Header list of 2ggp.pdb file
Complete list - r 9 2 Bytes
HEADER CHAPERONE, METAL TRANSPORT 24-MAR-06 2GGP
TITLE SOLUTION STRUCTURE OF THE ATX1-CU(I)-CCC2A COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: METAL HOMEOSTASIS FACTOR ATX1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HMA DOMAIN, RESIDUES 1-73;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROBABLE COPPER-TRANSPORTING ATPASE;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: HMA 1 DOMAIN, RESIDUES 2-72;
COMPND 10 SYNONYM: CU2+, -ATPASE;
COMPND 11 EC: 3.6.3.4;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 GENE: ATX1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11D;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 13 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 14 ORGANISM_TAXID: 4932;
SOURCE 15 GENE: CCC2;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET11D
KEYWDS COPPER TRANSPORT, COMPLEX, STRUCTURAL GENOMICS, STRUCTURAL PROTEOMICS
KEYWDS 2 IN EUROPE, SPINE, CHAPERONE, METAL TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.BANCI,I.BERTINI,F.CANTINI,I.C.FELLI,L.GONNELLI,N.HADJILIADIS,
AUTHOR 2 R.PIERATTELLI,A.ROSATO,P.VOULGARIS,STRUCTURAL PROTEOMICS IN EUROPE
AUTHOR 3 (SPINE)
REVDAT 3 09-MAR-22 2GGP 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 2GGP 1 VERSN
REVDAT 1 08-AUG-06 2GGP 0
JRNL AUTH L.BANCI,I.BERTINI,F.CANTINI,I.C.FELLI,L.GONNELLI,
JRNL AUTH 2 N.HADJILIADIS,R.PIERATTELLI,A.ROSATO,P.VOULGARIS
JRNL TITL THE ATX1-CCC2 COMPLEX IS A METAL-MEDIATED PROTEIN-PROTEIN
JRNL TITL 2 INTERACTION.
JRNL REF NAT.CHEM.BIOL. V. 2 367 2006
JRNL REFN ISSN 1552-4450
JRNL PMID 16732294
JRNL DOI 10.1038/NCHEMBIO797
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : AMBER 8.0
REMARK 3 AUTHORS : CASE, D.A. ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2GGP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000037095.
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 : 100 MM KPI
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM ATX1 U-15N,13C, 1MM CCC2A
REMARK 210 UNLABELED, 1MM CU(I), 100MM KPI,
REMARK 210 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 2D 15N
REMARK 210 EDITED NOESY; 2D 13C EDITED
REMARK 210 NOESY; 2D 13C FILTERED NOESY;
REMARK 210 NOESY FOR INTERMOLECULAR NOES
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 REMARK: NULL
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 1 ARG B 2 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 3 ARG B 2 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 3 ARG B 25 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 4 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 5 ARG B 70 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 7 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 7 ARG B 25 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 11 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 11 ARG B 25 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 12 ARG B 25 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 12 TYR B 46 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 12 ARG B 70 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 13 ARG A 68 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 13 ARG B 2 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 14 ARG B 25 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 14 ARG B 70 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 15 ARG B 25 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 16 ARG B 70 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 17 ARG B 70 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 18 ARG B 70 NE - CZ - NH1 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 ALA A 2 14.50 86.11
REMARK 500 1 ARG B 2 -151.24 -84.92
REMARK 500 1 GLU B 3 148.09 -172.92
REMARK 500 1 VAL B 8 74.55 -107.98
REMARK 500 1 THR B 12 -61.85 -141.45
REMARK 500 1 LYS B 28 25.53 -71.43
REMARK 500 1 ASN B 40 15.50 51.74
REMARK 500 1 ASN B 48 156.61 178.12
REMARK 500 1 GLU B 49 20.36 104.22
REMARK 500 1 PHE B 64 -164.63 -107.89
REMARK 500 1 ASP B 71 32.98 -87.59
REMARK 500 2 ALA A 2 -26.76 -141.43
REMARK 500 2 ILE A 4 146.37 72.88
REMARK 500 2 SER A 39 77.34 -102.36
REMARK 500 2 GLN A 43 10.20 80.39
REMARK 500 2 THR B 12 144.96 -170.65
REMARK 500 2 CYS B 13 -150.97 53.35
REMARK 500 2 SER B 14 -89.05 -118.05
REMARK 500 2 ASN B 40 18.94 50.64
REMARK 500 2 PHE B 64 -155.82 -109.93
REMARK 500 2 ASP B 71 23.03 -73.82
REMARK 500 3 GLN A 43 27.22 49.93
REMARK 500 3 THR B 12 -37.87 167.02
REMARK 500 3 ALA B 15 -24.14 -141.21
REMARK 500 3 TYR B 46 -144.08 -152.75
REMARK 500 4 ASP A 32 -30.95 -130.74
REMARK 500 4 ILE B 20 -64.56 -95.70
REMARK 500 4 TYR B 46 -151.46 -147.40
REMARK 500 4 PHE B 64 -167.09 -114.96
REMARK 500 4 ILE B 68 78.71 47.36
REMARK 500 4 ARG B 70 140.30 -170.26
REMARK 500 4 ASP B 71 36.31 -80.85
REMARK 500 5 GLN A 43 18.70 56.85
REMARK 500 5 THR B 12 -68.21 71.52
REMARK 500 5 ALA B 15 -44.64 -132.01
REMARK 500 5 ASN B 40 75.15 66.47
REMARK 500 5 ASN B 48 155.11 99.64
REMARK 500 5 GLU B 49 34.33 -71.75
REMARK 500 5 LYS B 56 32.49 -65.95
REMARK 500 5 GLU B 57 -42.83 -151.60
REMARK 500 5 PHE B 64 -163.52 -121.28
REMARK 500 5 ASP B 71 32.52 -67.86
REMARK 500 6 ALA A 2 -11.78 -160.21
REMARK 500 6 GLN A 43 19.78 59.91
REMARK 500 6 ARG B 2 147.81 179.85
REMARK 500 6 THR B 12 -17.47 -157.06
REMARK 500 6 TYR B 46 -144.60 -153.47
REMARK 500 6 LYS B 56 13.99 -69.61
REMARK 500 6 PHE B 64 -154.93 -115.81
REMARK 500 6 ASP B 71 22.03 -69.94
REMARK 500
REMARK 500 THIS ENTRY HAS 152 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 ASP B 65 CYS B 66 1 -148.56
REMARK 500 TYR B 46 ASP B 47 5 147.44
REMARK 500 ASP B 65 CYS B 66 7 -146.79
REMARK 500 ARG B 70 ASP B 71 7 147.04
REMARK 500 GLU B 67 ILE B 68 8 -147.07
REMARK 500 ASN B 18 THR B 19 13 145.12
REMARK 500 ASP B 65 CYS B 66 15 -149.81
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 68 0.09 SIDE CHAIN
REMARK 500 2 ARG B 70 0.09 SIDE CHAIN
REMARK 500 11 ARG B 70 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 B 73 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 15 SG
REMARK 620 2 CYS B 13 SG 106.5
REMARK 620 3 CYS B 16 SG 117.9 106.0
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 B 73
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: P38636 RELATED DB: TARGETDB
REMARK 900 RELATED ID: P38360 RELATED DB: TARGETDB
DBREF 2GGP A 1 73 UNP P38636 ATX1_YEAST 1 73
DBREF 2GGP B 2 72 UNP P38995 ATU2_YEAST 2 72
SEQADV 2GGP ALA B 1 UNP P38995 CLONING ARTIFACT
SEQRES 1 A 73 MET ALA GLU ILE LYS HIS TYR GLN PHE ASN VAL VAL MET
SEQRES 2 A 73 THR CYS SER GLY CYS SER GLY ALA VAL ASN LYS VAL LEU
SEQRES 3 A 73 THR LYS LEU GLU PRO ASP VAL SER LYS ILE ASP ILE SER
SEQRES 4 A 73 LEU GLU LYS GLN LEU VAL ASP VAL TYR THR THR LEU PRO
SEQRES 5 A 73 TYR ASP PHE ILE LEU GLU LYS ILE LYS LYS THR GLY LYS
SEQRES 6 A 73 GLU VAL ARG SER GLY LYS GLN LEU
SEQRES 1 B 72 ALA ARG GLU VAL ILE LEU ALA VAL HIS GLY MET THR CYS
SEQRES 2 B 72 SER ALA CYS THR ASN THR ILE ASN THR GLN LEU ARG ALA
SEQRES 3 B 72 LEU LYS GLY VAL THR LYS CYS ASP ILE SER LEU VAL THR
SEQRES 4 B 72 ASN GLU CYS GLN VAL THR TYR ASP ASN GLU VAL THR ALA
SEQRES 5 B 72 ASP SER ILE LYS GLU ILE ILE GLU ASP CYS GLY PHE ASP
SEQRES 6 B 72 CYS GLU ILE LEU ARG ASP SER
HET CU1 B 73 1
HETNAM CU1 COPPER (I) ION
FORMUL 3 CU1 CU 1+
HELIX 1 1 CYS A 15 LYS A 28 1 14
HELIX 2 2 PRO A 52 GLY A 64 1 13
HELIX 3 3 THR B 17 ARG B 25 1 9
HELIX 4 4 THR B 51 CYS B 62 1 12
SHEET 1 A 4 VAL A 33 SER A 39 0
SHEET 2 A 4 LEU A 44 THR A 49 -1 O LEU A 44 N SER A 39
SHEET 3 A 4 LYS A 5 VAL A 11 -1 N LYS A 5 O THR A 49
SHEET 4 A 4 VAL A 67 GLN A 72 -1 O LYS A 71 N GLN A 8
SHEET 1 B 4 VAL B 30 ILE B 35 0
SHEET 2 B 4 GLU B 41 TYR B 46 -1 O GLN B 43 N ASP B 34
SHEET 3 B 4 ARG B 2 ALA B 7 -1 N VAL B 4 O VAL B 44
SHEET 4 B 4 GLU B 67 ARG B 70 -1 O ARG B 70 N ILE B 5
LINK SG CYS A 15 CU CU1 B 73 1555 1555 2.18
LINK SG CYS B 13 CU CU1 B 73 1555 1555 2.16
LINK SG CYS B 16 CU CU1 B 73 1555 1555 2.20
SITE 1 AC1 4 CYS A 15 CYS B 13 ALA B 15 CYS B 16
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 9 2 Bytes