HEADER HYDROLASE 04-JUL-02 1IXS
TITLE STRUCTURE OF RUVB COMPLEXED WITH RUVA DOMAIN III
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HOLLIDAY JUNCTION DNA HELICASE RUVA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RUVA DOMAIN III;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: RUVB;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: RESIDUES 1-318;
COMPND 10 EC: 3.6.1.3;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 3 ORGANISM_TAXID: 274;
SOURCE 4 GENE: RUVA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;
SOURCE 12 ORGANISM_TAXID: 274;
SOURCE 13 GENE: RUVB;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS HETERODIMERIC PROTEIN COMPLEX, AAA-ATPASE DOMAIN, COMPLEX WITH
KEYWDS 2 NUCLEOTIDE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.YAMADA,T.MIYATA,D.TSUCHIYA,T.OYAMA,Y.FUJIWARA,T.OHNISHI,H.IWASAKI,
AUTHOR 2 H.SHINAGAWA,M.ARIYOSHI,K.MAYANAGI,K.MORIKAWA
REVDAT 3 25-OCT-23 1IXS 1 REMARK
REVDAT 2 24-FEB-09 1IXS 1 VERSN
REVDAT 1 06-NOV-02 1IXS 0
JRNL AUTH K.YAMADA,T.MIYATA,D.TSUCHIYA,T.OYAMA,Y.FUJIWARA,T.OHNISHI,
JRNL AUTH 2 H.IWASAKI,H.SHINAGAWA,M.ARIYOSHI,K.MAYANAGI,K.MORIKAWA
JRNL TITL CRYSTAL STRUCTURE OF THE RUVA-RUVB COMPLEX: A STRUCTURAL
JRNL TITL 2 BASIS FOR THE HOLLIDAY JUNCTION MIGRATING MOTOR MACHINERY
JRNL REF MOL.CELL V. 10 671 2002
JRNL REFN ISSN 1097-2765
JRNL PMID 12408833
JRNL DOI 10.1016/S1097-2765(02)00641-X
REMARK 2
REMARK 2 RESOLUTION. 3.20 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) : 3.20
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
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) (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 12434
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.231
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 633
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) : 3.20
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.31
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3500
REMARK 3 BIN FREE R VALUE : 0.4718
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 59
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 : 2848
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 0
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) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.40
REMARK 3 ESD FROM SIGMAA (A) : 0.46
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.56
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.67
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.334
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
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 : NULL
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 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IXS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUL-02.
REMARK 100 THE DEPOSITION ID IS D_1000005383.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-NOV-01
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 : SPRING-8
REMARK 200 BEAMLINE : BL24XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.836
REMARK 200 MONOCHROMATOR : DIAMOND
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS V
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA, CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 235468
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.200
REMARK 200 RESOLUTION RANGE LOW (A) : 41.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 7.100
REMARK 200 R MERGE (I) : 0.09100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.37
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 7.30
REMARK 200 R MERGE FOR SHELL (I) : 0.32400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1HQC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, PH 8.0, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+3/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+1/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+3/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+1/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.87500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 51.03000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 51.03000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 103.31250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 51.03000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 51.03000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 34.43750
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 51.03000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.03000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 103.31250
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 51.03000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.03000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 34.43750
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 68.87500
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: THE BIOLOGICAL ASSEMBLY IS A
REMARK 300 HETERODIMER IN THE ASYMMETRIC
REMARK 300 UNIT.
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 130
REMARK 465 VAL A 131
REMARK 465 PRO A 132
REMARK 465 PRO A 133
REMARK 465 HIS A 134
REMARK 465 LEU A 135
REMARK 465 LEU A 136
REMARK 465 ALA A 137
REMARK 465 GLY A 138
REMARK 465 GLU A 139
REMARK 465 LYS A 140
REMARK 465 VAL A 141
REMARK 465 MET B 1
REMARK 465 GLU B 2
REMARK 465 ASP B 3
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 ALA B 5 9.90 -151.31
REMARK 500 LYS B 9 -51.79 -124.64
REMARK 500 GLN B 17 24.18 47.76
REMARK 500 LEU B 28 -82.88 -62.92
REMARK 500 GLU B 29 -19.73 -43.19
REMARK 500 ALA B 30 -70.18 -69.51
REMARK 500 ARG B 34 -119.69 -64.10
REMARK 500 LYS B 35 -95.87 -72.06
REMARK 500 GLU B 36 -20.03 -166.56
REMARK 500 ILE B 74 86.97 -63.52
REMARK 500 GLU B 90 104.95 -29.25
REMARK 500 GLU B 98 28.92 48.63
REMARK 500 ILE B 99 -11.95 -47.34
REMARK 500 GLU B 115 -75.02 -65.24
REMARK 500 GLN B 125 -167.64 -164.08
REMARK 500 ALA B 129 35.55 37.49
REMARK 500 THR B 146 16.83 -66.01
REMARK 500 ARG B 147 84.80 -177.07
REMARK 500 LEU B 150 92.70 -24.32
REMARK 500 ALA B 153 -144.22 -68.12
REMARK 500 MET B 178 -81.58 -55.36
REMARK 500 ASP B 180 -24.33 -167.78
REMARK 500 VAL B 186 120.94 -20.15
REMARK 500 ARG B 201 44.03 -68.68
REMARK 500 ALA B 218 -89.96 -64.38
REMARK 500 GLN B 219 -9.89 -40.67
REMARK 500 ALA B 221 -29.11 -151.00
REMARK 500 GLU B 223 -11.73 -154.57
REMARK 500 VAL B 225 145.81 -174.06
REMARK 500 VAL B 255 0.41 -63.65
REMARK 500 ILE B 257 -58.39 -151.38
REMARK 500 PRO B 264 95.47 -38.53
REMARK 500 THR B 269 7.33 -67.66
REMARK 500 ALA B 271 -72.90 -52.25
REMARK 500 SER B 275 90.50 49.48
REMARK 500 GLU B 276 168.37 175.52
REMARK 500 LEU B 281 49.55 -74.28
REMARK 500 GLU B 282 -35.87 -166.10
REMARK 500 VAL B 284 -52.63 -144.91
REMARK 500 LEU B 294 -2.89 -143.64
REMARK 500 PRO B 299 43.71 -70.43
REMARK 500 ARG B 300 -63.70 -148.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 319
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HQC RELATED DB: PDB
REMARK 900 1HQC CONTAINS RUVB ALONE.
REMARK 900 RELATED ID: 1IXR RELATED DB: PDB
REMARK 900 1IXR CONTAINS RUVB COMPLEXED WITH RUVA.
DBREF 1IXS A 130 191 UNP Q9F1Q3 RUVA_THET8 130 191
DBREF 1IXS B 1 318 UNP Q5SL87 RUVB_THET8 1 318
SEQRES 1 A 62 LYS VAL PRO PRO HIS LEU LEU ALA GLY GLU LYS VAL GLU
SEQRES 2 A 62 SER GLU ALA ALA GLU GLU ALA VAL MET ALA LEU ALA ALA
SEQRES 3 A 62 LEU GLY PHE LYS GLU ALA GLN ALA ARG ALA VAL VAL LEU
SEQRES 4 A 62 ASP LEU LEU ALA GLN ASN PRO LYS ALA ARG ALA GLN ASP
SEQRES 5 A 62 LEU ILE LYS GLU ALA LEU LYS ARG LEU ARG
SEQRES 1 B 318 MET GLU ASP LEU ALA LEU ARG PRO LYS THR LEU ASP GLU
SEQRES 2 B 318 TYR ILE GLY GLN GLU ARG LEU LYS GLN LYS LEU ARG VAL
SEQRES 3 B 318 TYR LEU GLU ALA ALA LYS ALA ARG LYS GLU PRO LEU GLU
SEQRES 4 B 318 HIS LEU LEU LEU PHE GLY PRO PRO GLY LEU GLY LYS THR
SEQRES 5 B 318 THR LEU ALA HIS VAL ILE ALA HIS GLU LEU GLY VAL ASN
SEQRES 6 B 318 LEU ARG VAL THR SER GLY PRO ALA ILE GLU LYS PRO GLY
SEQRES 7 B 318 ASP LEU ALA ALA ILE LEU ALA ASN SER LEU GLU GLU GLY
SEQRES 8 B 318 ASP ILE LEU PHE ILE ASP GLU ILE HIS ARG LEU SER ARG
SEQRES 9 B 318 GLN ALA GLU GLU HIS LEU TYR PRO ALA MET GLU ASP PHE
SEQRES 10 B 318 VAL MET ASP ILE VAL ILE GLY GLN GLY PRO ALA ALA ARG
SEQRES 11 B 318 THR ILE ARG LEU GLU LEU PRO ARG PHE THR LEU ILE GLY
SEQRES 12 B 318 ALA THR THR ARG PRO GLY LEU ILE THR ALA PRO LEU LEU
SEQRES 13 B 318 SER ARG PHE GLY ILE VAL GLU HIS LEU GLU TYR TYR THR
SEQRES 14 B 318 PRO GLU GLU LEU ALA GLN GLY VAL MET ARG ASP ALA ARG
SEQRES 15 B 318 LEU LEU GLY VAL ARG ILE THR GLU GLU ALA ALA LEU GLU
SEQRES 16 B 318 ILE GLY ARG ARG SER ARG GLY THR MET ARG VAL ALA LYS
SEQRES 17 B 318 ARG LEU PHE ARG ARG VAL ARG ASP PHE ALA GLN VAL ALA
SEQRES 18 B 318 GLY GLU GLU VAL ILE THR ARG GLU ARG ALA LEU GLU ALA
SEQRES 19 B 318 LEU ALA ALA LEU GLY LEU ASP GLU LEU GLY LEU GLU LYS
SEQRES 20 B 318 ARG ASP ARG GLU ILE LEU GLU VAL LEU ILE LEU ARG PHE
SEQRES 21 B 318 GLY GLY GLY PRO VAL GLY LEU ALA THR LEU ALA THR ALA
SEQRES 22 B 318 LEU SER GLU ASP PRO GLY THR LEU GLU GLU VAL HIS GLU
SEQRES 23 B 318 PRO TYR LEU ILE ARG GLN GLY LEU LEU LYS ARG THR PRO
SEQRES 24 B 318 ARG GLY ARG VAL ALA THR GLU LEU ALA TYR ARG HIS LEU
SEQRES 25 B 318 GLY TYR PRO PRO PRO VAL
HET ANP B 319 31
HETNAM ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FORMUL 3 ANP C10 H17 N6 O12 P3
HELIX 1 1 SER A 143 LEU A 156 1 14
HELIX 2 2 LYS A 159 ASN A 174 1 16
HELIX 3 3 ARG A 178 LYS A 188 1 11
HELIX 4 4 THR B 10 TYR B 14 5 5
HELIX 5 5 GLN B 17 LYS B 32 1 16
HELIX 6 6 GLY B 50 GLY B 63 1 14
HELIX 7 7 LYS B 76 ASN B 86 1 11
HELIX 8 8 GLU B 98 LEU B 102 5 5
HELIX 9 9 SER B 103 PHE B 117 1 15
HELIX 10 10 ALA B 153 PHE B 159 5 7
HELIX 11 11 THR B 169 ARG B 179 1 11
HELIX 12 12 ASP B 180 GLY B 185 5 6
HELIX 13 13 THR B 189 SER B 200 1 12
HELIX 14 14 THR B 203 GLN B 219 1 17
HELIX 15 15 THR B 227 GLY B 239 1 13
HELIX 16 16 GLU B 246 VAL B 255 1 10
HELIX 17 17 LEU B 267 THR B 272 1 6
HELIX 18 18 ALA B 273 SER B 275 5 3
HELIX 19 19 HIS B 285 GLN B 292 1 8
HELIX 20 20 THR B 305 GLY B 313 1 9
SHEET 1 A 5 LEU B 66 SER B 70 0
SHEET 2 A 5 ILE B 93 ASP B 97 1 O PHE B 95 N ARG B 67
SHEET 3 A 5 THR B 140 THR B 145 1 O ILE B 142 N LEU B 94
SHEET 4 A 5 LEU B 41 PHE B 44 1 N LEU B 43 O GLY B 143
SHEET 5 A 5 ILE B 161 HIS B 164 1 O GLU B 163 N PHE B 44
SHEET 1 B 2 VAL B 118 VAL B 122 0
SHEET 2 B 2 THR B 131 GLU B 135 -1 O ILE B 132 N ILE B 121
SHEET 1 C 2 LEU B 295 ARG B 297 0
SHEET 2 C 2 ARG B 302 ALA B 304 -1 O VAL B 303 N LYS B 296
SITE 1 AC1 11 ARG B 7 TYR B 14 ILE B 15 GLY B 50
SITE 2 AC1 11 LYS B 51 THR B 52 THR B 53 TYR B 168
SITE 3 AC1 11 MET B 204 ARG B 205 LYS B 208
CRYST1 102.060 102.060 137.750 90.00 90.00 90.00 P 43 21 2 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.009798 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009798 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007260 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
