Header list of 1k0v.pdb file
Complete list - b 23 2 Bytes
HEADER METAL TRANSPORT 21-SEP-01 1K0V
TITLE COPPER TRAFFICKING: THE SOLUTION STRUCTURE OF BACILLUS SUBTILIS COPZ
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPZ;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: PROBABLE MERCURIC ION-BINDING PROTEIN YVGY;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: COPZ IS INVOLVED IN THE COPPER TRAFFICKING OF BACILLUS
COMPND 7 SUBTILIS AND IT DOES BIND COPPER(I) UNDER REDUCING CONDITIONS
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;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS BETA-ALPHA-BETA-BETA-ALPHA-BETA, METAL TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,R.DEL CONTE,J.MARKEY,F.J.RUIZ-DUENAS
REVDAT 5 23-FEB-22 1K0V 1 REMARK
REVDAT 4 24-FEB-09 1K0V 1 VERSN
REVDAT 3 16-OCT-07 1K0V 1 HET
REVDAT 2 13-MAR-02 1K0V 1 JRNL REMARK
REVDAT 1 19-DEC-01 1K0V 0
JRNL AUTH L.BANCI,I.BERTINI,R.DEL CONTE,J.MARKEY,F.J.RUIZ-DUENAS
JRNL TITL COPPER TRAFFICKING: THE SOLUTION STRUCTURE OF BACILLUS
JRNL TITL 2 SUBTILIS COPZ.
JRNL REF BIOCHEMISTRY V. 40 15660 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11747441
JRNL DOI 10.1021/BI0112715
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, AMBER 5.0
REMARK 3 AUTHORS : GUENTER ET AL. 1997 (DYANA), PEARLMAN ET AL. 1997
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K0V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014419.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300
REMARK 210 PH : 7.0; 7.0
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : SAMPLE 1: 2MM COPPER (I) LOADED
REMARK 210 -BACILLUS SUBTILIS COPZ, 15N
REMARK 210 LABELLED. DTT WAS USED AS
REMARK 210 REDUCTANT. SAMPLE 2: 2MM COPPER
REMARK 210 (I) LOADED-BACILLUS SUBTILIS
REMARK 210 COPZ, NOT LABELLED. DTT WAS USED
REMARK 210 AS REDUCTANT.; 2MM COPPER (I)
REMARK 210 LOADED BACILLUS SUBTILIS COPZ,
REMARK 210 NOT LABELLED. DTT WAS USED AS
REMARK 210 REDUCTANT.
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D TOSCY-HSQC; 3D NOESY-HSQC; 3D
REMARK 210 HNHA; 2D TOSCY; 2D NOESY; 2D HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 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 1.3.13,
REMARK 210 MOLMOL 2.4, CORMA
REMARK 210 METHOD USED : SIMULATED 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 : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HETERONUCLEAR TECHNIQUE
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 7 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 SER A 12 42.94 -156.17
REMARK 500 1 CYS A 16 -71.41 -54.66
REMARK 500 1 LEU A 27 95.37 -68.09
REMARK 500 1 ASP A 28 -51.73 -21.03
REMARK 500 1 HIS A 34 78.18 -116.66
REMARK 500 1 ASN A 36 48.78 -144.92
REMARK 500 1 SER A 45 66.36 -105.12
REMARK 500 1 ASP A 55 -72.14 -52.37
REMARK 500 1 TYR A 65 110.65 64.66
REMARK 500 1 ASP A 66 -32.25 163.47
REMARK 500 1 GLU A 71 -112.00 -110.14
REMARK 500 2 MET A 11 -179.35 -66.61
REMARK 500 2 SER A 12 65.23 -163.70
REMARK 500 2 GLN A 14 -3.24 -55.86
REMARK 500 2 LEU A 27 95.14 -68.08
REMARK 500 2 ASP A 28 -50.53 -19.02
REMARK 500 2 HIS A 34 88.83 -150.68
REMARK 500 2 ASN A 36 48.97 -145.48
REMARK 500 2 LYS A 50 -56.18 -121.19
REMARK 500 2 TYR A 65 102.25 62.64
REMARK 500 2 ASP A 66 -40.07 172.57
REMARK 500 2 VAL A 67 98.96 -69.06
REMARK 500 2 LYS A 69 146.28 -170.47
REMARK 500 3 GLN A 14 -4.20 -57.63
REMARK 500 3 CYS A 16 -74.45 -63.35
REMARK 500 3 ASN A 36 49.45 -156.79
REMARK 500 3 LYS A 50 -53.25 -130.52
REMARK 500 3 ASP A 55 -70.79 -68.90
REMARK 500 3 TYR A 65 112.96 64.00
REMARK 500 3 ASP A 66 -41.85 168.34
REMARK 500 3 GLU A 71 -82.49 -81.62
REMARK 500 4 SER A 12 21.28 -143.31
REMARK 500 4 GLN A 14 2.36 -66.80
REMARK 500 4 ASP A 43 71.39 -114.96
REMARK 500 4 SER A 45 71.32 -110.15
REMARK 500 4 LYS A 54 -54.47 -29.60
REMARK 500 4 TYR A 65 108.90 64.33
REMARK 500 4 ASP A 66 -36.58 171.75
REMARK 500 4 GLU A 71 -103.47 -106.39
REMARK 500 5 SER A 12 40.73 -156.07
REMARK 500 5 CYS A 16 -71.24 -57.53
REMARK 500 5 SER A 45 68.89 -103.80
REMARK 500 5 LYS A 50 -56.13 -121.48
REMARK 500 5 VAL A 51 -169.81 -128.41
REMARK 500 5 GLN A 63 46.57 -145.00
REMARK 500 5 TYR A 65 110.64 66.02
REMARK 500 5 ASP A 66 -38.55 169.78
REMARK 500 6 SER A 12 15.16 -155.53
REMARK 500 6 GLN A 14 2.56 -64.20
REMARK 500 6 CYS A 16 -70.16 -48.21
REMARK 500
REMARK 500 THIS ENTRY HAS 248 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 ARG A 73 0.08 SIDE CHAIN
REMARK 500 6 ARG A 73 0.10 SIDE CHAIN
REMARK 500 10 PHE A 46 0.09 SIDE CHAIN
REMARK 500 10 ARG A 73 0.10 SIDE CHAIN
REMARK 500 14 TYR A 65 0.09 SIDE CHAIN
REMARK 500 15 HIS A 15 0.10 SIDE CHAIN
REMARK 500 18 TYR A 65 0.06 SIDE CHAIN
REMARK 500 21 PHE A 46 0.09 SIDE CHAIN
REMARK 500 22 PHE A 46 0.08 SIDE CHAIN
REMARK 500 23 PHE A 46 0.08 SIDE CHAIN
REMARK 500 25 HIS A 15 0.08 SIDE CHAIN
REMARK 500 28 TYR A 65 0.08 SIDE CHAIN
REMARK 500 29 PHE A 46 0.12 SIDE CHAIN
REMARK 500 29 TYR A 65 0.07 SIDE CHAIN
REMARK 500 30 TYR A 65 0.16 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 600
REMARK 600 HETEROGEN
REMARK 600 COPPER (I) IS COORDINATED BY
REMARK 600 CYS 13 AND CYS 16.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 74
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1CPZ RELATED DB: PDB
REMARK 900 COPPER(I)-LOADED COPZ FROM BACILLUS SUBTILIS. COPZ PROTEIN IS
REMARK 900 INVOLVED IN THE COPPER TRAFFICKING OF BACILLUS SUBTILIS. COPZ FROM
REMARK 900 BACILLUS SUBTILIS HAS HIGH HOMOLOGY WITH THAT OF COPZ PROTEIN FROM
REMARK 900 ENTEROCOCCUS HIRAE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE LAST FOUR AMINO ACID SEGMENT IEGR,
REMARK 999 CORRESPONDING TO THE FACTORXA RECOGNITION
REMARK 999 SITE USED TO REMOVE THE HISTIDINE
REMARK 999 TAG, WAS ENGINEERED AT THE C-TERMINUS
REMARK 999 OF THE CONSTRUCT.
DBREF 1K0V A 1 69 UNP O32221 COPZ_BACSU 1 69
SEQADV 1K0V ILE A 70 UNP O32221 SEE REMARK 999
SEQADV 1K0V GLU A 71 UNP O32221 SEE REMARK 999
SEQADV 1K0V GLY A 72 UNP O32221 SEE REMARK 999
SEQADV 1K0V ARG A 73 UNP O32221 SEE REMARK 999
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
HET CU1 A 74 1
HETNAM CU1 COPPER (I) ION
FORMUL 2 CU1 CU 1+
HELIX 1 1 CYS A 13 GLY A 25 1 13
HELIX 2 2 SER A 52 GLY A 64 1 13
SHEET 1 A 4 VAL A 33 HIS A 34 0
SHEET 2 A 4 LYS A 41 VAL A 44 -1 O ASP A 43 N HIS A 34
SHEET 3 A 4 LYS A 4 VAL A 8 -1 N LEU A 6 O VAL A 42
SHEET 4 A 4 VAL A 67 ILE A 70 -1 O ALA A 68 N GLN A 7
SITE 1 AC1 2 CYS A 13 CYS A 16
CRYST1 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