Header list of 1tl4.pdb file
Complete list - r 2 2 Bytes
HEADER METAL TRANSPORT 09-JUN-04 1TL4
TITLE SOLUTION STRUCTURE OF CU(I) HAH1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER TRANSPORT PROTEIN ATOX1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: METAL TRANSPORT PROTEIN ATX1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ATOX1, HAH1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET20B+
KEYWDS COPPER PROTEIN, COPPER CHAPERONE, MENKES, WILSON, STRUCTURAL
KEYWDS 2 PROTEOMICS IN EUROPE, SPINE, STRUCTURAL GENOMICS, METAL TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR I.ANASTASSOPOULOU,L.BANCI,I.BERTINI,F.CANTINI,E.KATSARI,A.ROSATO,
AUTHOR 2 STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 3 02-MAR-22 1TL4 1 REMARK LINK
REVDAT 2 24-FEB-09 1TL4 1 VERSN
REVDAT 1 26-OCT-04 1TL4 0
JRNL AUTH I.ANASTASSOPOULOU,L.BANCI,I.BERTINI,F.CANTINI,E.KATSARI,
JRNL AUTH 2 A.ROSATO
JRNL TITL SOLUTION STRUCTURE OF THE APO AND COPPER(I)-LOADED HUMAN
JRNL TITL 2 METALLOCHAPERONE HAH1.
JRNL REF BIOCHEMISTRY V. 43 13046 2004
JRNL REFN ISSN 0006-2960
JRNL PMID 15476398
JRNL DOI 10.1021/BI0487591
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR, 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: THE STRUCTURES WERE BASED ON A TOTAL OF
REMARK 3 1219 MEANINGFUL DISTANCE CONSTRAINTS, 99 DIHEDRAL ANGLE
REMARK 3 RESTRAINTS.
REMARK 4
REMARK 4 1TL4 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022740.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 6; 7
REMARK 210 IONIC STRENGTH : 10 MM SODIUM ACETATE; 100 MM
REMARK 210 PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.0 MM CU(I)HAH1 U-15N; 10 MM
REMARK 210 SODIUM ACETATE; 2 MM CU(I)HAH1 U-
REMARK 210 95% 13C,U-98% 15N; 4 MM DTT; 100
REMARK 210 MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CBCANH; CBCACONH; HNCO;
REMARK 210 HN(CA)CO; (H)CCH_TOCSY; HNHA; 3D_
REMARK 210 15N-SEPARATED_NOESY; 2D NOESY;
REMARK 210 2D TOCSY; 3D_13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 900 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, DIANA 1.5, CYANA 1.0
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS COUPLED
REMARK 210 WITH SIMULATED ANNEALING
REMARK 210 FOLLOWED BY RESTRAINED ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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 PRO A 2 62.02 -112.49
REMARK 500 3 ASP A 9 79.15 -67.15
REMARK 500 3 THR A 61 78.11 -66.07
REMARK 500 4 ASP A 9 75.32 -112.34
REMARK 500 4 HIS A 46 96.40 -26.41
REMARK 500 4 SER A 47 138.86 -39.30
REMARK 500 4 LYS A 60 -157.16 -124.72
REMARK 500 4 THR A 61 43.91 -74.72
REMARK 500 5 THR A 61 84.09 -62.50
REMARK 500 6 LYS A 56 -35.21 -38.91
REMARK 500 7 PRO A 2 56.44 -94.71
REMARK 500 7 HIS A 46 94.33 -58.05
REMARK 500 7 THR A 61 47.70 -72.44
REMARK 500 8 PRO A 2 44.89 -99.68
REMARK 500 8 ASP A 9 74.39 -68.49
REMARK 500 8 THR A 61 48.26 -73.21
REMARK 500 9 PRO A 2 70.48 -112.12
REMARK 500 9 MET A 10 53.95 -116.98
REMARK 500 10 MET A 10 68.16 -113.16
REMARK 500 10 LYS A 38 66.14 60.76
REMARK 500 10 LYS A 60 -160.05 -102.46
REMARK 500 10 THR A 61 44.41 -75.44
REMARK 500 11 PRO A 2 70.38 -64.23
REMARK 500 12 PRO A 2 96.49 -55.03
REMARK 500 12 ASP A 9 79.93 -64.72
REMARK 500 13 PRO A 2 99.78 -46.74
REMARK 500 13 LYS A 60 -160.62 -118.24
REMARK 500 13 THR A 61 46.86 -73.79
REMARK 500 14 PRO A 2 86.48 -33.85
REMARK 500 14 THR A 11 27.49 -155.96
REMARK 500 15 PRO A 2 70.15 -101.82
REMARK 500 15 ASP A 9 77.47 -67.41
REMARK 500 15 THR A 11 -48.71 -149.23
REMARK 500 16 LYS A 38 67.73 70.77
REMARK 500 16 LYS A 60 -154.97 -99.94
REMARK 500 16 THR A 61 47.53 -75.68
REMARK 500 17 LYS A 38 61.44 61.04
REMARK 500 18 LYS A 38 73.64 73.19
REMARK 500 18 GLU A 45 75.73 -65.46
REMARK 500 18 SER A 63 -175.83 -69.10
REMARK 500 19 ASP A 9 87.78 -57.99
REMARK 500 19 MET A 10 78.36 -107.69
REMARK 500 20 ASP A 9 63.13 -56.05
REMARK 500 20 LYS A 38 63.22 72.19
REMARK 500 20 THR A 61 48.70 -76.79
REMARK 500 21 PRO A 2 78.08 -28.11
REMARK 500 21 ASP A 9 73.09 -117.55
REMARK 500 21 THR A 61 49.61 -72.25
REMARK 500 22 ASP A 9 76.16 -64.81
REMARK 500 22 THR A 61 75.36 -68.48
REMARK 500
REMARK 500 THIS ENTRY HAS 70 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 VAL A 29 LYS A 30 1 148.00
REMARK 500 MET A 1 PRO A 2 2 136.34
REMARK 500 MET A 1 PRO A 2 6 142.55
REMARK 500 LEU A 67 GLU A 68 9 148.65
REMARK 500 VAL A 29 LYS A 30 10 143.44
REMARK 500 VAL A 29 LYS A 30 11 149.59
REMARK 500 MET A 1 PRO A 2 12 -144.79
REMARK 500 MET A 1 PRO A 2 14 -146.29
REMARK 500 VAL A 29 LYS A 30 14 145.42
REMARK 500 MET A 1 PRO A 2 15 148.92
REMARK 500 VAL A 29 LYS A 30 15 143.09
REMARK 500 VAL A 8 ASP A 9 16 144.51
REMARK 500 ASP A 32 ILE A 33 18 -149.58
REMARK 500 VAL A 29 LYS A 30 21 145.69
REMARK 500 ASP A 32 ILE A 33 23 -145.05
REMARK 500 ASP A 32 ILE A 33 24 -136.97
REMARK 500 LEU A 65 GLY A 66 27 -145.85
REMARK 500 LEU A 67 GLU A 68 27 148.53
REMARK 500 MET A 1 PRO A 2 29 -147.18
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 HIS A 46 0.09 SIDE CHAIN
REMARK 500 1 TYR A 64 0.14 SIDE CHAIN
REMARK 500 2 PHE A 6 0.13 SIDE CHAIN
REMARK 500 2 HIS A 46 0.09 SIDE CHAIN
REMARK 500 2 TYR A 64 0.11 SIDE CHAIN
REMARK 500 4 TYR A 31 0.09 SIDE CHAIN
REMARK 500 7 TYR A 64 0.06 SIDE CHAIN
REMARK 500 10 PHE A 6 0.15 SIDE CHAIN
REMARK 500 11 TYR A 31 0.07 SIDE CHAIN
REMARK 500 12 PHE A 6 0.10 SIDE CHAIN
REMARK 500 12 HIS A 46 0.12 SIDE CHAIN
REMARK 500 12 TYR A 64 0.13 SIDE CHAIN
REMARK 500 14 PHE A 6 0.08 SIDE CHAIN
REMARK 500 16 TYR A 64 0.07 SIDE CHAIN
REMARK 500 17 TYR A 31 0.09 SIDE CHAIN
REMARK 500 17 TYR A 64 0.18 SIDE CHAIN
REMARK 500 18 TYR A 31 0.07 SIDE CHAIN
REMARK 500 18 TYR A 64 0.12 SIDE CHAIN
REMARK 500 26 TYR A 64 0.13 SIDE CHAIN
REMARK 500 28 TYR A 31 0.09 SIDE CHAIN
REMARK 500 30 TYR A 31 0.10 SIDE CHAIN
REMARK 500 30 TYR A 64 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CU1 A 69 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 12 O
REMARK 620 2 CYS A 12 SG 95.6
REMARK 620 3 CYS A 15 SG 98.7 152.5
REMARK 620 N 1 2
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 69
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TL5 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF APOHAH1
REMARK 900 RELATED ID: CIRMMP27 RELATED DB: TARGETDB
DBREF 1TL4 A 1 68 UNP O00244 ATOX1_HUMAN 1 68
SEQRES 1 A 68 MET PRO LYS HIS GLU PHE SER VAL ASP MET THR CYS GLY
SEQRES 2 A 68 GLY CYS ALA GLU ALA VAL SER ARG VAL LEU ASN LYS LEU
SEQRES 3 A 68 GLY GLY VAL LYS TYR ASP ILE ASP LEU PRO ASN LYS LYS
SEQRES 4 A 68 VAL CYS ILE GLU SER GLU HIS SER MET ASP THR LEU LEU
SEQRES 5 A 68 ALA THR LEU LYS LYS THR GLY LYS THR VAL SER TYR LEU
SEQRES 6 A 68 GLY LEU GLU
HET CU1 A 69 1
HETNAM CU1 COPPER (I) ION
FORMUL 2 CU1 CU 1+
HELIX 1 1 GLY A 13 GLY A 27 1 15
HELIX 2 2 SER A 47 LYS A 56 1 10
HELIX 3 3 LYS A 57 GLY A 59 5 3
SHEET 1 A 4 LYS A 30 ASP A 34 0
SHEET 2 A 4 LYS A 39 GLU A 43 -1 O GLU A 43 N LYS A 30
SHEET 3 A 4 LYS A 3 SER A 7 -1 N HIS A 4 O ILE A 42
SHEET 4 A 4 SER A 63 GLU A 68 -1 O GLU A 68 N LYS A 3
LINK O CYS A 12 CU CU1 A 69 1555 1555 2.69
LINK SG CYS A 12 CU CU1 A 69 1555 1555 2.15
LINK SG CYS A 15 CU CU1 A 69 1555 1555 2.16
SITE 1 AC1 2 CYS A 12 CYS A 15
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 2 2 Bytes