HEADER HYDROLASE 02-MAY-06 2GV1
TITLE NMR SOLUTION STRUCTURE OF THE ACYLPHOSPHATASE FROM ESCHAERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE ACYLPHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ACYLPHOSPHATE PHOSPHOHYDROLASE;
COMPND 5 EC: 3.6.1.7;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: YCCX;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GLOBULAR ALPHA-HELIX/BETA-SHEET PROTEIN, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.PAGANO,A.CORAZZA,P.VIGLINO,G.ESPOSITO
REVDAT 4 09-MAR-22 2GV1 1 REMARK
REVDAT 3 24-FEB-09 2GV1 1 VERSN
REVDAT 2 21-NOV-06 2GV1 1 JRNL
REVDAT 1 31-OCT-06 2GV1 0
JRNL AUTH K.PAGANO,M.RAMAZZOTTI,P.VIGLINO,G.ESPOSITO,D.DEGL'INNOCENTI,
JRNL AUTH 2 N.TADDEI,A.CORAZZA
JRNL TITL NMR SOLUTION STRUCTURE OF THE ACYLPHOSPHATASE FROM
JRNL TITL 2 ESCHERICHIA COLI.
JRNL REF J.BIOMOL.NMR V. 36 199 2006
JRNL REFN ISSN 0925-2738
JRNL PMID 17021943
JRNL DOI 10.1007/S10858-006-9073-2
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.CORAZZA,C.ROSANO,K.PAGANO,V.ALVERDI,G.ESPOSITO,C.CAPANNI,
REMARK 1 AUTH 2 F.BEMPORAD,G.PLAKOUTSI,M.STEFANI,F.CHITI,S.ZUCCOTTI,
REMARK 1 AUTH 3 M.BOLOGNESI,P.VIGLINO
REMARK 1 TITL STRUCTURE, CONFORMATIONAL STABILITY, AND ENZYMATIC
REMARK 1 TITL 2 PROPERTIES OF ACYLPHOSPHATASE FROM THE HYPERTHERMOPHILE
REMARK 1 TITL 3 SULFOLOBUS SOLFATARICUS
REMARK 1 REF PROTEINS V. 62 64 2006
REMARK 1 REFN ISSN 0887-3585
REMARK 1 PMID 16287076
REMARK 1 DOI 10.1002/PROT.20703
REMARK 1 REFERENCE 2
REMARK 1 AUTH M.M.THUNNISSEN,N.TADDEI,G.LIGURI,G.RAMPONI,P.NORDLUND
REMARK 1 TITL CRYSTAL STRUCTURE OF COMMON TYPE ACYLPHOSPHATASE FROM BOVINE
REMARK 1 TITL 2 TESTIS
REMARK 1 REF STRUCTURE V. 5 69 1997
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 9016712
REMARK 1 DOI 10.1016/S0969-2126(97)00167-6
REMARK 1 REFERENCE 3
REMARK 1 AUTH A.PASTORE,V.SAUDEK,G.RAMPONI,R.J.WILLIAMS
REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF ACYLPHOSPHATASE. REFINEMENT
REMARK 1 TITL 2 AND STRUCTURE ANALYSIS.
REMARK 1 REF J.MOL.BIOL. V. 224 427 1992
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 1313885
REMARK 1 DOI 10.1016/0022-2836(92)91005-A
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.0, DISCOVER 2.9.7
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), MSI, SAN DIEGO CA
REMARK 3 (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1029 RESTRAINTS, 970 ARE NOE-DERIVED DISTANCE RESTRAINTS AND 59
REMARK 3 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 2GV1 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037583.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 4.95
REMARK 210 IONIC STRENGTH : 65 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 50 MM SODIUM PHOSPHATE, 30 MM
REMARK 210 DEUTERATED SODIUM ACETATE, 50 MM
REMARK 210 NACL, 90% H2O, 10% D2O; U-15N,
REMARK 210 50 MM SODIUM PHOSPHATE, 30 MM
REMARK 210 DEUTERATED SODIUM ACETATE, 50 MM
REMARK 210 NACL, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; 2D
REMARK 210 15N HSQC; 3D 15N HSQC-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.0, CYANA 2.1
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 380
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY AND STANDARD 2D HOMONUCLEAR TECHNIQUES
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: MONOMERIC
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 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 14 CYS A 5 CA - CB - SG ANGL. DEV. = 11.7 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 1 SER A 2 -51.50 -145.15
REMARK 500 1 TYR A 21 -68.93 -103.56
REMARK 500 1 THR A 33 -161.39 -117.31
REMARK 500 1 THR A 87 -77.32 -77.32
REMARK 500 2 SER A 2 -49.68 -141.26
REMARK 500 2 TYR A 21 -72.21 -98.31
REMARK 500 2 THR A 33 -158.17 -111.47
REMARK 500 2 HIS A 81 77.89 -113.85
REMARK 500 2 THR A 87 -76.95 -83.20
REMARK 500 3 SER A 2 -53.60 -173.12
REMARK 500 3 TYR A 21 -74.61 -87.37
REMARK 500 3 SER A 69 -74.32 -84.69
REMARK 500 3 HIS A 81 72.37 -110.88
REMARK 500 4 ARG A 20 41.54 -68.69
REMARK 500 4 THR A 33 -159.39 -112.27
REMARK 500 5 TYR A 21 -75.05 -94.40
REMARK 500 5 THR A 33 -157.61 -111.87
REMARK 500 5 ARG A 68 -57.11 -136.76
REMARK 500 5 SER A 69 -45.79 -166.79
REMARK 500 5 ARG A 71 78.37 -113.08
REMARK 500 5 HIS A 81 74.22 -110.55
REMARK 500 5 THR A 87 -75.95 -75.54
REMARK 500 6 SER A 2 -53.77 -168.91
REMARK 500 6 TYR A 21 -73.51 -114.27
REMARK 500 6 ALA A 70 159.46 69.79
REMARK 500 6 HIS A 81 77.67 -109.34
REMARK 500 6 THR A 87 -73.43 -74.74
REMARK 500 7 SER A 2 -41.07 -138.17
REMARK 500 7 TYR A 21 -72.42 -110.99
REMARK 500 7 THR A 33 -160.89 -115.61
REMARK 500 7 ALA A 70 148.50 77.67
REMARK 500 7 VAL A 72 94.32 -67.54
REMARK 500 7 HIS A 81 74.21 -109.89
REMARK 500 7 THR A 87 -77.82 -79.59
REMARK 500 8 SER A 2 -49.89 -149.25
REMARK 500 8 TYR A 21 -71.02 -97.42
REMARK 500 8 THR A 33 -162.43 -120.29
REMARK 500 8 THR A 87 -79.26 -79.80
REMARK 500 9 SER A 2 -47.03 -136.42
REMARK 500 9 VAL A 14 -45.84 -131.52
REMARK 500 9 TYR A 21 -72.84 -111.76
REMARK 500 9 ARG A 71 78.45 -115.29
REMARK 500 9 HIS A 81 70.08 -117.43
REMARK 500 9 THR A 87 -75.81 -73.69
REMARK 500 10 SER A 2 -52.54 -140.89
REMARK 500 10 THR A 33 -162.76 -118.73
REMARK 500 10 ALA A 70 -168.82 63.82
REMARK 500 10 THR A 87 -79.93 -79.45
REMARK 500 11 SER A 2 -59.20 175.45
REMARK 500 11 VAL A 4 79.46 -112.78
REMARK 500
REMARK 500 THIS ENTRY HAS 100 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 2 TYR A 11 0.06 SIDE CHAIN
REMARK 500 3 PHE A 19 0.09 SIDE CHAIN
REMARK 500 4 TYR A 11 0.09 SIDE CHAIN
REMARK 500 4 TYR A 35 0.06 SIDE CHAIN
REMARK 500 11 PHE A 19 0.12 SIDE CHAIN
REMARK 500 20 TYR A 11 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y9O RELATED DB: PDB
REMARK 900 ACYLPHOSPHATASE FROM SULFOLOBUS SOLFATARICUS
REMARK 900 RELATED ID: 2ACY RELATED DB: PDB
REMARK 900 COMMON TYPE ACYLPHOSPHATASE FROM BOVINE TESTIS
REMARK 900 RELATED ID: 1APS RELATED DB: PDB
REMARK 900 MUSCLE TYPE ACYLPHOSPHATASE FROM HORSE
DBREF 2GV1 A 1 92 UNP P0AB65 ACYP_ECOLI 1 92
SEQRES 1 A 92 MET SER LYS VAL CYS ILE ILE ALA TRP VAL TYR GLY ARG
SEQRES 2 A 92 VAL GLN GLY VAL GLY PHE ARG TYR THR THR GLN TYR GLU
SEQRES 3 A 92 ALA LYS ARG LEU GLY LEU THR GLY TYR ALA LYS ASN LEU
SEQRES 4 A 92 ASP ASP GLY SER VAL GLU VAL VAL ALA CYS GLY GLU GLU
SEQRES 5 A 92 GLY GLN VAL GLU LYS LEU MET GLN TRP LEU LYS SER GLY
SEQRES 6 A 92 GLY PRO ARG SER ALA ARG VAL GLU ARG VAL LEU SER GLU
SEQRES 7 A 92 PRO HIS HIS PRO SER GLY GLU LEU THR ASP PHE ARG ILE
SEQRES 8 A 92 ARG
HELIX 1 1 THR A 22 GLY A 31 1 10
HELIX 2 2 GLU A 51 GLY A 65 1 15
SHEET 1 A 5 ARG A 71 HIS A 80 0
SHEET 2 A 5 CYS A 5 ARG A 13 -1 N TYR A 11 O ARG A 74
SHEET 3 A 5 VAL A 44 ALA A 48 -1 O VAL A 46 N ALA A 8
SHEET 4 A 5 TYR A 35 ASN A 38 -1 N LYS A 37 O GLU A 45
SHEET 5 A 5 ARG A 90 ILE A 91 1 O ARG A 90 N ALA A 36
SSBOND 1 CYS A 5 CYS A 49 1555 1555 2.04
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END
