Header list of 1p6t.pdb file
Complete list - t 27 2 Bytes
HEADER HYDROLASE 30-APR-03 1P6T
TITLE STRUCTURE CHARACTERIZATION OF THE WATER SOLUBLE REGION OF P-TYPE
TITLE 2 ATPASE COPA FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTENTIAL COPPER-TRANSPORTING ATPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL WATER SOLUBLE REGION (RESIDUES 1-147);
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 COPA; P-TYPE ATPASE; WATER-SOLUBLE REGION; BETA-ALPHA-BETA-BETA-
KEYWDS 2 ALPHA-BETA FOLD; NMR, STRUCTURAL PROTEOMICS IN EUROPE, SPINE,
KEYWDS 3 STRUCTURAL GENOMICS, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,L.GONNELLI,X.C.SU,STRUCTURAL
AUTHOR 2 PROTEOMICS IN EUROPE (SPINE)
REVDAT 3 27-OCT-21 1P6T 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1P6T 1 VERSN
REVDAT 1 16-DEC-03 1P6T 0
JRNL AUTH L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,L.GONNELLI,X.C.SU
JRNL TITL STRUCTURAL BASIS FOR THE FUNCTION OF THE N-TERMINAL DOMAIN
JRNL TITL 2 OF THE ATPASE COPA FROM BACILLUS SUBTILIS.
JRNL REF J.BIOL.CHEM. V. 278 50506 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 14514665
JRNL DOI 10.1074/JBC.M307389200
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: 5099 NOE CROSS PEAKS WERE ASSIGNED AND
REMARK 3 INTEGRATED, PROVIDING 4102 UNIQUE UPPER DISTANCE LIMITS, OF
REMARK 3 WHICH 3303 ARE MEANINGFUL. 152 ANGLE CONSTRAINTS, WERE
REMARK 3 EXPERIMENTALLY DETERMINED AND USED IN THE CALCULATIONS.
REMARK 4
REMARK 4 1P6T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019079.
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 MM DTT
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.5 MM APOS46VCOPA, 20MM
REMARK 210 PHOSPHATE, 90%H2O, 10%D2O,2.0
REMARK 210 MMDTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHA; HNHB;
REMARK 210 CC(CO)NH; (H)CCH-TOCSY; CBCANH;
REMARK 210 CBCA(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ; 700
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, XEASY 1.3
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED CONFORMER MODELS
REMARK 210 ARE THE 30 STRUCTURES WITH THE
REMARK 210 LOWEST VIOLATIONS.
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.
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 13 ARG A 151 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 23 ARG A 151 NE - CZ - NH2 ANGL. DEV. = -3.2 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 3 146.09 84.92
REMARK 500 1 CYS A 17 47.24 71.83
REMARK 500 1 ALA A 18 -110.17 -162.85
REMARK 500 1 VAL A 34 96.41 -50.29
REMARK 500 1 PRO A 52 48.99 -74.84
REMARK 500 1 ALA A 53 25.97 -159.16
REMARK 500 1 GLU A 54 -44.82 -147.33
REMARK 500 1 THR A 55 -84.31 -110.21
REMARK 500 1 THR A 84 -53.05 -179.53
REMARK 500 1 CYS A 85 32.57 -92.50
REMARK 500 1 ALA A 86 27.37 41.87
REMARK 500 1 ARG A 95 -70.63 -73.01
REMARK 500 1 ASN A 97 -48.92 -27.19
REMARK 500 1 LYS A 98 61.00 -152.74
REMARK 500 1 GLU A 100 -65.36 -156.14
REMARK 500 1 ALA A 105 60.07 -155.46
REMARK 500 1 GLN A 145 -47.34 -173.85
REMARK 500 2 MET A 15 97.86 -60.49
REMARK 500 2 ALA A 19 -31.99 67.70
REMARK 500 2 VAL A 34 100.30 -54.28
REMARK 500 2 PRO A 52 37.90 -80.66
REMARK 500 2 ALA A 53 27.50 -162.66
REMARK 500 2 GLU A 54 -47.12 -139.31
REMARK 500 2 THR A 55 -81.53 -107.56
REMARK 500 2 MET A 83 73.33 -51.61
REMARK 500 2 CYS A 85 -132.95 68.95
REMARK 500 2 ALA A 86 -78.64 55.58
REMARK 500 2 ALA A 87 40.28 178.52
REMARK 500 2 ARG A 95 -70.36 -68.98
REMARK 500 2 ASN A 97 -49.96 -29.94
REMARK 500 2 LYS A 98 76.54 -158.96
REMARK 500 2 ILE A 99 -76.23 -71.13
REMARK 500 2 GLU A 100 -105.24 -117.33
REMARK 500 2 ALA A 105 60.72 -156.92
REMARK 500 2 GLN A 145 -53.46 -169.75
REMARK 500 2 SER A 147 30.50 -153.88
REMARK 500 3 LEU A 2 121.48 -172.31
REMARK 500 3 SER A 3 126.70 72.73
REMARK 500 3 MET A 15 95.02 -58.31
REMARK 500 3 PRO A 52 35.53 -79.15
REMARK 500 3 ALA A 53 27.52 -158.80
REMARK 500 3 GLU A 54 -50.75 -138.99
REMARK 500 3 THR A 55 -80.71 -98.57
REMARK 500 3 MET A 83 -136.91 45.74
REMARK 500 3 THR A 84 56.21 36.56
REMARK 500 3 ALA A 87 48.58 -171.33
REMARK 500 3 ARG A 95 -70.44 -71.07
REMARK 500 3 ASN A 97 -47.32 -29.73
REMARK 500 3 LYS A 98 69.32 -156.33
REMARK 500 3 GLU A 100 -105.38 -146.92
REMARK 500
REMARK 500 THIS ENTRY HAS 540 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 1 PHE A 109 0.07 SIDE CHAIN
REMARK 500 1 TYR A 137 0.09 SIDE CHAIN
REMARK 500 2 TYR A 50 0.10 SIDE CHAIN
REMARK 500 2 TYR A 137 0.10 SIDE CHAIN
REMARK 500 3 TYR A 50 0.10 SIDE CHAIN
REMARK 500 3 TYR A 69 0.07 SIDE CHAIN
REMARK 500 3 TYR A 137 0.12 SIDE CHAIN
REMARK 500 3 ARG A 151 0.10 SIDE CHAIN
REMARK 500 4 TYR A 50 0.13 SIDE CHAIN
REMARK 500 4 TYR A 69 0.09 SIDE CHAIN
REMARK 500 5 TYR A 137 0.07 SIDE CHAIN
REMARK 500 8 PHE A 78 0.10 SIDE CHAIN
REMARK 500 9 TYR A 50 0.07 SIDE CHAIN
REMARK 500 9 TYR A 137 0.08 SIDE CHAIN
REMARK 500 10 TYR A 50 0.10 SIDE CHAIN
REMARK 500 10 PHE A 78 0.09 SIDE CHAIN
REMARK 500 11 TYR A 50 0.10 SIDE CHAIN
REMARK 500 11 PHE A 78 0.09 SIDE CHAIN
REMARK 500 12 TYR A 69 0.10 SIDE CHAIN
REMARK 500 12 TYR A 137 0.08 SIDE CHAIN
REMARK 500 13 PHE A 109 0.08 SIDE CHAIN
REMARK 500 14 TYR A 50 0.09 SIDE CHAIN
REMARK 500 14 TYR A 137 0.08 SIDE CHAIN
REMARK 500 15 TYR A 50 0.07 SIDE CHAIN
REMARK 500 16 TYR A 118 0.07 SIDE CHAIN
REMARK 500 16 TYR A 137 0.12 SIDE CHAIN
REMARK 500 17 PHE A 109 0.07 SIDE CHAIN
REMARK 500 17 TYR A 137 0.10 SIDE CHAIN
REMARK 500 18 TYR A 50 0.12 SIDE CHAIN
REMARK 500 19 TYR A 137 0.14 SIDE CHAIN
REMARK 500 20 TYR A 50 0.11 SIDE CHAIN
REMARK 500 20 PHE A 78 0.10 SIDE CHAIN
REMARK 500 20 TYR A 118 0.07 SIDE CHAIN
REMARK 500 20 TYR A 137 0.12 SIDE CHAIN
REMARK 500 21 TYR A 50 0.15 SIDE CHAIN
REMARK 500 21 TYR A 69 0.15 SIDE CHAIN
REMARK 500 21 PHE A 78 0.08 SIDE CHAIN
REMARK 500 21 TYR A 137 0.09 SIDE CHAIN
REMARK 500 22 TYR A 50 0.11 SIDE CHAIN
REMARK 500 22 TYR A 137 0.12 SIDE CHAIN
REMARK 500 23 TYR A 50 0.10 SIDE CHAIN
REMARK 500 23 ARG A 151 0.10 SIDE CHAIN
REMARK 500 24 TYR A 50 0.11 SIDE CHAIN
REMARK 500 24 TYR A 69 0.07 SIDE CHAIN
REMARK 500 25 TYR A 69 0.07 SIDE CHAIN
REMARK 500 25 PHE A 78 0.09 SIDE CHAIN
REMARK 500 27 TYR A 50 0.09 SIDE CHAIN
REMARK 500 28 TYR A 50 0.07 SIDE CHAIN
REMARK 500 28 TYR A 137 0.09 SIDE CHAIN
REMARK 500 29 TYR A 69 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 53 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OQ3 RELATED DB: PDB
REMARK 900 WATER-SOLUBLE PART
REMARK 900 RELATED ID: 1KQK RELATED DB: PDB
REMARK 900 WATER-SOLUBLE PART
REMARK 900 RELATED ID: CIRMMP06 RELATED DB: TARGETDB
DBREF 1P6T A 1 147 UNP O32220 COPA_BACSU 1 147
SEQADV 1P6T VAL A 46 UNP O32220 SER 46 ENGINEERED MUTATION
SEQADV 1P6T ILE A 148 UNP O32220 CLONING ARTIFACT
SEQADV 1P6T GLU A 149 UNP O32220 CLONING ARTIFACT
SEQADV 1P6T GLY A 150 UNP O32220 CLONING ARTIFACT
SEQADV 1P6T ARG A 151 UNP O32220 CLONING ARTIFACT
SEQRES 1 A 151 MET LEU SER GLU GLN LYS GLU ILE ALA MET GLN VAL SER
SEQRES 2 A 151 GLY MET THR CYS ALA ALA CYS ALA ALA ARG ILE GLU LYS
SEQRES 3 A 151 GLY LEU LYS ARG MET PRO GLY VAL THR ASP ALA ASN VAL
SEQRES 4 A 151 ASN LEU ALA THR GLU THR VAL ASN VAL ILE TYR ASP PRO
SEQRES 5 A 151 ALA GLU THR GLY THR ALA ALA ILE GLN GLU LYS ILE GLU
SEQRES 6 A 151 LYS LEU GLY TYR HIS VAL VAL THR GLU LYS ALA GLU PHE
SEQRES 7 A 151 ASP ILE GLU GLY MET THR CYS ALA ALA CYS ALA ASN ARG
SEQRES 8 A 151 ILE GLU LYS ARG LEU ASN LYS ILE GLU GLY VAL ALA ASN
SEQRES 9 A 151 ALA PRO VAL ASN PHE ALA LEU GLU THR VAL THR VAL GLU
SEQRES 10 A 151 TYR ASN PRO LYS GLU ALA SER VAL SER ASP LEU LYS GLU
SEQRES 11 A 151 ALA VAL ASP LYS LEU GLY TYR LYS LEU LYS LEU LYS GLY
SEQRES 12 A 151 GLU GLN ASP SER ILE GLU GLY ARG
HELIX 1 1 ALA A 18 LYS A 29 1 12
HELIX 2 2 LEU A 41 THR A 43 5 3
HELIX 3 3 GLY A 56 GLY A 68 1 13
HELIX 4 4 ALA A 87 ASN A 97 1 11
HELIX 5 5 SER A 124 GLY A 136 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 ILE A 49 N ASP A 36
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 71 -1 O HIS A 70 N SER A 13
SHEET 1 B 4 LEU A 139 LEU A 141 0
SHEET 2 B 4 GLU A 74 ILE A 80 -1 N ASP A 79 O LYS A 140
SHEET 3 B 4 THR A 113 TYR A 118 -1 O VAL A 116 N ALA A 76
SHEET 4 B 4 VAL A 102 ASN A 104 -1 N ASN A 104 O GLU A 117
SHEET 1 C 4 LEU A 139 LEU A 141 0
SHEET 2 C 4 GLU A 74 ILE A 80 -1 N ASP A 79 O LYS A 140
SHEET 3 C 4 THR A 113 TYR A 118 -1 O VAL A 116 N ALA A 76
SHEET 4 C 4 VAL A 107 ASN A 108 -1 N ASN A 108 O THR A 113
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
Complete list - t 27 2 Bytes