE HIS ILE PHE ASN THR LEU TYR LEU LEU
SEQRES 11 A 324 GLU LYS GLN ILE ILE LEU ALA SER ASP ARG HIS PRO GLN
SEQRES 12 A 324 LYS LEU ASP GLY VAL SER ASP ARG LEU VAL SER ARG PHE
SEQRES 13 A 324 GLU GLY GLY ILE LEU VAL GLU ILE GLU LEU ASP ASN LYS
SEQRES 14 A 324 THR ARG PHE LYS ILE ILE LYS GLU LYS LEU LYS GLU PHE
SEQRES 15 A 324 ASN LEU GLU LEU ARG LYS GLU VAL ILE ASP TYR LEU LEU
SEQRES 16 A 324 GLU ASN THR LYS ASN VAL ARG GLU ILE GLU GLY LYS ILE
SEQRES 17 A 324 LYS LEU ILE LYS LEU LYS GLY PHE GLU GLY LEU GLU ARG
SEQRES 18 A 324 LYS GLU ARG LYS GLU ARG ASP LYS LEU MET GLN ILE VAL
SEQRES 19 A 324 GLU PHE VAL ALA ASN TYR TYR ALA VAL LYS VAL GLU ASP
SEQRES 20 A 324 ILE LEU SER ASP LYS ARG ASN LYS ARG THR SER GLU ALA
SEQRES 21 A 324 ARG LYS ILE ALA MET TYR LEU CYS ARG LYS VAL CYS SER
SEQRES 22 A 324 ALA SER LEU ILE GLU ILE ALA ARG ALA PHE LYS ARG LYS
SEQRES 23 A 324 ASP HIS THR THR VAL ILE HIS ALA ILE ARG SER VAL GLU
SEQRES 24 A 324 GLU GLU LYS LYS LYS ASP ARG LYS PHE LYS HIS LEU VAL
SEQRES 25 A 324 GLY PHE LEU GLU LYS GLN ALA PHE ASP LYS ILE CYS
SEQRES 1 B 324 LYS ASP PHE LEU ASN PRO LYS TYR THR LEU GLU ASN PHE
SEQRES 2 B 324 ILE VAL GLY GLU GLY ASN ARG LEU ALA TYR GLU VAL VAL
SEQRES 3 B 324 LYS GLU ALA LEU GLU ASN LEU GLY SER LEU TYR ASN PRO
SEQRES 4 B 324 ILE PHE ILE TYR GLY SER VAL GLY THR GLY LYS THR HIS
SEQRES 5 B 324 LEU LEU GLN ALA ALA GLY ASN GLU ALA LYS LYS ARG GLY
SEQRES 6 B 324 TYR ARG VAL ILE TYR SER SER ALA ASP ASP PHE ALA GLN
SEQRES 7 B 324 ALA MET VAL GLU HIS LEU LYS LYS GLY THR ILE ASN GLU
SEQRES 8 B 324 PHE ARG ASN MET TYR LYS SER VAL ASP LEU LEU LEU LEU
SEQRES 9 B 324 ASP ASP VAL GLN PHE LEU SER GLY LYS GLU ARG THR GLN
SEQRES 10 B 324 ILE GLU PHE PHE HIS ILE PHE ASN THR LEU TYR LEU LEU
SEQRES 11 B 324 GLU LYS GLN ILE ILE LEU ALA SER ASP ARG HIS PRO GLN
SEQRES 12 B 324 LYS LEU ASP GLY VAL SER ASP ARG LEU VAL SER ARG PHE
SEQRES 13 B 324 GLU GLY GLY ILE LEU VAL GLU ILE GLU LEU ASP ASN LYS
SEQRES 14 B 324 THR ARG PHE LYS ILE ILE LYS GLU LYS LEU LYS GLU PHE
SEQRES 15 B 324 ASN LEU GLU LEU ARG LYS GLU VAL ILE ASP TYR LEU LEU
SEQRES 16 B 324 GLU ASN THR LYS ASN VAL ARG GLU ILE GLU GLY LYS ILE
SEQRES 17 B 324 LYS LEU ILE LYS LEU LYS GLY PHE GLU GLY LEU GLU ARG
SEQRES 18 B 324 LYS GLU ARG LYS GLU ARG ASP LYS LEU MET GLN ILE VAL
SEQRES 19 B 324 GLU PHE VAL ALA ASN TYR TYR ALA VAL LYS VAL GLU ASP
SEQRES 20 B 324 ILE LEU SER ASP LYS ARG ASN LYS ARG THR SER GLU ALA
SEQRES 21 B 324 ARG LYS ILE ALA MET TYR LEU CYS ARG LYS VAL CYS SER
SEQRES 22 B 324 ALA SER LEU ILE GLU ILE ALA ARG ALA PHE LYS ARG LYS
SEQRES 23 B 324 ASP HIS THR THR VAL ILE HIS ALA ILE ARG SER VAL GLU
SEQRES 24 B 324 GLU GLU LYS LYS LYS ASP ARG LYS PHE LYS HIS LEU VAL
SEQRES 25 B 324 GLY PHE LEU GLU LYS GLN ALA PHE ASP LYS ILE CYS
SEQRES 1 C 324 LYS ASP PHE LEU ASN PRO LYS TYR THR LEU GLU ASN PHE
SEQRES 2 C 324 ILE VAL GLY GLU GLY ASN ARG LEU ALA TYR GLU VAL VAL
SEQRES 3 C 324 LYS GLU ALA LEU GLU ASN LEU GLY SER LEU TYR ASN PRO
SEQRES 4 C 324 ILE PHE ILE TYR GLY SER VAL GLY THR GLY LYS THR HIS
SEQRES 5 C 324 LEU LEU GLN ALA ALA GLY ASN GLU ALA LYS LYS ARG GLY
SEQRES 6 C 324 TYR ARG VAL ILE TYR SER SER ALA ASP ASP PHE ALA GLN
SEQRES 7 C 324 ALA MET VAL GLU HIS LEU LYS LYS GLY THR ILE ASN GLU
SEQRES 8 C 324 PHE ARG ASN MET TYR LYS SER VAL ASP LEU LEU LEU LEU
SEQRES 9 C 324 ASP ASP VAL GLN PHE LEU SER GLY LYS GLU ARG THR GLN
SEQRES 10 C 324 ILE GLU PHE PHE HIS ILE PHE ASN THR LEU TYR LEU LEU
SEQRES 11 C 324 GLU LYS GLN ILE ILE LEU ALA SER ASP ARG HIS PRO GLN
SEQRES 12 C 324 LYS LEU ASP GLY VAL SER ASP ARG LEU VAL SER ARG PHE
SEQRES 13 C 324 GLU GLY GLY ILE LEU VAL GLU ILE GLU LEU ASP ASN LYS
SEQRES 14 C 324 THR ARG PHE LYS ILE ILE LYS GLU LYS LEU LYS GLU PHE
SEQRES 15 C 324 ASN LEU GLU LEU ARG LYS GLU VAL ILE ASP TYR LEU LEU
SEQRES 16 C 324 GLU ASN THR LYS ASN VAL ARG GLU ILE GLU GLY LYS ILE
SEQRES 17 C 324 LYS LEU ILE LYS LEU LYS GLY PHE GLU GLY LEU GLU ARG
SEQRES 18 C 324 LYS GLU ARG LYS GLU ARG ASP LYS LEU MET GLN ILE VAL
SEQRES 19 C 324 GLU PHE VAL ALA ASN TYR TYR ALA VAL LYS VAL GLU ASP
SEQRES 20 C 324 ILE LEU SER ASP LYS ARG ASN LYS ARG THR SER GLU ALA
SEQRES 21 C 324 ARG LYS ILE ALA MET TYR LEU CYS ARG LYS VAL CYS SER
SEQRES 22 C 324 ALA SER LEU ILE GLU ILE ALA ARG ALA PHE LYS ARG LYS
SEQRES 23 C 324 ASP HIS THR THR VAL ILE HIS ALA ILE ARG SER VAL GLU
SEQRES 24 C 324 GLU GLU LYS LYS LYS ASP ARG LYS PHE LYS HIS LEU VAL
SEQRES 25 C 324 GLY PHE LEU GLU LYS GLN ALA PHE ASP LYS ILE CYS
SEQRES 1 D 324 LYS ASP PHE LEU ASN PRO LYS TYR THR LEU GLU ASN PHE
SEQRES 2 D 324 ILE VAL GLY GLU GLY ASN ARG LEU ALA TYR GLU VAL VAL
SEQRES 3 D 324 LYS GLU ALA LEU GLU ASN LEU GLY SER LEU TYR ASN PRO
SEQRES 4 D 324 ILE PHE ILE TYR GLY SER VAL GLY THR GLY LYS THR HIS
SEQRES 5 D 324 LEU LEU GLN ALA ALA GLY ASN GLU ALA LYS LYS ARG GLY
SEQRES 6 D 324 TYR ARG VAL ILE TYR SER SER ALA ASP ASP PHE ALA GLN
SEQRES 7 D 324 ALA MET VAL GLU HIS LEU LYS LYS GLY THR ILE ASN GLU
SEQRES 8 D 324 PHE ARG ASN MET TYR LYS SER VAL ASP LEU LEU LEU LEU
SEQRES 9 D 324 ASP ASP VAL GLN PHE LEU SER GLY LYS GLU ARG THR GLN
SEQRES 10 D 324 ILE GLU PHE PHE HIS ILE PHE ASN THR LEU TYR LEU LEU
SEQRES 11 D 324 GLU LYS GLN ILE ILE LEU ALA SER ASP ARG HIS PRO GLN
SEQRES 12 D 324 LYS LEU ASP GLY VAL SER ASP ARG LEU VAL SER ARG PHE
SEQRES 13 D 324 GLU GLY GLY ILE LEU VAL GLU ILE GLU LEU ASP ASN LYS
SEQRES 14 D 324 THR ARG PHE LYS ILE ILE LYS GLU LYS LEU LYS GLU PHE
SEQRES 15 D 324 ASN LEU GLU LEU ARG LYS GLU VAL ILE ASP TYR LEU LEU
SEQRES 16 D 324 GLU ASN THR LYS ASN VAL ARG GLU ILE GLU GLY LYS ILE
SEQRES 17 D 324 LYS LEU ILE LYS LEU LYS GLY PHE GLU GLY LEU GLU ARG
SEQRES 18 D 324 LYS GLU ARG LYS GLU ARG ASP LYS LEU MET GLN ILE VAL
SEQRES 19 D 324 GLU PHE VAL ALA ASN TYR TYR ALA VAL LYS VAL GLU ASP
SEQRES 20 D 324 ILE LEU SER ASP LYS ARG ASN LYS ARG THR SER GLU ALA
SEQRES 21 D 324 ARG LYS ILE ALA MET TYR LEU CYS ARG LYS VAL CYS SER
SEQRES 22 D 324 ALA SER LEU ILE GLU ILE ALA ARG ALA PHE LYS ARG LYS
SEQRES 23 D 324 ASP HIS THR THR VAL ILE HIS ALA ILE ARG SER VAL GLU
SEQRES 24 D 324 GLU GLU LYS LYS LYS ASP ARG LYS PHE LYS HIS LEU VAL
SEQRES 25 D 324 GLY PHE LEU GLU LYS GLN ALA PHE ASP LYS ILE CYS
SEQRES 1 E 12 DA DA DA DA DA DA DA DA DA DA DA DA
HET MG A 401 1
HET ACP A 700 31
HET MG B 401 1
HET ACP B 700 31
HET MG C 401 1
HET ACP C 700 31
HET MG D 401 1
HET ACP D 700 31
HETNAM MG MAGNESIUM ION
HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
FORMUL 6 MG 4(MG 2+)
FORMUL 7 ACP 4(C11 H18 N5 O12 P3)
FORMUL 14 HOH *22(H2 O)
HELIX 1 1 ASN A 94 ASN A 107 1 14
HELIX 2 2 GLY A 124 ARG A 139 1 16
HELIX 3 3 ALA A 148 LYS A 161 1 14
HELIX 4 4 THR A 163 SER A 173 1 11
HELIX 5 5 ASP A 181 SER A 186 5 6
HELIX 6 6 LYS A 188 LEU A 205 1 18
HELIX 7 7 HIS A 216 LEU A 220 5 5
HELIX 8 8 SER A 224 GLY A 233 1 10
HELIX 9 9 ASP A 242 PHE A 257 1 16
HELIX 10 10 ARG A 262 THR A 273 1 12
HELIX 11 11 ASN A 275 GLY A 290 1 16
HELIX 12 12 GLY A 290 LYS A 304 1 15
HELIX 13 13 MET A 306 PHE A 311 1 6
HELIX 14 14 PHE A 311 TYR A 316 1 6
HELIX 15 15 LYS A 319 SER A 325 1 7
HELIX 16 16 THR A 332 VAL A 346 1 15
HELIX 17 17 SER A 350 LYS A 359 1 10
HELIX 18 18 THR A 364 GLU A 376 1 13
HELIX 19 19 LYS A 382 CYS A 399 1 18
HELIX 20 20 ASN B 94 ASN B 107 1 14
HELIX 21 21 GLY B 124 ARG B 139 1 16
HELIX 22 22 ALA B 148 LYS B 161 1 14
HELIX 23 23 THR B 163 SER B 173 1 11
HELIX 24 24 ASP B 181 SER B 186 5 6
HELIX 25 25 LYS B 188 LEU B 205 1 18
HELIX 26 26 HIS B 216 LEU B 220 5 5
HELIX 27 27 SER B 224 GLY B 233 1 10
HELIX 28 28 ASP B 242 PHE B 257 1 16
HELIX 29 29 ARG B 262 THR B 273 1 12
HELIX 30 30 ASN B 275 GLY B 290 1 16
HELIX 31 31 GLY B 290 LYS B 304 1 15
HELIX 32 32 MET B 306 PHE B 311 1 6
HELIX 33 33 PHE B 311 TYR B 316 1 6
HELIX 34 34 LYS B 319 SER B 325 1 7
HELIX 35 35 THR B 332 VAL B 346 1 15
HELIX 36 36 SER B 350 LYS B 359 1 10
HELIX 37 37 THR B 364 GLU B 376 1 13
HELIX 38 38 LYS B 382 CYS B 399 1 18
HELIX 39 39 ASN C 94 ASN C 107 1 14
HELIX 40 40 GLY C 124 ARG C 139 1 16
HELIX 41 41 ALA C 148 LYS C 161 1 14
HELIX 42 42 THR C 163 SER C 173 1 11
HELIX 43 43 ASP C 181 SER C 186 5 6
HELIX 44 44 LYS C 188 LEU C 205 1 18
HELIX 45 45 HIS C 216 LEU C 220 5 5
HELIX 46 46 SER C 224 GLY C 233 1 10
HELIX 47 47 ASP C 242 PHE C 257 1 16
HELIX 48 48 ARG C 262 THR C 273 1 12
HELIX 49 49 ASN C 275 GLY C 290 1 16
HELIX 50 50 GLY C 290 LYS C 304 1 15
HELIX 51 51 MET C 306 PHE C 311 1 6
HELIX 52 52 PHE C 311 TYR C 316 1 6
HELIX 53 53 LYS C 319 SER C 325 1 7
HELIX 54 54 THR C 332 VAL C 346 1 15
HELIX 55 55 SER C 350 LYS C 359 1 10
HELIX 56 56 THR C 364 GLU C 376 1 13
HELIX 57 57 LYS C 382 CYS C 399 1 18
HELIX 58 58 ASN D 94 ASN D 107 1 14
HELIX 59 59 GLY D 124 ARG D 139 1 16
HELIX 60 60 ALA D 148 LYS D 161 1 14
HELIX 61 61 THR D 163 SER D 173 1 11
HELIX 62 62 ASP D 181 SER D 186 5 6
HELIX 63 63 LYS D 188 LEU D 205 1 18
HELIX 64 64 HIS D 216 LEU D 220 5 5
HELIX 65 65 SER D 224 GLY D 233 1 10
HELIX 66 66 ASP D 242 PHE D 257 1 16
HELIX 67 67 ARG D 262 THR D 273 1 12
HELIX 68 68 ASN D 275 GLY D 290 1 16
HELIX 69 69 GLY D 290 LYS D 304 1 15
HELIX 70 70 MET D 306 PHE D 311 1 6
HELIX 71 71 PHE D 311 TYR D 316 1 6
HELIX 72 72 LYS D 319 SER D 325 1 7
HELIX 73 73 THR D 332 VAL D 346 1 15
HELIX 74 74 SER D 350 LYS D 359 1 10
HELIX 75 75 THR D 364 GLU D 376 1 13
HELIX 76 76 LYS D 382 CYS D 399 1 18
SHEET 1 A 5 VAL A 143 SER A 147 0
SHEET 2 A 5 LEU A 176 ASP A 180 1 O LEU A 178 N ILE A 144
SHEET 3 A 5 GLN A 208 SER A 213 1 O ILE A 210 N LEU A 177
SHEET 4 A 5 PRO A 114 GLY A 119 1 N ILE A 115 O LEU A 211
SHEET 5 A 5 ILE A 235 ILE A 239 1 O ILE A 235 N PHE A 116
SHEET 1 B 5 VAL B 143 SER B 147 0
SHEET 2 B 5 LEU B 176 ASP B 180 1 O LEU B 178 N ILE B 144
SHEET 3 B 5 GLN B 208 SER B 213 1 O ILE B 210 N LEU B 177
SHEET 4 B 5 PRO B 114 GLY B 119 1 N ILE B 115 O LEU B 211
SHEET 5 B 5 ILE B 235 ILE B 239 1 O ILE B 235 N PHE B 116
SHEET 1 C 5 VAL C 143 SER C 147 0
SHEET 2 C 5 LEU C 176 ASP C 180 1 O LEU C 178 N ILE C 144
SHEET 3 C 5 GLN C 208 SER C 213 1 O ILE C 210 N LEU C 177
SHEET 4 C 5 PRO C 114 GLY C 119 1 N ILE C 115 O LEU C 211
SHEET 5 C 5 ILE C 235 ILE C 239 1 O ILE C 235 N PHE C 116
SHEET 1 D 5 VAL D 143 SER D 147 0
SHEET 2 D 5 LEU D 176 ASP D 180 1 O LEU D 178 N ILE D 144
SHEET 3 D 5 GLN D 208 SER D 213 1 O ILE D 210 N LEU D 177
SHEET 4 D 5 PRO D 114 GLY D 119 1 N ILE D 115 O LEU D 211
SHEET 5 D 5 ILE D 235 ILE D 239 1 O ILE D 235 N PHE D 116
LINK OG1 THR D 126 MG MG D 401 1555 1555 2.50
LINK OG1 THR C 126 MG MG C 401 1555 1555 2.50
LINK OG1 THR B 126 MG MG B 401 1555 1555 2.50
LINK OG1 THR A 126 MG MG A 401 1555 1555 2.50
LINK MG MG D 401 O3G ACP D 700 1555 1555 1.79
LINK MG MG A 401 O3G ACP A 700 1555 1555 2.05
LINK MG MG C 401 O3G ACP C 700 1555 1555 2.07
LINK MG MG B 401 O1G ACP B 700 1555 1555 2.30
LINK MG MG C 401 O1B ACP C 700 1555 1555 2.47
LINK MG MG B 401 O1B ACP B 700 1555 1555 2.51
LINK MG MG D 401 O1B ACP D 700 1555 1555 2.61
LINK MG MG A 401 O2B ACP A 700 1555 1555 2.73
SITE 1 AC1 4 THR A 126 ASP A 180 ASP A 181 ACP A 700
SITE 1 AC2 19 HOH A 3 TYR A 83 ASN A 87 PHE A 88
SITE 2 AC2 19 ILE A 89 ASN A 94 VAL A 121 GLY A 122
SITE 3 AC2 19 THR A 123 GLY A 124 LYS A 125 THR A 126
SITE 4 AC2 19 HIS A 127 LYS A 253 VAL A 276 ARG A 277
SITE 5 AC2 19 GLU A 280 MG A 401 ARG D 230
SITE 1 AC3 4 THR B 126 ASP B 180 ASP B 181 ACP B 700
SITE 1 AC4 18 ARG A 230 HOH B 9 TYR B 83 ASN B 87
SITE 2 AC4 18 PHE B 88 ILE B 89 VAL B 121 GLY B 122
SITE 3 AC4 18 THR B 123 GLY B 124 LYS B 125 THR B 126
SITE 4 AC4 18 HIS B 127 LYS B 253 VAL B 276 ARG B 277
SITE 5 AC4 18 GLU B 280 MG B 401
SITE 1 AC5 4 THR C 126 ASP C 180 ASP C 181 ACP C 700
SITE 1 AC6 17 ARG B 230 ASN C 87 PHE C 88 ILE C 89
SITE 2 AC6 17 ASN C 94 VAL C 121 GLY C 122 THR C 123
SITE 3 AC6 17 GLY C 124 LYS C 125 THR C 126 HIS C 127
SITE 4 AC6 17 LYS C 253 VAL C 276 ARG C 277 GLU C 280
SITE 5 AC6 17 MG C 401
SITE 1 AC7 4 THR D 126 ASP D 180 ASP D 181 ACP D 700
SITE 1 AC8 19 ARG C 230 HOH D 22 TYR D 83 ASN D 87
SITE 2 AC8 19 PHE D 88 ILE D 89 ASN D 94 VAL D 121
SITE 3 AC8 19 GLY D 122 THR D 123 GLY D 124 LYS D 125
SITE 4 AC8 19 THR D 126 HIS D 127 LYS D 253 VAL D 276
SITE 5 AC8 19 ARG D 277 GLU D 280 MG D 401
CRYST1 99.797 114.219 201.266 90.00 90.00 90.00 P 21 21 21 16
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 0.010020 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008755 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004969 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
