Header list of 1y3j.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 25-NOV-04 1Y3J
TITLE SOLUTION STRUCTURE OF THE COPPER(I) FORM OF THE FIFTH DOMAIN OF MENKES
TITLE 2 PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER-TRANSPORTING ATPASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FIFTH DOMAIN OF THE MENKES PROTEIN;
COMPND 5 SYNONYM: MENKES PROTEIN, COPPER PUMP 1, MENKES DISEASE-ASSOCIATED
COMPND 6 PROTEIN;
COMPND 7 EC: 3.6.3.4;
COMPND 8 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: ATP7A;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET20B(+)
KEYWDS FERRODOXIN-LIKE FOLD, BETA-ALPHA-BETA-BETA-ALPHA-BETA STRUCTURE,
KEYWDS 2 STRUCTURAL PROTEOMICS IN EUROPE, SPINE, STRUCTURAL GENOMICS,
KEYWDS 3 HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.BANCI,C.T.CHASAPIS,S.CIOFI-BAFFONI,N.HADJILIADIS,A.ROSATO,
AUTHOR 2 STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 3 02-MAR-22 1Y3J 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1Y3J 1 VERSN
REVDAT 1 08-MAR-05 1Y3J 0
JRNL AUTH L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,C.T.CHASAPIS,
JRNL AUTH 2 N.HADJILIADIS,A.ROSATO
JRNL TITL AN NMR STUDY OF THE INTERACTION BETWEEN THE HUMAN COPPER(I)
JRNL TITL 2 CHAPERONE AND THE SECOND AND FIFTH METAL-BINDING DOMAINS OF
JRNL TITL 3 THE MENKES PROTEIN
JRNL REF FEBS J. V. 272 865 2005
JRNL REFN ISSN 1742-464X
JRNL PMID 15670166
JRNL DOI 10.1111/J.1742-4658.2004.04526.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, 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 ARE BASED ON NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS AND DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1Y3J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031070.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 50MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM MNK5 DOMAIN U-15N,13C; 50MM
REMARK 210 PHOSPHATE BUFFER NA
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; CBCANH;
REMARK 210 CBCA(CO)NH; HCCH-TOCSY; HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 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 : NEASY, DYANA, XWINNMR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 3 PHE A 60 CB - CG - CD2 ANGL. DEV. = -4.6 DEGREES
REMARK 500 3 ARG A 62 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 5 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 6 ARG A 27 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 7 ARG A 46 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 10 TYR A 47 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 14 VAL A 18 CA - CB - CG1 ANGL. DEV. = 9.9 DEGREES
REMARK 500 14 ASN A 24 CA - CB - CG ANGL. DEV. = 13.9 DEGREES
REMARK 500 15 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 20 LEU A 25 CB - CA - C ANGL. DEV. = 11.4 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 THR A 13 41.97 -79.09
REMARK 500 1 ALA A 15 161.00 76.76
REMARK 500 1 SER A 16 -53.38 72.05
REMARK 500 1 CYS A 17 -54.65 -29.56
REMARK 500 1 GLU A 28 -176.66 169.76
REMARK 500 1 GLU A 29 53.46 84.82
REMARK 500 1 SER A 33 147.63 -170.21
REMARK 500 1 ALA A 37 53.54 -158.73
REMARK 500 1 GLN A 53 129.72 101.16
REMARK 500 2 MET A 12 -69.96 75.94
REMARK 500 2 ALA A 15 109.90 -52.61
REMARK 500 2 ARG A 26 -74.61 -21.50
REMARK 500 2 TYR A 32 47.03 -147.88
REMARK 500 2 MET A 39 44.22 -85.06
REMARK 500 2 ALA A 40 -36.71 -179.33
REMARK 500 2 PRO A 49 88.23 -61.79
REMARK 500 2 ALA A 50 -57.56 -169.97
REMARK 500 2 ILE A 52 -73.02 -93.61
REMARK 500 2 GLN A 53 134.99 117.17
REMARK 500 2 PHE A 66 -72.13 -135.53
REMARK 500 3 MET A 12 -71.71 66.38
REMARK 500 3 TYR A 32 48.13 -145.29
REMARK 500 3 ALA A 37 58.95 -155.62
REMARK 500 3 ALA A 50 -57.39 -150.27
REMARK 500 3 ILE A 52 -72.97 -90.54
REMARK 500 3 GLN A 53 136.66 112.98
REMARK 500 3 ALA A 68 81.52 -153.24
REMARK 500 4 THR A 10 94.30 -67.03
REMARK 500 4 ALA A 15 145.30 84.27
REMARK 500 4 SER A 16 -30.91 71.49
REMARK 500 4 ARG A 26 3.17 -63.00
REMARK 500 4 GLU A 28 33.15 78.86
REMARK 500 4 TYR A 32 42.51 -148.47
REMARK 500 4 ALA A 37 58.47 -155.92
REMARK 500 4 ALA A 50 -46.97 -165.53
REMARK 500 4 ILE A 52 -73.32 -113.17
REMARK 500 4 GLN A 53 131.93 110.86
REMARK 500 4 GLU A 72 -176.43 -173.52
REMARK 500 5 MET A 12 -66.38 62.92
REMARK 500 5 THR A 13 53.38 -151.72
REMARK 500 5 ALA A 15 93.99 -172.52
REMARK 500 5 GLU A 28 -108.52 -167.15
REMARK 500 5 TYR A 32 36.45 -148.22
REMARK 500 5 ALA A 37 57.02 -153.73
REMARK 500 5 ALA A 50 -43.71 -159.51
REMARK 500 5 ILE A 52 -128.50 -124.69
REMARK 500 5 GLN A 53 112.65 -175.18
REMARK 500 5 ASN A 73 126.23 165.46
REMARK 500 5 GLU A 75 64.70 26.67
REMARK 500 6 SER A 2 59.42 -165.08
REMARK 500
REMARK 500 THIS ENTRY HAS 213 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 TYR A 32 SER A 33 1 134.78
REMARK 500 LEU A 35 VAL A 36 1 123.05
REMARK 500 ARG A 27 GLU A 28 2 -134.30
REMARK 500 TYR A 32 SER A 33 2 148.65
REMARK 500 ARG A 26 ARG A 27 4 146.70
REMARK 500 TYR A 32 SER A 33 4 144.21
REMARK 500 GLY A 65 PHE A 66 4 -146.78
REMARK 500 TYR A 32 SER A 33 5 139.86
REMARK 500 GLY A 65 PHE A 66 5 -147.63
REMARK 500 GLY A 76 ARG A 77 5 -142.10
REMARK 500 SER A 16 CYS A 17 6 -146.48
REMARK 500 TYR A 32 SER A 33 6 122.32
REMARK 500 ARG A 27 GLU A 28 7 -149.66
REMARK 500 TYR A 32 SER A 33 7 140.84
REMARK 500 THR A 10 GLY A 11 9 138.31
REMARK 500 PHE A 66 GLY A 67 9 -149.56
REMARK 500 ASN A 1 SER A 2 10 133.87
REMARK 500 THR A 10 GLY A 11 10 -138.69
REMARK 500 TYR A 32 SER A 33 10 135.70
REMARK 500 ARG A 27 GLU A 28 11 -140.80
REMARK 500 TYR A 32 SER A 33 11 129.19
REMARK 500 VAL A 51 ILE A 52 11 -146.45
REMARK 500 THR A 10 GLY A 11 12 148.40
REMARK 500 TYR A 32 SER A 33 12 142.84
REMARK 500 TYR A 32 SER A 33 13 133.14
REMARK 500 SER A 16 CYS A 17 14 -99.73
REMARK 500 ARG A 27 GLU A 28 14 -146.60
REMARK 500 VAL A 51 ILE A 52 14 -149.81
REMARK 500 GLY A 11 MET A 12 15 136.90
REMARK 500 THR A 13 CYS A 14 15 119.70
REMARK 500 SER A 16 CYS A 17 15 -142.09
REMARK 500 GLU A 28 GLU A 29 15 -144.13
REMARK 500 ILE A 31 TYR A 32 15 146.10
REMARK 500 PHE A 66 GLY A 67 15 -143.50
REMARK 500 ARG A 27 GLU A 28 16 -144.78
REMARK 500 TYR A 32 SER A 33 16 145.79
REMARK 500 PHE A 66 GLY A 67 16 -149.91
REMARK 500 TYR A 32 SER A 33 17 144.45
REMARK 500 GLY A 65 PHE A 66 17 -147.02
REMARK 500 ARG A 26 ARG A 27 18 143.92
REMARK 500 TYR A 32 SER A 33 18 144.76
REMARK 500 GLY A 11 MET A 12 19 137.54
REMARK 500 ARG A 26 ARG A 27 19 145.65
REMARK 500 TYR A 32 SER A 33 19 141.37
REMARK 500 SER A 33 ILE A 34 19 149.29
REMARK 500 TYR A 32 SER A 33 20 145.02
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 27 0.09 SIDE CHAIN
REMARK 500 2 TYR A 6 0.13 SIDE CHAIN
REMARK 500 2 TYR A 47 0.10 SIDE CHAIN
REMARK 500 2 PHE A 66 0.10 SIDE CHAIN
REMARK 500 3 TYR A 6 0.17 SIDE CHAIN
REMARK 500 3 TYR A 47 0.08 SIDE CHAIN
REMARK 500 3 PHE A 60 0.18 SIDE CHAIN
REMARK 500 3 ARG A 62 0.11 SIDE CHAIN
REMARK 500 4 TYR A 32 0.19 SIDE CHAIN
REMARK 500 4 TYR A 47 0.12 SIDE CHAIN
REMARK 500 4 PHE A 60 0.15 SIDE CHAIN
REMARK 500 4 ARG A 77 0.12 SIDE CHAIN
REMARK 500 5 TYR A 6 0.08 SIDE CHAIN
REMARK 500 5 ARG A 27 0.09 SIDE CHAIN
REMARK 500 5 TYR A 32 0.08 SIDE CHAIN
REMARK 500 5 TYR A 47 0.15 SIDE CHAIN
REMARK 500 6 TYR A 6 0.15 SIDE CHAIN
REMARK 500 6 ARG A 27 0.07 SIDE CHAIN
REMARK 500 6 TYR A 47 0.07 SIDE CHAIN
REMARK 500 7 TYR A 6 0.13 SIDE CHAIN
REMARK 500 7 TYR A 32 0.11 SIDE CHAIN
REMARK 500 7 ARG A 62 0.13 SIDE CHAIN
REMARK 500 8 TYR A 6 0.11 SIDE CHAIN
REMARK 500 8 ARG A 62 0.09 SIDE CHAIN
REMARK 500 8 PHE A 66 0.07 SIDE CHAIN
REMARK 500 9 TYR A 6 0.10 SIDE CHAIN
REMARK 500 9 TYR A 32 0.08 SIDE CHAIN
REMARK 500 9 TYR A 47 0.09 SIDE CHAIN
REMARK 500 10 TYR A 32 0.09 SIDE CHAIN
REMARK 500 11 TYR A 6 0.09 SIDE CHAIN
REMARK 500 11 ARG A 26 0.16 SIDE CHAIN
REMARK 500 11 ARG A 77 0.17 SIDE CHAIN
REMARK 500 12 TYR A 6 0.07 SIDE CHAIN
REMARK 500 12 ARG A 62 0.08 SIDE CHAIN
REMARK 500 12 ARG A 77 0.12 SIDE CHAIN
REMARK 500 13 ARG A 26 0.09 SIDE CHAIN
REMARK 500 13 TYR A 32 0.08 SIDE CHAIN
REMARK 500 13 PHE A 66 0.11 SIDE CHAIN
REMARK 500 14 TYR A 6 0.10 SIDE CHAIN
REMARK 500 15 TYR A 6 0.07 SIDE CHAIN
REMARK 500 15 ARG A 27 0.08 SIDE CHAIN
REMARK 500 15 TYR A 47 0.09 SIDE CHAIN
REMARK 500 16 TYR A 6 0.17 SIDE CHAIN
REMARK 500 16 TYR A 32 0.13 SIDE CHAIN
REMARK 500 16 TYR A 47 0.11 SIDE CHAIN
REMARK 500 16 ARG A 62 0.09 SIDE CHAIN
REMARK 500 16 PHE A 66 0.09 SIDE CHAIN
REMARK 500 16 ARG A 77 0.12 SIDE CHAIN
REMARK 500 17 TYR A 32 0.07 SIDE CHAIN
REMARK 500 17 TYR A 47 0.08 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 61 PLANE DEVIATIONS.
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 CU A 78 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 14 SG
REMARK 620 2 ALA A 15 O 107.5
REMARK 620 3 CYS A 17 SG 111.0 104.5
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 CU A 78
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Y3K RELATED DB: PDB
REMARK 900 THE SAME PROTEIN OF THE APO FORM
REMARK 900 RELATED ID: CIRMMP26 RELATED DB: TARGETDB
DBREF 1Y3J A 1 73 UNP Q04656 ATP7A_HUMAN 486 558
SEQADV 1Y3J ILE A 74 UNP Q04656 CLONING ARTIFACT
SEQADV 1Y3J GLU A 75 UNP Q04656 CLONING ARTIFACT
SEQADV 1Y3J GLY A 76 UNP Q04656 CLONING ARTIFACT
SEQADV 1Y3J ARG A 77 UNP Q04656 CLONING ARTIFACT
SEQRES 1 A 77 ASN SER SER LYS CYS TYR ILE GLN VAL THR GLY MET THR
SEQRES 2 A 77 CYS ALA SER CYS VAL ALA ASN ILE GLU ARG ASN LEU ARG
SEQRES 3 A 77 ARG GLU GLU GLY ILE TYR SER ILE LEU VAL ALA LEU MET
SEQRES 4 A 77 ALA GLY LYS ALA GLU VAL ARG TYR ASN PRO ALA VAL ILE
SEQRES 5 A 77 GLN PRO PRO MET ILE ALA GLU PHE ILE ARG GLU LEU GLY
SEQRES 6 A 77 PHE GLY ALA THR VAL ILE GLU ASN ILE GLU GLY ARG
HET CU A 78 1
HETNAM CU COPPER (II) ION
FORMUL 2 CU CU 2+
HELIX 1 1 GLY A 11 ALA A 15 5 5
HELIX 2 2 SER A 16 ARG A 26 1 11
HELIX 3 3 GLN A 53 GLY A 65 1 13
SHEET 1 A 4 ILE A 31 SER A 33 0
SHEET 2 A 4 ALA A 43 TYR A 47 -1 O ARG A 46 N SER A 33
SHEET 3 A 4 SER A 3 VAL A 9 -1 N SER A 3 O TYR A 47
SHEET 4 A 4 ALA A 68 ILE A 71 -1 O ILE A 71 N TYR A 6
LINK SG CYS A 14 CU CU A 78 1555 1555 2.18
LINK O ALA A 15 CU CU A 78 1555 1555 2.65
LINK SG CYS A 17 CU CU A 78 1555 1555 2.18
SITE 1 AC1 3 CYS A 14 ALA A 15 CYS A 17
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