HEADER UNKNOWN FUNCTION 16-OCT-14 4RLE
TITLE CRYSTAL STRUCTURE OF THE C-DI-AMP BINDING PII-LIKE PROTEIN DARA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UNCHARACTERIZED PROTEIN YAAQ;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: DARA;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 224308;
SOURCE 4 STRAIN: 168;
SOURCE 5 GENE: BSU00290, YAAQ;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PWH844
KEYWDS PII-LIKE, CDIAMP, UNKNOWN FUNCTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DICKMANNS,P.NEUMANN,R.FICNER
REVDAT 4 04-SEP-19 4RLE 1 REMARK
REVDAT 3 11-FEB-15 4RLE 1 JRNL
REVDAT 2 17-DEC-14 4RLE 1 JRNL
REVDAT 1 03-DEC-14 4RLE 0
JRNL AUTH J.GUNDLACH,A.DICKMANNS,K.SCHRODER-TITTMANN,P.NEUMANN,
JRNL AUTH 2 J.KAESLER,J.KAMPF,C.HERZBERG,E.HAMMER,F.SCHWEDE,V.KAEVER,
JRNL AUTH 3 K.TITTMANN,J.STULKE,R.FICNER
JRNL TITL IDENTIFICATION, CHARACTERIZATION, AND STRUCTURE ANALYSIS OF
JRNL TITL 2 THE CYCLIC DI-AMP-BINDING PII-LIKE SIGNAL TRANSDUCTION
JRNL TITL 3 PROTEIN DARA.
JRNL REF J.BIOL.CHEM. V. 290 3069 2015
JRNL REFN ISSN 0021-9258
JRNL PMID 25433025
JRNL DOI 10.1074/JBC.M114.619619
REMARK 2
REMARK 2 RESOLUTION. 1.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.46
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 26015
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.131
REMARK 3 R VALUE (WORKING SET) : 0.130
REMARK 3 FREE R VALUE : 0.155
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.500
REMARK 3 FREE R VALUE TEST SET COUNT : 911
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 37.4768 - 2.4866 1.00 3638 132 0.1406 0.1604
REMARK 3 2 2.4866 - 1.9737 1.00 3589 131 0.1417 0.1440
REMARK 3 3 1.9737 - 1.7242 1.00 3564 129 0.1136 0.1416
REMARK 3 4 1.7242 - 1.5666 1.00 3601 131 0.1030 0.1586
REMARK 3 5 1.5666 - 1.4543 1.00 3573 129 0.1017 0.1531
REMARK 3 6 1.4543 - 1.3686 1.00 3564 129 0.1088 0.1598
REMARK 3 7 1.3686 - 1.3000 1.00 3575 130 0.1167 0.1739
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.070
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 15.440
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 14.05
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.02
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 1092
REMARK 3 ANGLE : 1.469 1500
REMARK 3 CHIRALITY : 0.054 168
REMARK 3 PLANARITY : 0.008 192
REMARK 3 DIHEDRAL : 18.624 454
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ( CHAIN A AND RESID 74:88 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.963 5.402 108.046
REMARK 3 T TENSOR
REMARK 3 T11: 1.0871 T22: 0.3752
REMARK 3 T33: 1.3349 T12: 0.4224
REMARK 3 T13: -0.2868 T23: -0.0763
REMARK 3 L TENSOR
REMARK 3 L11: 3.1175 L22: 1.7071
REMARK 3 L33: 9.6702 L12: -0.0400
REMARK 3 L13: 4.5085 L23: 2.0682
REMARK 3 S TENSOR
REMARK 3 S11: -1.9985 S12: 3.4292 S13: 1.2309
REMARK 3 S21: -0.9388 S22: 1.0337 S23: -1.4214
REMARK 3 S31: -2.6943 S32: 2.1038 S33: -2.1361
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4RLE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000087490.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0-8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9100
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26017
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.300
REMARK 200 RESOLUTION RANGE LOW (A) : 37.461
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.02500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 38.8600
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.17600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 10.49
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3M05
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1-0.2 M SODIUM TARTRATE, 16-20%
REMARK 280 PEG5000, 10 MM DTT, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/2
REMARK 290 6555 X-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 29.10050
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 29.10050
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 29.10050
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -77.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 350 BIOMT1 2 -0.500000 -0.866025 0.000000 28.26050
REMARK 350 BIOMT2 2 0.866025 -0.500000 0.000000 48.94862
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 -0.500000 0.866025 0.000000 -28.26050
REMARK 350 BIOMT2 3 -0.866025 -0.500000 0.000000 48.94862
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 NI NI A 202 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 354 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 369 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 405 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 419 LIES ON A SPECIAL POSITION.
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 HIS A -7
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 O HOH A 306 O HOH A 424 2.10
REMARK 500 OG SER A 39 O HOH A 431 2.13
REMARK 500 O MET A 77 N GLY A 79 2.16
REMARK 500 O HOH A 443 O HOH A 444 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 86 C - N - CA ANGL. DEV. = 14.6 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 TYR A 84 -128.93 -102.24
REMARK 500 VAL A 85 90.06 35.81
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 NI A 202 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A -4 NE2
REMARK 620 2 HIS A -2 NE2 91.7
REMARK 620 N 1
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2BA A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 202
DBREF 4RLE A 1 109 UNP P37538 YAAQ_BACSU 1 109
SEQADV 4RLE HIS A -7 UNP P37538 EXPRESSION TAG
SEQADV 4RLE HIS A -6 UNP P37538 EXPRESSION TAG
SEQADV 4RLE HIS A -5 UNP P37538 EXPRESSION TAG
SEQADV 4RLE HIS A -4 UNP P37538 EXPRESSION TAG
SEQADV 4RLE HIS A -3 UNP P37538 EXPRESSION TAG
SEQADV 4RLE HIS A -2 UNP P37538 EXPRESSION TAG
SEQADV 4RLE GLY A -1 UNP P37538 EXPRESSION TAG
SEQADV 4RLE SER A 0 UNP P37538 EXPRESSION TAG
SEQRES 1 A 117 HIS HIS HIS HIS HIS HIS GLY SER MET LYS LEU ILE VAL
SEQRES 2 A 117 ALA VAL VAL GLN ASP GLN ASP SER ASN ARG LEU LEU LYS
SEQRES 3 A 117 THR LEU THR ASP HIS ASN PHE ARG VAL THR LYS LEU ALA
SEQRES 4 A 117 THR THR GLY GLY PHE LEU LYS SER GLY ASN THR THR PHE
SEQRES 5 A 117 MET ILE GLY VAL GLU ASP ILE ARG VAL ASN LYS ALA LEU
SEQRES 6 A 117 SER LEU ILE LYS GLU ASN GLY GLN LYS ARG ASP GLN MET
SEQRES 7 A 117 ILE ALA PRO VAL SER PRO MET GLY GLY ASN ALA ASP SER
SEQRES 8 A 117 TYR VAL PRO TYR PRO VAL GLU VAL GLU VAL GLY GLY ALA
SEQRES 9 A 117 THR VAL PHE VAL LEU PRO VAL ASP GLU PHE HIS GLN PHE
HET 2BA A 201 44
HET NI A 202 1
HETNAM 2BA (2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-2,9-BIS(6-
HETNAM 2 2BA AMINO-9H-PURIN-9-YL)OCTAHYDRO-2H,7H-DIFURO[3,2-D:3',
HETNAM 3 2BA 2'-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-3,5,
HETNAM 4 2BA 10,12-TETROL 5,12-DIOXIDE
HETNAM NI NICKEL (II) ION
HETSYN 2BA BIS-(3',5')-CYCLIC-DIMERIC-ADENOSINE-MONOPHOSPHATE
FORMUL 2 2BA C20 H24 N10 O12 P2
FORMUL 3 NI NI 2+
FORMUL 4 HOH *145(H2 O)
HELIX 1 1 GLN A 9 HIS A 23 1 15
HELIX 2 2 ARG A 52 GLY A 64 1 13
SHEET 1 A 4 THR A 28 THR A 33 0
SHEET 2 A 4 GLY A 40 GLU A 49 -1 O THR A 43 N LEU A 30
SHEET 3 A 4 MET A 1 VAL A 8 -1 N VAL A 8 O THR A 42
SHEET 4 A 4 ALA A 96 PRO A 102 -1 O THR A 97 N VAL A 7
SHEET 1 B 2 ARG A 67 MET A 70 0
SHEET 2 B 2 GLU A 90 VAL A 93 -1 O VAL A 93 N ARG A 67
LINK NE2 HIS A -4 NI NI A 202 1555 1555 2.16
LINK NE2 HIS A -2 NI NI A 202 1555 1555 2.19
SITE 1 AC1 23 VAL A 7 THR A 21 ASN A 24 PHE A 25
SITE 2 AC1 23 ARG A 26 VAL A 27 THR A 28 GLY A 34
SITE 3 AC1 23 GLY A 35 PHE A 36 LEU A 37 ASN A 41
SITE 4 AC1 23 MET A 45 GLY A 47 VAL A 91 GLU A 92
SITE 5 AC1 23 GLY A 94 THR A 97 HOH A 302 HOH A 304
SITE 6 AC1 23 HOH A 328 HOH A 416 HOH A 417
SITE 1 AC2 2 HIS A -2 HIS A -4
CRYST1 56.521 56.521 58.201 90.00 90.00 120.00 P 63 6
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 0.017693 0.010215 0.000000 0.00000
SCALE2 0.000000 0.020430 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017182 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
