HEADER STRUCTURAL PROTEIN 26-MAR-07 2P9U
TITLE CRYSTAL STRUCTURE OF BOVINE ARP2/3 COMPLEX CO-CRYSTALLIZED WITH AMP-
TITLE 2 PNP AND CALCIUM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTIN-LIKE PROTEIN 3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACTIN-RELATED PROTEIN 3;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: ACTIN-LIKE PROTEIN 2;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: ACTIN-RELATED PROTEIN 2;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: ACTIN-RELATED PROTEIN 2/3 COMPLEX SUBUNIT 1B;
COMPND 13 CHAIN: C;
COMPND 14 SYNONYM: ARP2/3 COMPLEX 41 KDA SUBUNIT, P41-ARC;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: ACTIN-RELATED PROTEIN 2/3 COMPLEX SUBUNIT 2;
COMPND 18 CHAIN: D;
COMPND 19 SYNONYM: ARP2/3 COMPLEX 34 KDA SUBUNIT, P34-ARC;
COMPND 20 ENGINEERED: YES;
COMPND 21 MOL_ID: 5;
COMPND 22 MOLECULE: ACTIN-RELATED PROTEIN 2/3 COMPLEX SUBUNIT 3;
COMPND 23 CHAIN: E;
COMPND 24 SYNONYM: ARP2/3 COMPLEX 21 KDA SUBUNIT, P21-ARC;
COMPND 25 ENGINEERED: YES;
COMPND 26 MOL_ID: 6;
COMPND 27 MOLECULE: ACTIN-RELATED PROTEIN 2/3 COMPLEX SUBUNIT 4;
COMPND 28 CHAIN: F;
COMPND 29 SYNONYM: ARP2/3 COMPLEX 20 KDA SUBUNIT, P20-ARC;
COMPND 30 ENGINEERED: YES;
COMPND 31 MOL_ID: 7;
COMPND 32 MOLECULE: ACTIN-RELATED PROTEIN 2/3 COMPLEX SUBUNIT 5;
COMPND 33 CHAIN: G;
COMPND 34 SYNONYM: ARP2/3 COMPLEX 16 KDA SUBUNIT, P16-ARC;
COMPND 35 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: ACTR3;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 8 ORGANISM_COMMON: CATTLE;
SOURCE 9 ORGANISM_TAXID: 9913;
SOURCE 10 GENE: ACTR2;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 13 ORGANISM_COMMON: CATTLE;
SOURCE 14 ORGANISM_TAXID: 9913;
SOURCE 15 GENE: ARPC1B;
SOURCE 16 MOL_ID: 4;
SOURCE 17 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 18 ORGANISM_COMMON: CATTLE;
SOURCE 19 ORGANISM_TAXID: 9913;
SOURCE 20 GENE: ARPC2;
SOURCE 21 MOL_ID: 5;
SOURCE 22 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 23 ORGANISM_COMMON: CATTLE;
SOURCE 24 ORGANISM_TAXID: 9913;
SOURCE 25 GENE: ARPC3;
SOURCE 26 MOL_ID: 6;
SOURCE 27 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 28 ORGANISM_COMMON: CATTLE;
SOURCE 29 ORGANISM_TAXID: 9913;
SOURCE 30 GENE: ARPC4;
SOURCE 31 MOL_ID: 7;
SOURCE 32 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 33 ORGANISM_COMMON: CATTLE;
SOURCE 34 ORGANISM_TAXID: 9913;
SOURCE 35 GENE: ARPC5
KEYWDS ACTIN, WD REPEAT, COMPLEX, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR B.J.NOLEN,T.D.POLLARD
REVDAT 5 21-FEB-24 2P9U 1 REMARK SEQADV LINK
REVDAT 4 18-OCT-17 2P9U 1 REMARK
REVDAT 3 24-MAR-09 2P9U 1 SOURCE DBREF
REVDAT 2 24-FEB-09 2P9U 1 VERSN
REVDAT 1 29-MAY-07 2P9U 0
JRNL AUTH B.J.NOLEN,T.D.POLLARD
JRNL TITL INSIGHTS INTO THE INFLUENCE OF NUCLEOTIDES ON ACTIN FAMILY
JRNL TITL 2 PROTEINS FROM SEVEN STRUCTURES OF ARP2/3 COMPLEX.
JRNL REF MOL.CELL V. 26 449 2007
JRNL REFN ISSN 1097-2765
JRNL PMID 17499050
JRNL DOI 10.1016/J.MOLCEL.2007.04.017
REMARK 2
REMARK 2 RESOLUTION. 2.75 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 94.5
REMARK 3 NUMBER OF REFLECTIONS : 72729
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 3684
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13403
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 252
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 45.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 9.38300
REMARK 3 B22 (A**2) : 2.61700
REMARK 3 B33 (A**2) : -12.00000
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 33.43
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : CNS_TOPPAR:PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : CNS_TOPPAR:ION.PARAM
REMARK 3 PARAMETER FILE 3 : ANP.PARAM
REMARK 3 PARAMETER FILE 4 : CNS_TOPPAR:WATER.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2P9U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-07.
REMARK 100 THE DEPOSITION ID IS D_1000042147.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934
REMARK 200 MONOCHROMATOR : SI111
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 76237
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.750
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.9
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.4
REMARK 200 DATA REDUNDANCY IN SHELL : 3.50
REMARK 200 R MERGE FOR SHELL (I) : 0.41100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.33
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 7.5% PEG3350 50MM HEPES 100MM KSCN 10%
REMARK 280 SUCROSE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K, PH 7
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 55.56100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 101.90050
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 64.67750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 101.90050
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 55.56100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 64.67750
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: HEPTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 21750 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 67510 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G
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 ALA A 2
REMARK 465 SER A 40
REMARK 465 ALA A 41
REMARK 465 LYS A 42
REMARK 465 VAL A 43
REMARK 465 GLY A 44
REMARK 465 ASP A 45
REMARK 465 GLN A 46
REMARK 465 ALA A 47
REMARK 465 GLN A 48
REMARK 465 ARG A 49
REMARK 465 ARG A 50
REMARK 465 ARG A 156
REMARK 465 GLY A 355
REMARK 465 GLY A 356
REMARK 465 ARG A 357
REMARK 465 LEU A 358
REMARK 465 MET A 417
REMARK 465 SER A 418
REMARK 465 MET B 1
REMARK 465 ASP B 2
REMARK 465 SER B 3
REMARK 465 GLN B 4
REMARK 465 GLY B 5
REMARK 465 ARG B 6
REMARK 465 LYS B 7
REMARK 465 VAL B 8
REMARK 465 VAL B 9
REMARK 465 VAL B 10
REMARK 465 CYS B 11
REMARK 465 ASP B 12
REMARK 465 ASN B 13
REMARK 465 GLY B 14
REMARK 465 THR B 15
REMARK 465 GLY B 16
REMARK 465 PHE B 17
REMARK 465 VAL B 18
REMARK 465 LYS B 19
REMARK 465 CYS B 20
REMARK 465 GLY B 21
REMARK 465 TYR B 22
REMARK 465 ALA B 23
REMARK 465 GLY B 24
REMARK 465 SER B 25
REMARK 465 ASN B 26
REMARK 465 PHE B 27
REMARK 465 PRO B 28
REMARK 465 GLU B 29
REMARK 465 HIS B 30
REMARK 465 ILE B 31
REMARK 465 PHE B 32
REMARK 465 PRO B 33
REMARK 465 ALA B 34
REMARK 465 LEU B 35
REMARK 465 VAL B 36
REMARK 465 GLY B 37
REMARK 465 ARG B 38
REMARK 465 PRO B 39
REMARK 465 ILE B 40
REMARK 465 ILE B 41
REMARK 465 ARG B 42
REMARK 465 SER B 43
REMARK 465 THR B 44
REMARK 465 THR B 45
REMARK 465 LYS B 46
REMARK 465 VAL B 47
REMARK 465 GLY B 48
REMARK 465 ASN B 49
REMARK 465 ILE B 50
REMARK 465 GLU B 51
REMARK 465 ILE B 52
REMARK 465 LYS B 53
REMARK 465 ASP B 54
REMARK 465 LEU B 55
REMARK 465 MET B 56
REMARK 465 VAL B 57
REMARK 465 GLY B 58
REMARK 465 ASP B 59
REMARK 465 GLU B 60
REMARK 465 ALA B 61
REMARK 465 SER B 62
REMARK 465 GLU B 63
REMARK 465 LEU B 64
REMARK 465 ARG B 65
REMARK 465 SER B 66
REMARK 465 MET B 67
REMARK 465 LEU B 68
REMARK 465 GLU B 69
REMARK 465 VAL B 70
REMARK 465 ASN B 71
REMARK 465 TYR B 72
REMARK 465 PRO B 73
REMARK 465 MET B 74
REMARK 465 GLU B 75
REMARK 465 ASN B 76
REMARK 465 GLY B 77
REMARK 465 ILE B 78
REMARK 465 VAL B 79
REMARK 465 ARG B 80
REMARK 465 ASN B 81
REMARK 465 TRP B 82
REMARK 465 ASP B 83
REMARK 465 ASP B 84
REMARK 465 MET B 85
REMARK 465 LYS B 86
REMARK 465 HIS B 87
REMARK 465 LEU B 88
REMARK 465 TRP B 89
REMARK 465 ASP B 90
REMARK 465 TYR B 91
REMARK 465 THR B 92
REMARK 465 PHE B 93
REMARK 465 GLY B 94
REMARK 465 PRO B 95
REMARK 465 GLU B 96
REMARK 465 LYS B 97
REMARK 465 LEU B 98
REMARK 465 ASN B 99
REMARK 465 ILE B 100
REMARK 465 ASP B 101
REMARK 465 THR B 102
REMARK 465 ARG B 103
REMARK 465 ASN B 104
REMARK 465 CYS B 105
REMARK 465 LYS B 106
REMARK 465 ILE B 107
REMARK 465 LEU B 108
REMARK 465 LEU B 109
REMARK 465 ASN B 115
REMARK 465 PRO B 116
REMARK 465 THR B 117
REMARK 465 LYS B 118
REMARK 465 ASN B 119
REMARK 465 ARG B 120
REMARK 465 GLU B 121
REMARK 465 LYS B 122
REMARK 465 ILE B 123
REMARK 465 VAL B 124
REMARK 465 GLU B 125
REMARK 465 VAL B 126
REMARK 465 MET B 127
REMARK 465 PHE B 128
REMARK 465 GLU B 129
REMARK 465 THR B 130
REMARK 465 TYR B 131
REMARK 465 GLN B 132
REMARK 465 PHE B 133
REMARK 465 SER B 134
REMARK 465 GLY B 135
REMARK 465 VAL B 136
REMARK 465 TYR B 137
REMARK 465 VAL B 138
REMARK 465 ALA B 139
REMARK 465 ALA B 148
REMARK 465 GLY B 358
REMARK 465 ALA B 359
REMARK 465 VAL B 360
REMARK 465 LEU B 361
REMARK 465 ALA B 362
REMARK 465 ASP B 363
REMARK 465 ILE B 364
REMARK 465 MET B 365
REMARK 465 LYS B 366
REMARK 465 ASP B 367
REMARK 465 LYS B 368
REMARK 465 ASP B 369
REMARK 465 ASN B 370
REMARK 465 PHE B 371
REMARK 465 TRP B 372
REMARK 465 MET B 373
REMARK 465 THR B 374
REMARK 465 ARG B 375
REMARK 465 GLN B 376
REMARK 465 GLU B 377
REMARK 465 TYR B 378
REMARK 465 GLN B 379
REMARK 465 GLU B 380
REMARK 465 LYS B 381
REMARK 465 GLY B 382
REMARK 465 VAL B 383
REMARK 465 ARG B 384
REMARK 465 VAL B 385
REMARK 465 LEU B 386
REMARK 465 GLU B 387
REMARK 465 LYS B 388
REMARK 465 LEU B 389
REMARK 465 GLY B 390
REMARK 465 VAL B 391
REMARK 465 THR B 392
REMARK 465 VAL B 393
REMARK 465 ARG B 394
REMARK 465 MET C 1
REMARK 465 LYS C 289
REMARK 465 GLN C 290
REMARK 465 SER C 291
REMARK 465 SER C 292
REMARK 465 GLN C 293
REMARK 465 ARG C 294
REMARK 465 GLY C 295
REMARK 465 LEU C 296
REMARK 465 THR C 297
REMARK 465 ALA C 298
REMARK 465 ARG C 299
REMARK 465 GLU C 300
REMARK 465 ARG C 301
REMARK 465 PHE C 302
REMARK 465 GLN C 303
REMARK 465 ASN C 304
REMARK 465 LEU C 305
REMARK 465 ASP C 306
REMARK 465 LYS C 307
REMARK 465 LYS C 308
REMARK 465 ALA C 309
REMARK 465 SER C 310
REMARK 465 SER C 311
REMARK 465 GLU C 312
REMARK 465 GLY C 313
REMARK 465 SER C 314
REMARK 465 ALA C 315
REMARK 465 ALA C 316
REMARK 465 ALA C 317
REMARK 465 GLY C 318
REMARK 465 LYS D 210
REMARK 465 ASP D 211
REMARK 465 ASP D 283
REMARK 465 ALA D 284
REMARK 465 GLU D 285
REMARK 465 LYS D 286
REMARK 465 LYS D 287
REMARK 465 GLU D 288
REMARK 465 MET D 289
REMARK 465 LYS D 290
REMARK 465 THR D 291
REMARK 465 ILE D 292
REMARK 465 THR D 293
REMARK 465 GLY D 294
REMARK 465 LYS D 295
REMARK 465 THR D 296
REMARK 465 PHE D 297
REMARK 465 SER D 298
REMARK 465 SER D 299
REMARK 465 ARG D 300
REMARK 465 MET E 1
REMARK 465 PRO E 176
REMARK 465 GLY E 177
REMARK 465 GLN E 178
REMARK 465 MET F 1
REMARK 465 MET G 1
REMARK 465 SER G 2
REMARK 465 LYS G 3
REMARK 465 ASN G 4
REMARK 465 THR G 5
REMARK 465 VAL G 6
REMARK 465 SER G 7
REMARK 465 SER G 8
REMARK 465 ASP G 28
REMARK 465 ASP G 29
REMARK 465 GLY G 30
REMARK 465 GLY G 31
REMARK 465 ASP G 32
REMARK 465 GLY G 33
REMARK 465 GLN G 34
REMARK 465 ALA G 35
REMARK 465 GLY G 36
REMARK 465 PRO G 37
REMARK 465 ASP G 38
REMARK 465 GLU G 39
REMARK 465 GLY G 40
REMARK 465 GLU G 41
REMARK 465 VAL G 42
REMARK 465 ASP G 43
REMARK 465 SER G 44
REMARK 465 CYS G 45
REMARK 465 LEU G 46
REMARK 465 ARG G 47
REMARK 465 GLN G 48
REMARK 465 GLY G 49
REMARK 465 ASN G 50
REMARK 465 ILE G 64
REMARK 465 ASN G 65
REMARK 465 THR G 66
REMARK 465 LYS G 67
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 ARG A 161 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 259 CG1 CG2 CD1
REMARK 470 ILE A 262 CG1 CG2 CD1
REMARK 470 THR B 110 OG1 CG2
REMARK 470 GLU B 111 CG CD OE1 OE2
REMARK 470 PRO B 112 CG CD
REMARK 470 MET B 114 CG SD CE
REMARK 470 ILE B 140 CG1 CG2 CD1
REMARK 470 GLN B 141 CG CD OE1 NE2
REMARK 470 VAL B 143 CG1 CG2
REMARK 470 LEU B 144 CG CD1 CD2
REMARK 470 TYR B 147 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 149 CG CD OE1 NE2
REMARK 470 LEU B 152 CG CD1 CD2
REMARK 470 PHE B 173 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASN B 272 CG OD1 ND2
REMARK 470 LYS B 331 CG CD CE NZ
REMARK 470 VAL B 334 CG1 CG2
REMARK 470 GLU B 335 CG CD OE1 OE2
REMARK 470 LYS B 336 CG CD CE NZ
REMARK 470 SER B 338 OG
REMARK 470 LYS B 339 CG CD CE NZ
REMARK 470 LYS B 341 CG CD CE NZ
REMARK 470 ARG B 343 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 349 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 351 CG CD CE NZ
REMARK 470 HIS B 352 CG ND1 CD2 CE1 NE2
REMARK 470 LEU B 356 CG CD1 CD2
REMARK 470 ARG C 84 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 87 CG CD CE NZ
REMARK 470 ARG D 78 CG CD NE CZ NH1 NH2
REMARK 470 ARG G 10 CG CD NE CZ NH1 NH2
REMARK 470 LYS G 13 CG CD CE NZ
REMARK 470 GLN G 69 CG CD OE1 NE2
REMARK 470 LYS G 72 CG CD CE NZ
REMARK 470 ASP G 73 CG OD1 OD2
REMARK 470 ARG G 74 CG CD NE CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OG SER C 257 O ILE C 371 2.16
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 ILE C 11 N - CA - C ANGL. DEV. = -16.6 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 SER A 33 50.29 -66.77
REMARK 500 GLU A 65 -8.67 -55.65
REMARK 500 PRO A 70 -38.33 -36.08
REMARK 500 LEU A 117 33.28 71.77
REMARK 500 PRO A 194 31.59 -67.04
REMARK 500 ASP A 248 52.38 -104.87
REMARK 500 SER A 263 -34.24 175.73
REMARK 500 LYS A 264 -3.23 60.30
REMARK 500 ASP A 310 0.13 -59.73
REMARK 500 ASP A 330 2.14 58.60
REMARK 500 THR A 342 -32.21 -38.16
REMARK 500 LEU A 353 44.15 -76.00
REMARK 500 PRO A 412 127.82 -39.87
REMARK 500 THR B 145 -74.55 -41.87
REMARK 500 LEU B 146 -36.80 -34.90
REMARK 500 GLU B 171 53.23 26.99
REMARK 500 LEU B 178 -17.41 66.37
REMARK 500 ILE B 184 117.89 -177.98
REMARK 500 ALA B 185 -149.38 -141.98
REMARK 500 VAL B 278 -38.39 -29.83
REMARK 500 HIS B 300 39.87 -145.85
REMARK 500 VAL B 329 -41.87 -139.50
REMARK 500 LYS B 331 -8.06 64.48
REMARK 500 VAL B 334 34.73 -76.43
REMARK 500 ARG B 343 81.84 -152.80
REMARK 500 PRO B 347 104.81 -41.99
REMARK 500 ARG B 350 -10.46 -152.63
REMARK 500 GLU C 50 -37.01 -167.24
REMARK 500 ARG C 74 -12.83 76.49
REMARK 500 LYS C 138 -66.12 -102.24
REMARK 500 SER C 154 18.01 57.72
REMARK 500 LYS C 174 -7.11 -55.13
REMARK 500 ARG C 179 108.31 -11.68
REMARK 500 THR C 244 -168.15 -106.77
REMARK 500 CYS C 265 7.26 82.71
REMARK 500 LYS C 341 72.26 -156.18
REMARK 500 ASP C 368 30.79 -89.94
REMARK 500 GLU D 208 -18.05 -43.51
REMARK 500 ASP D 213 11.36 -68.17
REMARK 500 ALA D 234 5.80 -66.23
REMARK 500 ARG D 237 -70.02 -17.79
REMARK 500 PRO E 33 171.74 -53.90
REMARK 500 LYS E 37 -146.91 -106.34
REMARK 500 SER E 87 147.69 178.95
REMARK 500 PRO E 151 -14.43 -42.13
REMARK 500 ASN E 153 167.50 -42.03
REMARK 500 TRP E 160 -38.67 -131.85
REMARK 500 ASN E 170 15.51 56.81
REMARK 500 ASN F 56 -162.28 -167.81
REMARK 500 PHE F 101 76.11 -102.51
REMARK 500
REMARK 500 THIS ENTRY HAS 54 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR D 261 0.06 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 801 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ANP A 901 O2G
REMARK 620 2 ANP A 901 O1B 48.3
REMARK 620 3 HOH A 906 O 113.1 69.1
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 CA A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 902
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2P9I RELATED DB: PDB
REMARK 900 RELATED ID: 2P9L RELATED DB: PDB
REMARK 900 RELATED ID: 2P9K RELATED DB: PDB
REMARK 900 RELATED ID: 2P9N RELATED DB: PDB
REMARK 900 RELATED ID: 2P9P RELATED DB: PDB
REMARK 900 RELATED ID: 2P9S RELATED DB: PDB
DBREF 2P9U A 1 418 UNP P61157 ARP3_BOVIN 1 418
DBREF 2P9U B 1 394 UNP A7MB62 ARP2_BOVIN 1 394
DBREF 2P9U C 1 372 UNP Q58CQ2 ARC1B_BOVIN 1 372
DBREF 2P9U D 1 300 UNP Q3MHR7 ARPC2_BOVIN 1 300
DBREF 2P9U E 1 178 UNP Q3T035 ARPC3_BOVIN 1 178
DBREF 2P9U F 1 168 UNP Q148J6 ARPC4_BOVIN 1 168
DBREF 2P9U G 1 151 UNP Q3SYX9 ARPC5_BOVIN 1 151
SEQADV 2P9U VAL C 58 UNP Q58CQ2 ILE 58 CONFLICT
SEQADV 2P9U ASP G 17 UNP Q3SYX9 GLY 17 CONFLICT
SEQADV 2P9U ASP G 28 UNP Q3SYX9 GLU 28 CONFLICT
SEQRES 1 A 418 MET ALA GLY ARG LEU PRO ALA CYS VAL VAL ASP CYS GLY
SEQRES 2 A 418 THR GLY TYR THR LYS LEU GLY TYR ALA GLY ASN THR GLU
SEQRES 3 A 418 PRO GLN PHE ILE ILE PRO SER CYS ILE ALA ILE LYS GLU
SEQRES 4 A 418 SER ALA LYS VAL GLY ASP GLN ALA GLN ARG ARG VAL MET
SEQRES 5 A 418 LYS GLY VAL ASP ASP LEU ASP PHE PHE ILE GLY ASP GLU
SEQRES 6 A 418 ALA ILE GLU LYS PRO THR TYR ALA THR LYS TRP PRO ILE
SEQRES 7 A 418 ARG HIS GLY ILE VAL GLU ASP TRP ASP LEU MET GLU ARG
SEQRES 8 A 418 PHE MET GLU GLN VAL ILE PHE LYS TYR LEU ARG ALA GLU
SEQRES 9 A 418 PRO GLU ASP HIS TYR PHE LEU LEU THR GLU PRO PRO LEU
SEQRES 10 A 418 ASN THR PRO GLU ASN ARG GLU TYR THR ALA GLU ILE MET
SEQRES 11 A 418 PHE GLU SER PHE ASN VAL PRO GLY LEU TYR ILE ALA VAL
SEQRES 12 A 418 GLN ALA VAL LEU ALA LEU ALA ALA SER TRP THR SER ARG
SEQRES 13 A 418 GLN VAL GLY GLU ARG THR LEU THR GLY THR VAL ILE ASP
SEQRES 14 A 418 SER GLY ASP GLY VAL THR HIS VAL ILE PRO VAL ALA GLU
SEQRES 15 A 418 GLY TYR VAL ILE GLY SER CYS ILE LYS HIS ILE PRO ILE
SEQRES 16 A 418 ALA GLY ARG ASP ILE THR TYR PHE ILE GLN GLN LEU LEU
SEQRES 17 A 418 ARG ASP ARG GLU VAL GLY ILE PRO PRO GLU GLN SER LEU
SEQRES 18 A 418 GLU THR ALA LYS ALA VAL LYS GLU ARG TYR SER TYR VAL
SEQRES 19 A 418 CYS PRO ASP LEU VAL LYS GLU PHE ASN LYS TYR ASP THR
SEQRES 20 A 418 ASP GLY SER LYS TRP ILE LYS GLN TYR THR GLY ILE ASN
SEQRES 21 A 418 ALA ILE SER LYS LYS GLU PHE SER ILE ASP VAL GLY TYR
SEQRES 22 A 418 GLU ARG PHE LEU GLY PRO GLU ILE PHE PHE HIS PRO GLU
SEQRES 23 A 418 PHE ALA ASN PRO ASP PHE THR GLN PRO ILE SER GLU VAL
SEQRES 24 A 418 VAL ASP GLU VAL ILE GLN ASN CYS PRO ILE ASP VAL ARG
SEQRES 25 A 418 ARG PRO LEU TYR LYS ASN ILE VAL LEU SER GLY GLY SER
SEQRES 26 A 418 THR MET PHE ARG ASP PHE GLY ARG ARG LEU GLN ARG ASP
SEQRES 27 A 418 LEU LYS ARG THR VAL ASP ALA ARG LEU LYS LEU SER GLU
SEQRES 28 A 418 GLU LEU SER GLY GLY ARG LEU LYS PRO LYS PRO ILE ASP
SEQRES 29 A 418 VAL GLN VAL ILE THR HIS HIS MET GLN ARG TYR ALA VAL
SEQRES 30 A 418 TRP PHE GLY GLY SER MET LEU ALA SER THR PRO GLU PHE
SEQRES 31 A 418 TYR GLN VAL CYS HIS THR LYS LYS ASP TYR GLU GLU ILE
SEQRES 32 A 418 GLY PRO SER ILE CYS ARG HIS ASN PRO VAL PHE GLY VAL
SEQRES 33 A 418 MET SER
SEQRES 1 B 394 MET ASP SER GLN GLY ARG LYS VAL VAL VAL CYS ASP ASN
SEQRES 2 B 394 GLY THR GLY PHE VAL LYS CYS GLY TYR ALA GLY SER ASN
SEQRES 3 B 394 PHE PRO GLU HIS ILE PHE PRO ALA LEU VAL GLY ARG PRO
SEQRES 4 B 394 ILE ILE ARG SER THR THR LYS VAL GLY ASN ILE GLU ILE
SEQRES 5 B 394 LYS ASP LEU MET VAL GLY ASP GLU ALA SER GLU LEU ARG
SEQRES 6 B 394 SER MET LEU GLU VAL ASN TYR PRO MET GLU ASN GLY ILE
SEQRES 7 B 394 VAL ARG ASN TRP ASP ASP MET LYS HIS LEU TRP ASP TYR
SEQRES 8 B 394 THR PHE GLY PRO GLU LYS LEU ASN ILE ASP THR ARG ASN
SEQRES 9 B 394 CYS LYS ILE LEU LEU THR GLU PRO PRO MET ASN PRO THR
SEQRES 10 B 394 LYS ASN ARG GLU LYS ILE VAL GLU VAL MET PHE GLU THR
SEQRES 11 B 394 TYR GLN PHE SER GLY VAL TYR VAL ALA ILE GLN ALA VAL
SEQRES 12 B 394 LEU THR LEU TYR ALA GLN GLY LEU LEU THR GLY VAL VAL
SEQRES 13 B 394 VAL ASP SER GLY ASP GLY VAL THR HIS ILE CYS PRO VAL
SEQRES 14 B 394 TYR GLU GLY PHE SER LEU PRO HIS LEU THR ARG ARG LEU
SEQRES 15 B 394 ASP ILE ALA GLY ARG ASP ILE THR ARG TYR LEU ILE LYS
SEQRES 16 B 394 LEU LEU LEU LEU ARG GLY TYR ALA PHE ASN HIS SER ALA
SEQRES 17 B 394 ASP PHE GLU THR VAL ARG MET ILE LYS GLU LYS LEU CYS
SEQRES 18 B 394 TYR VAL GLY TYR ASN ILE GLU GLN GLU GLN LYS LEU ALA
SEQRES 19 B 394 LEU GLU THR THR VAL LEU VAL GLU SER TYR THR LEU PRO
SEQRES 20 B 394 ASP GLY ARG ILE ILE LYS VAL GLY GLY GLU ARG PHE GLU
SEQRES 21 B 394 ALA PRO GLU ALA LEU PHE GLN PRO HIS LEU ILE ASN VAL
SEQRES 22 B 394 GLU GLY VAL GLY VAL ALA GLU LEU LEU PHE ASN THR ILE
SEQRES 23 B 394 GLN ALA ALA ASP ILE ASP THR ARG SER GLU PHE TYR LYS
SEQRES 24 B 394 HIS ILE VAL LEU SER GLY GLY SER THR MET TYR PRO GLY
SEQRES 25 B 394 LEU PRO SER ARG LEU GLU ARG GLU LEU LYS GLN LEU TYR
SEQRES 26 B 394 LEU GLU ARG VAL LEU LYS GLY ASP VAL GLU LYS LEU SER
SEQRES 27 B 394 LYS PHE LYS ILE ARG ILE GLU ASP PRO PRO ARG ARG LYS
SEQRES 28 B 394 HIS MET VAL PHE LEU GLY GLY ALA VAL LEU ALA ASP ILE
SEQRES 29 B 394 MET LYS ASP LYS ASP ASN PHE TRP MET THR ARG GLN GLU
SEQRES 30 B 394 TYR GLN GLU LYS GLY VAL ARG VAL LEU GLU LYS LEU GLY
SEQRES 31 B 394 VAL THR VAL ARG
SEQRES 1 C 372 MET ALA TYR HIS SER PHE LEU VAL GLU PRO ILE SER CYS
SEQRES 2 C 372 HIS ALA TRP ASN LYS ASP ARG THR GLN ILE ALA ILE CYS
SEQRES 3 C 372 PRO ASN ASN HIS GLU VAL HIS ILE TYR GLU LYS SER GLY
SEQRES 4 C 372 ASN LYS TRP VAL GLN VAL HIS GLU LEU LYS GLU HIS ASN
SEQRES 5 C 372 GLY GLN VAL THR GLY VAL ASP TRP ALA PRO ASP SER ASN
SEQRES 6 C 372 ARG ILE VAL THR CYS GLY THR ASP ARG ASN ALA TYR VAL
SEQRES 7 C 372 TRP THR LEU LYS GLY ARG THR TRP LYS PRO THR LEU VAL
SEQRES 8 C 372 ILE LEU ARG ILE ASN ARG ALA ALA ARG CYS VAL ARG TRP
SEQRES 9 C 372 ALA PRO ASN GLU LYS LYS PHE ALA VAL GLY SER GLY SER
SEQRES 10 C 372 ARG VAL ILE SER ILE CYS TYR PHE GLU GLN GLU ASN ASP
SEQRES 11 C 372 TRP TRP VAL CYS LYS HIS ILE LYS LYS PRO ILE ARG SER
SEQRES 12 C 372 THR VAL LEU SER LEU ASP TRP HIS PRO ASN SER VAL LEU
SEQRES 13 C 372 LEU ALA ALA GLY SER CYS ASP PHE LYS CYS ARG ILE PHE
SEQRES 14 C 372 SER ALA TYR ILE LYS GLU VAL GLU GLU ARG PRO ALA PRO
SEQRES 15 C 372 THR PRO TRP GLY SER LYS MET PRO PHE GLY GLU LEU MET
SEQRES 16 C 372 PHE GLU SER SER SER SER CYS GLY TRP VAL HIS GLY VAL
SEQRES 17 C 372 CYS PHE SER ALA ASN GLY SER ARG VAL ALA TRP VAL SER
SEQRES 18 C 372 HIS ASP SER THR VAL CYS LEU ALA ASP ALA ASP LYS LYS
SEQRES 19 C 372 MET ALA VAL ALA THR LEU ALA SER GLU THR LEU PRO LEU
SEQRES 20 C 372 LEU ALA VAL THR PHE ILE THR GLU SER SER LEU VAL ALA
SEQRES 21 C 372 ALA GLY HIS ASP CYS PHE PRO VAL LEU PHE THR TYR ASP
SEQRES 22 C 372 SER ALA ALA GLY LYS LEU SER PHE GLY GLY ARG LEU ASP
SEQRES 23 C 372 VAL PRO LYS GLN SER SER GLN ARG GLY LEU THR ALA ARG
SEQRES 24 C 372 GLU ARG PHE GLN ASN LEU ASP LYS LYS ALA SER SER GLU
SEQRES 25 C 372 GLY SER ALA ALA ALA GLY ALA GLY LEU ASP SER LEU HIS
SEQRES 26 C 372 LYS ASN SER VAL SER GLN ILE SER VAL LEU SER GLY GLY
SEQRES 27 C 372 LYS ALA LYS CYS SER GLN PHE CYS THR THR GLY MET ASP
SEQRES 28 C 372 GLY GLY MET SER ILE TRP ASP VAL ARG SER LEU GLU SER
SEQRES 29 C 372 ALA LEU LYS ASP LEU LYS ILE VAL
SEQRES 1 D 300 MET ILE LEU LEU GLU VAL ASN ASN ARG ILE ILE GLU GLU
SEQRES 2 D 300 THR LEU ALA LEU LYS PHE GLU ASN ALA ALA ALA GLY ASN
SEQRES 3 D 300 LYS PRO GLU ALA VAL GLU VAL THR PHE ALA ASP PHE ASP
SEQRES 4 D 300 GLY VAL LEU TYR HIS ILE SER ASN PRO ASN GLY ASP LYS
SEQRES 5 D 300 THR LYS VAL MET VAL SER ILE SER LEU LYS PHE TYR LYS
SEQRES 6 D 300 GLU LEU GLN ALA HIS GLY ALA ASP GLU LEU LEU LYS ARG
SEQRES 7 D 300 VAL TYR GLY SER TYR LEU VAL ASN PRO GLU SER GLY TYR
SEQRES 8 D 300 ASN VAL SER LEU LEU TYR ASP LEU GLU ASN LEU PRO ALA
SEQRES 9 D 300 SER LYS ASP SER ILE VAL HIS GLN ALA GLY MET LEU LYS
SEQRES 10 D 300 ARG ASN CYS PHE ALA SER VAL PHE GLU LYS TYR PHE GLN
SEQRES 11 D 300 PHE GLN GLU GLU GLY LYS GLU GLY GLU ASN ARG ALA VAL
SEQRES 12 D 300 ILE HIS TYR ARG ASP ASP GLU THR MET TYR VAL GLU SER
SEQRES 13 D 300 LYS LYS ASP ARG VAL THR VAL VAL PHE SER THR VAL PHE
SEQRES 14 D 300 LYS ASP ASP ASP ASP VAL VAL ILE GLY LYS VAL PHE MET
SEQRES 15 D 300 GLN GLU PHE LYS GLU GLY ARG ARG ALA SER HIS THR ALA
SEQRES 16 D 300 PRO GLN VAL LEU PHE SER HIS ARG GLU PRO PRO LEU GLU
SEQRES 17 D 300 LEU LYS ASP THR ASP ALA ALA VAL GLY ASP ASN ILE GLY
SEQRES 18 D 300 TYR ILE THR PHE VAL LEU PHE PRO ARG HIS THR ASN ALA
SEQRES 19 D 300 SER ALA ARG ASP ASN THR ILE ASN LEU ILE HIS THR PHE
SEQRES 20 D 300 ARG ASP TYR LEU HIS TYR HIS ILE LYS CYS SER LYS ALA
SEQRES 21 D 300 TYR ILE HIS THR ARG MET ARG ALA LYS THR SER ASP PHE
SEQRES 22 D 300 LEU LYS VAL LEU ASN ARG ALA ARG PRO ASP ALA GLU LYS
SEQRES 23 D 300 LYS GLU MET LYS THR ILE THR GLY LYS THR PHE SER SER
SEQRES 24 D 300 ARG
SEQRES 1 E 178 MET PRO ALA TYR HIS SER SER LEU MET ASP PRO ASP THR
SEQRES 2 E 178 LYS LEU ILE GLY ASN MET ALA LEU LEU PRO ILE ARG SER
SEQRES 3 E 178 GLN PHE LYS GLY PRO ALA PRO ARG GLU THR LYS ASP THR
SEQRES 4 E 178 ASP ILE VAL ASP GLU ALA ILE TYR TYR PHE LYS ALA ASN
SEQRES 5 E 178 VAL PHE PHE LYS ASN TYR GLU ILE LYS ASN GLU ALA ASP
SEQRES 6 E 178 ARG THR LEU ILE TYR ILE THR LEU TYR ILE SER GLU CYS
SEQRES 7 E 178 LEU LYS LYS LEU GLN LYS CYS ASN SER LYS SER GLN GLY
SEQRES 8 E 178 GLU LYS GLU MET TYR THR LEU GLY ILE THR ASN PHE PRO
SEQRES 9 E 178 ILE PRO GLY GLU PRO GLY PHE PRO LEU ASN ALA ILE TYR
SEQRES 10 E 178 ALA LYS PRO ALA ASN LYS GLN GLU ASP GLU VAL MET ARG
SEQRES 11 E 178 ALA TYR LEU GLN GLN LEU ARG GLN GLU THR GLY LEU ARG
SEQRES 12 E 178 LEU CYS GLU LYS VAL PHE ASP PRO GLN ASN ASP LYS PRO
SEQRES 13 E 178 SER LYS TRP TRP THR CYS PHE VAL LYS ARG GLN PHE MET
SEQRES 14 E 178 ASN LYS SER LEU SER GLY PRO GLY GLN
SEQRES 1 F 168 MET THR ALA THR LEU ARG PRO TYR LEU SER ALA VAL ARG
SEQRES 2 F 168 ALA THR LEU GLN ALA ALA LEU CYS LEU GLU ASN PHE SER
SEQRES 3 F 168 SER GLN VAL VAL GLU ARG HIS ASN LYS PRO GLU VAL GLU
SEQRES 4 F 168 VAL ARG SER SER LYS GLU LEU LEU LEU GLN PRO VAL THR
SEQRES 5 F 168 ILE SER ARG ASN GLU LYS GLU LYS VAL LEU ILE GLU GLY
SEQRES 6 F 168 SER ILE ASN SER VAL ARG VAL SER ILE ALA VAL LYS GLN
SEQRES 7 F 168 ALA ASP GLU ILE GLU LYS ILE LEU CYS HIS LYS PHE MET
SEQRES 8 F 168 ARG PHE MET MET MET ARG ALA GLU ASN PHE PHE ILE LEU
SEQRES 9 F 168 ARG ARG LYS PRO VAL GLU GLY TYR ASP ILE SER PHE LEU
SEQRES 10 F 168 ILE THR ASN PHE HIS THR GLU GLN MET TYR LYS HIS LYS
SEQRES 11 F 168 LEU VAL ASP PHE VAL ILE HIS PHE MET GLU GLU ILE ASP
SEQRES 12 F 168 LYS GLU ILE SER GLU MET LYS LEU SER VAL ASN ALA ARG
SEQRES 13 F 168 ALA ARG ILE VAL ALA GLU GLU PHE LEU LYS ASN PHE
SEQRES 1 G 151 MET SER LYS ASN THR VAL SER SER ALA ARG PHE ARG LYS
SEQRES 2 G 151 VAL ASP VAL ASP GLU TYR ASP GLU ASN LYS PHE VAL ASP
SEQRES 3 G 151 GLU ASP ASP GLY GLY ASP GLY GLN ALA GLY PRO ASP GLU
SEQRES 4 G 151 GLY GLU VAL ASP SER CYS LEU ARG GLN GLY ASN MET THR
SEQRES 5 G 151 ALA ALA LEU GLN ALA ALA LEU LYS ASN PRO PRO ILE ASN
SEQRES 6 G 151 THR LYS SER GLN ALA VAL LYS ASP ARG ALA GLY SER ILE
SEQRES 7 G 151 VAL LEU LYS VAL LEU ILE SER PHE LYS ALA ASN ASP ILE
SEQRES 8 G 151 GLU LYS ALA VAL GLN SER LEU ASP LYS ASN GLY VAL ASP
SEQRES 9 G 151 LEU LEU MET LYS TYR ILE TYR LYS GLY PHE GLU SER PRO
SEQRES 10 G 151 SER ASP ASN SER SER ALA VAL LEU LEU GLN TRP HIS GLU
SEQRES 11 G 151 LYS ALA LEU ALA ALA GLY GLY VAL GLY SER ILE VAL ARG
SEQRES 12 G 151 VAL LEU THR ALA ARG LYS THR VAL
HET CA A 801 1
HET ANP A 901 31
HET CA B 802 1
HET ANP B 902 31
HETNAM CA CALCIUM ION
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 8 CA 2(CA 2+)
FORMUL 9 ANP 2(C10 H17 N6 O12 P3)
FORMUL 12 HOH *252(H2 O)
HELIX 1 1 VAL A 55 LEU A 58 5 4
HELIX 2 2 ASP A 64 ILE A 67 5 4
HELIX 3 3 ASP A 85 LYS A 99 1 15
HELIX 4 4 GLU A 104 ASP A 107 5 4
HELIX 5 5 THR A 119 SER A 133 1 15
HELIX 6 6 GLN A 144 SER A 152 1 9
HELIX 7 7 TRP A 153 SER A 155 5 3
HELIX 8 8 GLY A 187 ILE A 190 5 4
HELIX 9 9 ALA A 196 GLU A 212 1 17
HELIX 10 10 PRO A 216 GLU A 218 5 3
HELIX 11 11 GLN A 219 TYR A 231 1 13
HELIX 12 12 ASP A 237 ASP A 248 1 12
HELIX 13 13 ASP A 248 ILE A 253 1 6
HELIX 14 14 TYR A 273 ILE A 281 1 9
HELIX 15 15 PHE A 282 PHE A 283 5 2
HELIX 16 16 HIS A 284 ALA A 288 5 5
HELIX 17 17 PRO A 295 CYS A 307 1 13
HELIX 18 18 PRO A 308 ASN A 318 1 11
HELIX 19 19 GLY A 323 MET A 327 5 5
HELIX 20 20 ASP A 330 SER A 350 1 21
HELIX 21 21 TYR A 375 SER A 386 1 12
HELIX 22 22 THR A 387 VAL A 393 1 7
HELIX 23 23 LYS A 397 GLY A 404 1 8
HELIX 24 24 PRO A 405 HIS A 410 5 6
HELIX 25 25 ILE B 140 TYR B 147 1 8
HELIX 26 26 ALA B 185 ARG B 200 1 16
HELIX 27 27 ASP B 209 CYS B 221 1 13
HELIX 28 28 ASN B 226 THR B 237 1 12
HELIX 29 29 GLY B 256 ALA B 261 1 6
HELIX 30 30 PRO B 262 PHE B 266 5 5
HELIX 31 31 GLN B 267 ASN B 272 5 6
HELIX 32 32 GLY B 277 ALA B 289 1 13
HELIX 33 33 ASP B 290 LYS B 299 1 10
HELIX 34 34 GLY B 305 MET B 309 5 5
HELIX 35 35 GLY B 312 VAL B 329 1 18
HELIX 36 36 LYS B 336 PHE B 340 5 5
HELIX 37 37 HIS B 352 GLY B 357 1 6
HELIX 38 38 ASP C 232 LYS C 234 5 3
HELIX 39 39 VAL C 359 LEU C 366 1 8
HELIX 40 40 ASN D 8 ALA D 24 1 17
HELIX 41 41 PRO D 48 ASP D 51 5 4
HELIX 42 42 PHE D 63 ALA D 69 1 7
HELIX 43 43 GLY D 71 GLY D 81 1 11
HELIX 44 44 LYS D 106 MET D 115 1 10
HELIX 45 45 MET D 115 GLU D 134 1 20
HELIX 46 46 ASP D 171 GLU D 187 1 17
HELIX 47 47 GLY D 188 ALA D 191 5 4
HELIX 48 48 PHE D 228 ASN D 233 1 6
HELIX 49 49 ALA D 236 HIS D 245 1 10
HELIX 50 50 THR D 246 ALA D 280 1 35
HELIX 51 51 ASP E 40 VAL E 53 1 14
HELIX 52 52 ASN E 62 GLN E 83 1 22
HELIX 53 53 SER E 87 THR E 101 1 15
HELIX 54 54 ASN E 122 PHE E 149 1 28
HELIX 55 55 SER E 157 CYS E 162 1 6
HELIX 56 56 GLN E 167 LYS E 171 5 5
HELIX 57 57 THR F 4 LEU F 20 1 17
HELIX 58 58 PRO F 36 ARG F 41 1 6
HELIX 59 59 SER F 43 LEU F 47 5 5
HELIX 60 60 ASP F 80 ARG F 97 1 18
HELIX 61 61 ASN F 120 MET F 126 1 7
HELIX 62 62 TYR F 127 LYS F 166 1 40
HELIX 63 63 ALA G 9 VAL G 14 5 6
HELIX 64 64 ASP G 15 ASP G 20 5 6
HELIX 65 65 MET G 51 LEU G 59 1 9
HELIX 66 66 SER G 68 SER G 85 1 18
HELIX 67 67 ASP G 90 GLN G 96 1 7
HELIX 68 68 ASP G 99 GLU G 115 1 17
HELIX 69 69 ASN G 120 GLY G 137 1 18
HELIX 70 70 GLY G 137 ALA G 147 1 11
SHEET 1 A 6 PHE A 29 PRO A 32 0
SHEET 2 A 6 TYR A 16 TYR A 21 -1 N THR A 17 O ILE A 31
SHEET 3 A 6 CYS A 8 CYS A 12 -1 N ASP A 11 O LYS A 18
SHEET 4 A 6 TYR A 109 GLU A 114 1 O TYR A 109 N CYS A 8
SHEET 5 A 6 GLY A 138 VAL A 143 1 O ALA A 142 N LEU A 112
SHEET 6 A 6 HIS A 395 THR A 396 -1 O HIS A 395 N LEU A 139
SHEET 1 B 3 PHE A 60 ILE A 62 0
SHEET 2 B 3 ILE A 35 ILE A 37 -1 N ALA A 36 O PHE A 61
SHEET 3 B 3 ALA A 73 LYS A 75 -1 O ALA A 73 N ILE A 37
SHEET 1 C 2 ILE A 78 ARG A 79 0
SHEET 2 C 2 ILE A 82 VAL A 83 -1 O ILE A 82 N ARG A 79
SHEET 1 D 3 TYR A 184 VAL A 185 0
SHEET 2 D 3 THR A 175 ALA A 181 -1 N ALA A 181 O TYR A 184
SHEET 3 D 3 LYS A 191 ILE A 193 -1 O LYS A 191 N VAL A 177
SHEET 1 E 5 TYR A 184 VAL A 185 0
SHEET 2 E 5 THR A 175 ALA A 181 -1 N ALA A 181 O TYR A 184
SHEET 3 E 5 GLY A 165 ASP A 169 -1 N ASP A 169 O HIS A 176
SHEET 4 E 5 ILE A 319 SER A 322 1 O VAL A 320 N THR A 166
SHEET 5 E 5 VAL A 367 ILE A 368 1 O ILE A 368 N ILE A 319
SHEET 1 F 2 LYS A 254 ILE A 259 0
SHEET 2 F 2 GLU A 266 VAL A 271 -1 O VAL A 271 N LYS A 254
SHEET 1 G 5 ARG B 180 LEU B 182 0
SHEET 2 G 5 THR B 164 VAL B 169 -1 N THR B 164 O LEU B 182
SHEET 3 G 5 GLY B 154 SER B 159 -1 N ASP B 158 O HIS B 165
SHEET 4 G 5 ILE B 301 SER B 304 1 O VAL B 302 N VAL B 155
SHEET 5 G 5 ILE B 344 GLU B 345 1 O GLU B 345 N ILE B 301
SHEET 1 H 2 GLU B 242 THR B 245 0
SHEET 2 H 2 ILE B 251 VAL B 254 -1 O ILE B 252 N TYR B 244
SHEET 1 I 4 TYR C 3 SER C 5 0
SHEET 2 I 4 GLY C 353 ASP C 358 -1 O MET C 354 N HIS C 4
SHEET 3 I 4 GLN C 344 GLY C 349 -1 N PHE C 345 O TRP C 357
SHEET 4 I 4 VAL C 329 SER C 336 -1 N SER C 333 O CYS C 346
SHEET 1 J 4 HIS C 14 TRP C 16 0
SHEET 2 J 4 GLN C 22 ILE C 25 -1 O ALA C 24 N ALA C 15
SHEET 3 J 4 GLU C 31 SER C 38 -1 O TYR C 35 N ILE C 23
SHEET 4 J 4 LYS C 41 LYS C 49 -1 O VAL C 43 N GLU C 36
SHEET 1 K 4 VAL C 55 ALA C 61 0
SHEET 2 K 4 ARG C 66 GLY C 71 -1 O VAL C 68 N ASP C 59
SHEET 3 K 4 ALA C 76 LYS C 82 -1 O TRP C 79 N ILE C 67
SHEET 4 K 4 THR C 85 VAL C 91 -1 O THR C 85 N LYS C 82
SHEET 1 L 4 ALA C 99 TRP C 104 0
SHEET 2 L 4 LYS C 110 SER C 115 -1 O GLY C 114 N ARG C 100
SHEET 3 L 4 ILE C 120 GLU C 126 -1 O CYS C 123 N PHE C 111
SHEET 4 L 4 TRP C 131 ILE C 137 -1 O TRP C 131 N GLU C 126
SHEET 1 M 4 VAL C 145 TRP C 150 0
SHEET 2 M 4 LEU C 156 SER C 161 -1 O ALA C 158 N ASP C 149
SHEET 3 M 4 CYS C 166 SER C 170 -1 O ARG C 167 N ALA C 159
SHEET 4 M 4 LEU C 194 GLU C 197 -1 O MET C 195 N ILE C 168
SHEET 1 N 4 VAL C 205 PHE C 210 0
SHEET 2 N 4 ARG C 216 SER C 221 -1 O ALA C 218 N CYS C 209
SHEET 3 N 4 THR C 225 ASP C 230 -1 O ALA C 229 N VAL C 217
SHEET 4 N 4 VAL C 237 ALA C 241 -1 O ALA C 238 N LEU C 228
SHEET 1 O 4 LEU C 247 PHE C 252 0
SHEET 2 O 4 SER C 257 GLY C 262 -1 O VAL C 259 N THR C 251
SHEET 3 O 4 VAL C 268 ASP C 273 -1 O PHE C 270 N LEU C 258
SHEET 4 O 4 LYS C 278 ARG C 284 -1 O LYS C 278 N ASP C 273
SHEET 1 P 5 GLU D 32 ASP D 37 0
SHEET 2 P 5 VAL D 41 SER D 46 -1 O TYR D 43 N PHE D 35
SHEET 3 P 5 LYS D 54 SER D 60 -1 O MET D 56 N SER D 46
SHEET 4 P 5 VAL D 93 ASP D 98 -1 O LEU D 95 N VAL D 57
SHEET 5 P 5 LEU D 84 VAL D 85 -1 N VAL D 85 O SER D 94
SHEET 1 Q 5 ALA D 142 ARG D 147 0
SHEET 2 Q 5 GLU D 150 SER D 156 -1 O MET D 152 N ILE D 144
SHEET 3 Q 5 VAL D 161 VAL D 168 -1 O SER D 166 N THR D 151
SHEET 4 Q 5 ILE D 220 LEU D 227 -1 O ILE D 223 N PHE D 165
SHEET 5 Q 5 GLN D 197 SER D 201 -1 N SER D 201 O TYR D 222
SHEET 1 R 2 LEU E 15 ILE E 16 0
SHEET 2 R 2 MET E 19 ALA E 20 -1 O MET E 19 N ILE E 16
SHEET 1 S 4 VAL F 51 SER F 54 0
SHEET 2 S 4 LYS F 60 SER F 66 -1 O ILE F 63 N VAL F 51
SHEET 3 S 4 SER F 69 ALA F 75 -1 O ARG F 71 N GLU F 64
SHEET 4 S 4 ILE F 114 THR F 119 -1 O ILE F 118 N VAL F 70
LINK CA CA A 801 O2G ANP A 901 1555 1555 2.73
LINK CA CA A 801 O1B ANP A 901 1555 1555 2.81
LINK CA CA A 801 O HOH A 906 1555 1555 3.04
LINK CA CA B 802 O3A ANP B 902 1555 1555 2.68
CISPEP 1 LYS C 139 PRO C 140 0 0.18
SITE 1 AC1 3 GLN A 144 ANP A 901 HOH A 906
SITE 1 AC2 1 ANP B 902
SITE 1 AC3 13 THR A 14 GLY A 15 TYR A 16 LYS A 18
SITE 2 AC3 13 GLY A 171 ASP A 172 GLY A 197 LYS A 228
SITE 3 AC3 13 GLU A 229 GLY A 324 PHE A 328 CA A 801
SITE 4 AC3 13 HOH A 913
SITE 1 AC4 13 GLY B 160 ASP B 161 GLY B 186 ARG B 214
SITE 2 AC4 13 LYS B 217 GLU B 218 GLY B 306 SER B 307
SITE 3 AC4 13 MET B 309 TYR B 310 CA B 802 HOH B 906
SITE 4 AC4 13 HOH B 909
CRYST1 111.122 129.355 203.801 90.00 90.00 90.00 P 21 21 21 4
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 0.008999 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007731 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004907 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
