Header list of 1sb6.pdb file
Complete list - r 25 2 Bytes
HEADER CHAPERONE 10-FEB-04 1SB6
TITLE SOLUTION STRUCTURE OF A CYANOBACTERIAL COPPER METALLOCHAPERONE, SCATX1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER CHAPERONE SCATX1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP.;
SOURCE 3 ORGANISM_TAXID: 1148;
SOURCE 4 STRAIN: PCC 6803;
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: PETATX1
KEYWDS COPPER CHAPERONE, NEW METAL BINDING MOTIF, STRUCTURAL PROTEOMICS IN
KEYWDS 2 EUROPE, SPINE, STRUCTURAL GENOMICS, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,X.C.SU,G.P.BORRELLY,N.J.ROBINSON,
AUTHOR 2 STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 4 13-JUL-11 1SB6 1 VERSN
REVDAT 3 24-FEB-09 1SB6 1 VERSN
REVDAT 2 29-JUN-04 1SB6 1 JRNL
REVDAT 1 27-APR-04 1SB6 0
JRNL AUTH L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,X.C.SU,G.P.BORRELLY,
JRNL AUTH 2 N.J.ROBINSON
JRNL TITL SOLUTION STRUCTURES OF A CYANOBACTERIAL METALLOCHAPERONE:
JRNL TITL 2 INSIGHT INTO AN ATYPICAL COPPER-BINDING MOTIF.
JRNL REF J.BIOL.CHEM. V. 279 27502 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15075318
JRNL DOI 10.1074/JBC.M402005200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 5.0
REMARK 3 AUTHORS : PEALMAN, CASE, CALDWELL, ROSS, CHEATHAM, FERGUSON,
REMARK 3 SEIBEL, SINGH, WEINER, KOLLMAN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: IN THE ENSEMBLE EACH STRUCTURE IS BASED
REMARK 3 ON A TOTAL OF 1017 MEANINGFUL NOES CONSTRANTS TOGETHER WITH 44
REMARK 3 DIHEDRAL ANGLE(PHI)RESTRAINTS.
REMARK 4
REMARK 4 1SB6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-04.
REMARK 100 THE RCSB ID CODE IS RCSB021574.
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 : 50 MM PHOSPHATE
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.7 MM APOSCATX1,50MM PHOSPHATE,
REMARK 210 90%H2O, 10%D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N-SEPARATED_
REMARK 210 NOESY; 2D TOCSY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, XEASY 1.3, DYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : THE SUBMITTED STRUCTURES ARE THE
REMARK 210 20 STRUCTURES WITH THE LOWEST
REMARK 210 TARGET FUNCTION OF 200 CONFORMERS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 15N LABELLED APO SCATX1
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 1 ILE A 10 160.60 -48.22
REMARK 500 1 ALA A 11 -31.92 76.84
REMARK 500 1 GLU A 13 64.85 62.42
REMARK 500 1 CYS A 15 152.85 71.48
REMARK 500 1 SER A 38 -108.19 -144.09
REMARK 500 1 LYS A 39 30.25 -157.42
REMARK 500 1 GLU A 62 48.92 -82.90
REMARK 500 2 THR A 9 41.45 -99.32
REMARK 500 2 ILE A 10 158.79 -44.95
REMARK 500 2 GLU A 13 -125.94 -87.79
REMARK 500 2 ALA A 14 38.19 -98.21
REMARK 500 2 CYS A 15 153.92 66.90
REMARK 500 2 SER A 38 -115.93 -134.61
REMARK 500 2 LYS A 39 52.84 -156.95
REMARK 500 3 THR A 9 39.48 -97.29
REMARK 500 3 GLU A 13 -79.09 -86.73
REMARK 500 3 ALA A 14 35.92 -142.21
REMARK 500 3 CYS A 15 148.76 71.06
REMARK 500 3 SER A 38 -115.61 -132.16
REMARK 500 3 LYS A 39 29.17 -157.02
REMARK 500 4 THR A 9 39.48 -97.29
REMARK 500 4 GLU A 13 -79.09 -86.73
REMARK 500 4 ALA A 14 35.92 -142.21
REMARK 500 4 CYS A 15 148.76 71.06
REMARK 500 4 SER A 38 -115.61 -132.16
REMARK 500 4 LYS A 39 29.17 -157.02
REMARK 500 5 THR A 2 77.19 35.71
REMARK 500 5 VAL A 7 78.81 -113.36
REMARK 500 5 THR A 9 40.63 -94.60
REMARK 500 5 ILE A 10 156.78 -47.60
REMARK 500 5 ALA A 11 -26.36 70.01
REMARK 500 5 GLU A 13 -82.56 -88.77
REMARK 500 5 ALA A 14 41.57 -147.49
REMARK 500 5 CYS A 15 153.87 67.32
REMARK 500 5 SER A 38 -123.67 -123.78
REMARK 500 5 LYS A 39 38.23 -156.17
REMARK 500 6 ILE A 10 152.20 -45.33
REMARK 500 6 GLU A 13 -99.07 -86.71
REMARK 500 6 CYS A 15 155.39 67.93
REMARK 500 6 ASP A 27 74.29 -110.53
REMARK 500 6 THR A 37 -40.24 -144.13
REMARK 500 6 SER A 38 -97.74 -142.96
REMARK 500 6 LYS A 39 64.58 -157.60
REMARK 500 7 THR A 2 67.52 25.34
REMARK 500 7 GLU A 13 -107.06 -166.87
REMARK 500 7 CYS A 15 145.43 69.06
REMARK 500 7 GLN A 33 71.13 -151.34
REMARK 500 7 SER A 38 -121.59 -127.16
REMARK 500 7 LYS A 39 36.62 -157.18
REMARK 500 8 THR A 9 34.94 -90.76
REMARK 500
REMARK 500 THIS ENTRY HAS 141 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MET A 1 THR A 2 18 -149.82
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 7 HIS A 61 0.09 SIDE CHAIN
REMARK 500 9 HIS A 61 0.09 SIDE CHAIN
REMARK 500 15 HIS A 61 0.11 SIDE CHAIN
REMARK 500 16 HIS A 61 0.09 SIDE CHAIN
REMARK 500 17 HIS A 61 0.10 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: CIRMMP34 RELATED DB: TARGETDB
DBREF 1SB6 A 1 64 UNP P73213 P73213_SYNY3 1 64
SEQRES 1 A 64 MET THR ILE GLN LEU THR VAL PRO THR ILE ALA CYS GLU
SEQRES 2 A 64 ALA CYS ALA GLU ALA VAL THR LYS ALA VAL GLN ASN GLU
SEQRES 3 A 64 ASP ALA GLN ALA THR VAL GLN VAL ASP LEU THR SER LYS
SEQRES 4 A 64 LYS VAL THR ILE THR SER ALA LEU GLY GLU GLU GLN LEU
SEQRES 5 A 64 ARG THR ALA ILE ALA SER ALA GLY HIS GLU VAL GLU
HELIX 1 1 ALA A 16 ASP A 27 1 12
HELIX 2 2 GLY A 48 GLY A 60 1 13
SHEET 1 A 3 THR A 2 THR A 6 0
SHEET 2 A 3 LYS A 40 THR A 44 -1 O ILE A 43 N ILE A 3
SHEET 3 A 3 THR A 31 ASP A 35 -1 N THR A 31 O THR A 44
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 - r 25 2 Bytes