Header list of 1opz.pdb file
Complete list - 27 20 Bytes
HEADER HYDROLASE 06-MAR-03 1OPZ
TITLE A CORE MUTATION AFFECTING THE FOLDING PROPERTIES OF A SOLUBLE DOMAIN
TITLE 2 OF THE ATPASE PROTEIN COPA FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTENTIAL COPPER-TRANSPORTING ATPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THE FIRST N-TERMINAL WATER SOLUBLE DOMAIN OF COPA;
COMPND 5 EC: 3.6.3.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: YVGX;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS MUTATION, FOLDING, ABBAB FOLD, HYDROLASE
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,L.GONNELI,X.C.SU
REVDAT 3 27-OCT-21 1OPZ 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1OPZ 1 VERSN
REVDAT 1 16-MAR-04 1OPZ 0
JRNL AUTH L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,L.GONNELLI,X.C.SU
JRNL TITL A CORE MUTATION AFFECTING THE FOLDING PROPERTIES OF A
JRNL TITL 2 SOLUBLE DOMAIN OF THE ATPASE PROTEIN COPA FROM BACILLUS
JRNL TITL 3 SUBTILIS.
JRNL REF J.MOL.BIOL. V. 331 473 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 12888353
JRNL DOI 10.1016/S0022-2836(03)00769-1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, AMBER 5.0
REMARK 3 AUTHORS : BRUKER (XWINNMR), PEARLMAN, CASE, CALDWELL, ROSS,
REMARK 3 CHEATHAM, FERGUSON, SEIBEL, SINGH, WEINER, KOLLMAN
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1OPZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018547.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 20 MM PHOSPHATE + 2 MMDTT
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5 MM APOD1S46VCOPA, 20MM
REMARK 210 PHOSPHATE, 90%H2O, 10%D2O,2.0 MM
REMARK 210 DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3, DYANA 1.5
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS, RESTRAINED
REMARK 210 ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODEL IS
REMARK 210 THE AVERAGE OF 30 STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 15N LABELED D1S46VCOPA
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: 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 CYS A 17 -136.28 51.35
REMARK 500 ALA A 18 57.27 32.93
REMARK 500 PRO A 52 7.94 -67.56
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 A 50 0.09 SIDE CHAIN
REMARK 500 ARG A 76 0.15 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OQ3 RELATED DB: PDB
REMARK 900 RELATED ID: 1OQ6 RELATED DB: PDB
DBREF 1OPZ A 1 76 UNP O32220 COPA_BACSU 1 76
SEQADV 1OPZ VAL A 46 UNP O32220 SER 46 ENGINEERED MUTATION
SEQADV 1OPZ ILE A 73 UNP O32220 THR 73 CLONING ARTIFACT
SEQADV 1OPZ GLY A 75 UNP O32220 LYS 75 CLONING ARTIFACT
SEQADV 1OPZ ARG A 76 UNP O32220 ALA 76 CLONING ARTIFACT
SEQRES 1 A 76 MET LEU SER GLU GLN LYS GLU ILE ALA MET GLN VAL SER
SEQRES 2 A 76 GLY MET THR CYS ALA ALA CYS ALA ALA ARG ILE GLU LYS
SEQRES 3 A 76 GLY LEU LYS ARG MET PRO GLY VAL THR ASP ALA ASN VAL
SEQRES 4 A 76 ASN LEU ALA THR GLU THR VAL ASN VAL ILE TYR ASP PRO
SEQRES 5 A 76 ALA GLU THR GLY THR ALA ALA ILE GLN GLU LYS ILE GLU
SEQRES 6 A 76 LYS LEU GLY TYR HIS VAL VAL ILE GLU GLY ARG
HELIX 1 1 ALA A 19 ARG A 30 1 12
HELIX 2 2 LEU A 41 THR A 43 5 3
HELIX 3 3 GLY A 56 GLY A 68 1 13
SHEET 1 A 4 VAL A 34 ASN A 40 0
SHEET 2 A 4 THR A 45 TYR A 50 -1 O ASN A 47 N ASN A 38
SHEET 3 A 4 LYS A 6 SER A 13 -1 N MET A 10 O VAL A 46
SHEET 4 A 4 HIS A 70 VAL A 72 -1 O VAL A 72 N GLN A 11
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
Complete list - 27 20 Bytes