Header list of 1p8g.pdb file
Complete list - b 23 2 Bytes
HEADER CHAPERONE 07-MAY-03 1P8G
TITLE THE SOLUTION STRUCTURE OF APO COPZ FROM BACILLUS SUBTILIS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIMILAR TO MERCURIC TRANSPORT PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: BSCOPZ;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS M-X-C-X-X-C MOTIF, BETA-ALPHA-BETA-BETA-ALPHA-BETA SECONDARY
KEYWDS 2 STRUCTURE, COPPER CHAPERONE, CHAPERONE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,R.DEL CONTE
REVDAT 3 23-FEB-22 1P8G 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1P8G 1 VERSN
REVDAT 1 25-NOV-03 1P8G 0
JRNL AUTH L.BANCI,I.BERTINI,R.DEL CONTE
JRNL TITL SOLUTION STRUCTURE OF APO COPZ FROM BACILLUS SUBTILIS:
JRNL TITL 2 FURTHER ANALYSIS OF THE CHANGES ASSOCIATED WITH THE PRESENCE
JRNL TITL 3 OF COPPER
JRNL REF BIOCHEMISTRY V. 42 13422 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14621987
JRNL DOI 10.1021/BI0353326
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, AMBER 5.0
REMARK 3 AUTHORS :
REMARK 3 PEARLMAN,CASE,CALDWELL,ROSS,CHEATHAM,FERGUSON,SEIBEL,SINGH,
REMARK 3 WEINER,KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 1639 UPPER DISTANCE LIMITS
REMARK 3 (OF WHICH 1431 MEANINGFUL), 31 DIHEDRAL PHI ANGLE CONSTRAINTS
REMARK 3 AND 48 PSI ANGLE CONSTRAINTS WERE MEASURED AND USED IN THE
REMARK 3 STRUCTURAL CALCULATIONS. 5 STEREOSPECIFIC ASSIGNMENTS WERE ALSO
REMARK 3 OBTAINED FROM THE ANALYSIS OF HNHB SPECTRA AND 11 THROUGH THE
REMARK 3 PROGRAM GLOMSA.
REMARK 4
REMARK 4 1P8G COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAY-03.
REMARK 100 THE DEPOSITION ID IS D_1000019138.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 298
REMARK 210 PH : 7.0; 7.0
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 2MM APO-BSCOPZ; 2MM APO-BSCOPZ
REMARK 210 LABELLED WITH 15N
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_15N HSQC
REMARK 210 TOSCY; 15N-HSQC; HNHA; HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 700 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.1, XEASY 1.3.13,
REMARK 210 CORMA, MOLMOL 2.4, GLOMSA
REMARK 210 METHOD USED : SIMULATE ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURE WITH THE LOWEST ENERGY
REMARK 210 TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE 500 MHZ SPECTROMETER IS EQUIPPED WITH A CRYO PROBE
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 15 ARG A 73 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 20 ARG A 73 NE - CZ - NH2 ANGL. DEV. = -3.1 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 GLN A 7 110.50 -34.38
REMARK 500 1 SER A 12 -132.39 -175.71
REMARK 500 1 CYS A 13 -51.50 -143.27
REMARK 500 1 GLN A 14 -46.86 -158.80
REMARK 500 1 CYS A 16 -47.04 -147.44
REMARK 500 1 SER A 31 -42.56 -131.00
REMARK 500 1 VAL A 33 59.12 -142.30
REMARK 500 1 ASN A 36 58.69 -150.01
REMARK 500 1 ALA A 48 -39.13 -36.95
REMARK 500 1 GLN A 63 -63.71 -120.13
REMARK 500 1 TYR A 65 52.98 -162.79
REMARK 500 1 ALA A 68 -70.44 -49.74
REMARK 500 1 LYS A 69 -174.46 163.07
REMARK 500 2 SER A 12 -170.22 65.64
REMARK 500 2 GLU A 21 -70.39 -66.13
REMARK 500 2 SER A 31 -44.57 -133.24
REMARK 500 2 VAL A 33 58.31 -141.11
REMARK 500 2 ASN A 36 55.86 -154.55
REMARK 500 2 TYR A 65 55.16 -161.98
REMARK 500 2 LYS A 69 172.70 168.74
REMARK 500 3 MET A 11 -152.36 -144.47
REMARK 500 3 CYS A 13 -48.25 -135.74
REMARK 500 3 GLN A 14 -155.67 62.14
REMARK 500 3 VAL A 17 18.48 51.89
REMARK 500 3 SER A 31 -45.43 -141.00
REMARK 500 3 VAL A 33 58.45 -144.48
REMARK 500 3 GLN A 63 -62.11 -105.45
REMARK 500 3 TYR A 65 51.43 -163.15
REMARK 500 3 LYS A 69 169.79 117.87
REMARK 500 4 SER A 12 74.38 -68.10
REMARK 500 4 HIS A 15 46.41 -82.64
REMARK 500 4 LYS A 18 -43.60 -179.85
REMARK 500 4 SER A 31 -47.34 -133.82
REMARK 500 4 VAL A 33 59.10 -141.54
REMARK 500 4 ASN A 36 58.03 -145.80
REMARK 500 4 TYR A 65 54.28 -67.89
REMARK 500 4 ALA A 68 -73.32 -62.45
REMARK 500 4 LYS A 69 174.91 175.80
REMARK 500 4 GLU A 71 -84.52 -84.04
REMARK 500 5 GLN A 7 122.12 -37.43
REMARK 500 5 MET A 11 -69.32 -96.45
REMARK 500 5 VAL A 17 62.17 -69.09
REMARK 500 5 LYS A 18 -40.29 178.09
REMARK 500 5 GLU A 21 -69.82 -91.01
REMARK 500 5 VAL A 33 58.24 -143.40
REMARK 500 5 ASN A 36 56.61 -149.29
REMARK 500 5 VAL A 53 -55.21 -25.53
REMARK 500 5 TYR A 65 51.22 -164.80
REMARK 500 5 LYS A 69 179.95 165.86
REMARK 500 6 SER A 12 -137.80 61.78
REMARK 500
REMARK 500 THIS ENTRY HAS 306 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 ARG A 73 0.09 SIDE CHAIN
REMARK 500 3 TYR A 65 0.09 SIDE CHAIN
REMARK 500 6 PHE A 46 0.08 SIDE CHAIN
REMARK 500 6 TYR A 65 0.08 SIDE CHAIN
REMARK 500 6 ARG A 73 0.14 SIDE CHAIN
REMARK 500 7 TYR A 65 0.18 SIDE CHAIN
REMARK 500 7 ARG A 73 0.08 SIDE CHAIN
REMARK 500 9 TYR A 65 0.09 SIDE CHAIN
REMARK 500 11 TYR A 65 0.10 SIDE CHAIN
REMARK 500 13 TYR A 65 0.14 SIDE CHAIN
REMARK 500 15 PHE A 46 0.10 SIDE CHAIN
REMARK 500 18 TYR A 65 0.08 SIDE CHAIN
REMARK 500 20 PHE A 46 0.09 SIDE CHAIN
REMARK 500 23 TYR A 65 0.11 SIDE CHAIN
REMARK 500 24 PHE A 46 0.08 SIDE CHAIN
REMARK 500 27 TYR A 65 0.08 SIDE CHAIN
REMARK 500 28 TYR A 65 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K0V RELATED DB: PDB
REMARK 900 COPPER TRAFFICKING: THE SOLUTION STRUCTURE OF COPPER LOADED
REMARK 900 BACILLUS SUBTILIS COPZ
DBREF 1P8G A 1 69 UNP O32221 COPZ_BACSU 1 69
SEQADV 1P8G ILE A 70 UNP O32221 CLONING ARTIFACT
SEQADV 1P8G GLU A 71 UNP O32221 CLONING ARTIFACT
SEQADV 1P8G GLY A 72 UNP O32221 CLONING ARTIFACT
SEQADV 1P8G ARG A 73 UNP O32221 CLONING ARTIFACT
SEQRES 1 A 73 MET GLU GLN LYS THR LEU GLN VAL GLU GLY MET SER CYS
SEQRES 2 A 73 GLN HIS CYS VAL LYS ALA VAL GLU THR SER VAL GLY GLU
SEQRES 3 A 73 LEU ASP GLY VAL SER ALA VAL HIS VAL ASN LEU GLU ALA
SEQRES 4 A 73 GLY LYS VAL ASP VAL SER PHE ASP ALA ASP LYS VAL SER
SEQRES 5 A 73 VAL LYS ASP ILE ALA ASP ALA ILE GLU ASP GLN GLY TYR
SEQRES 6 A 73 ASP VAL ALA LYS ILE GLU GLY ARG
HELIX 1 1 CYS A 16 GLU A 26 1 11
HELIX 2 3 SER A 52 ASP A 62 1 11
SHEET 1 A 4 VAL A 30 ASN A 36 0
SHEET 2 A 4 LYS A 41 PHE A 46 -1 O ASP A 43 N HIS A 34
SHEET 3 A 4 GLU A 2 GLN A 7 -1 N LYS A 4 O VAL A 44
SHEET 4 A 4 LYS A 69 ILE A 70 -1 N LYS A 69 O GLN A 7
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 - b 23 2 Bytes