Header list of 2ga7.pdb file
Complete list - t 20 2 Bytes
HEADER HYDROLASE 08-MAR-06 2GA7
TITLE SOLUTION STRUCTURE OF THE COPPER(I) FORM OF THE THIRD METAL-BINDING
TITLE 2 DOMAIN OF ATP7A PROTEIN (MENKES DISEASE PROTEIN)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: COPPER-TRANSPORTING ATPASE 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THIRD SOLUBLE DOMAIN, RESIDUES 275-352;
COMPND 5 SYNONYM: COPPER PUMP 1, MENKES DISEASE-ASSOCIATED PROTEIN;
COMPND 6 EC: 3.6.3.4;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: 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, MC1, MNK;
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
KEYWDS SOLUTION STRUCTURE, MENKES DISEASE-ASSOCIATED PROTEIN, COPPER(I),
KEYWDS 2 STRUCTURAL GENOMICS, STRUCTURAL PROTEOMICS IN EUROPE, SPINE,
KEYWDS 3 HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,F.CANTINI,N.DELLAMALVA,A.ROSATO,T.HERRMANN,
AUTHOR 2 K.WUTHRICH,STRUCTURAL PROTEOMICS IN EUROPE (SPINE)
REVDAT 4 20-OCT-21 2GA7 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2GA7 1 VERSN
REVDAT 2 10-OCT-06 2GA7 1 JRNL
REVDAT 1 01-AUG-06 2GA7 0
JRNL AUTH L.BANCI,I.BERTINI,F.CANTINI,N.DELLAMALVA,T.HERRMANN,
JRNL AUTH 2 A.ROSATO,K.WUTHRICH
JRNL TITL SOLUTION STRUCTURE AND INTERMOLECULAR INTERACTIONS OF THE
JRNL TITL 2 THIRD METAL-BINDING DOMAIN OF ATP7A, THE MENKES DISEASE
JRNL TITL 3 PROTEIN.
JRNL REF J.BIOL.CHEM. V. 281 29141 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16873374
JRNL DOI 10.1074/JBC.M603176200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.3, AMBER 8.0
REMARK 3 AUTHORS : CASE, D.A. ET AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1011 MEANINGFUL PROTON-PROTON DISTANCE
REMARK 3 RESTRAINTS, 143 DIHEDRAL ANGLES RESTRAINTS WERE USED FOR
REMARK 3 STRUCTURE CALCULATIONS
REMARK 4
REMARK 4 2GA7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAR-06.
REMARK 100 THE DEPOSITION ID IS D_1000036882.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7
REMARK 210 IONIC STRENGTH : 100MM PHOSPHATE BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM COPPER(I)MNK3 UNLABELLED
REMARK 210 SAMPLE, 100MM PHOSPHATE BUFFER,
REMARK 210 PH 7.0, 90% H2O, 10% D2O; 0.5MM
REMARK 210 COPPER(I)MNK3 15N LABELED SAMPLE,
REMARK 210 100MM PHOSPHATE BUFFER, PH 7.0,
REMARK 210 90% H2O, 10% D2O; 0.5MM COPPER(I)
REMARK 210 MNK3 15N,13C LABELED SAMPLE,
REMARK 210 100MM PHOSPHATE BUFFER, PH 7.0,
REMARK 210 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; CBCACONH;
REMARK 210 CBCANH; H(CCH)-TOCSY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 15N-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 700 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3, CARA 1.5, CYANA 2.1
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 : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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: 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-30
REMARK 465 RES C SSSEQI
REMARK 465 GLU A 78
REMARK 465 ILE A 79
REMARK 465 GLU A 80
REMARK 465 GLY A 81
REMARK 465 ARG A 82
REMARK 465 LEU A 83
REMARK 465 GLU A 84
REMARK 465 HIS A 85
REMARK 465 HIS A 86
REMARK 465 HIS A 87
REMARK 465 HIS A 88
REMARK 465 HIS A 89
REMARK 465 HIS A 90
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 HG SER A 19 OE2 GLU A 22 1.59
REMARK 500 OE2 GLU A 55 HG SER A 75 1.59
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 CYS A 17 N - CA - CB ANGL. DEV. = -11.6 DEGREES
REMARK 500 2 CYS A 17 N - CA - CB ANGL. DEV. = -12.1 DEGREES
REMARK 500 2 VAL A 18 CA - CB - CG1 ANGL. DEV. = 9.8 DEGREES
REMARK 500 2 TYR A 30 CB - CG - CD2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 2 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 2 VAL A 64 CG1 - CB - CG2 ANGL. DEV. = -13.5 DEGREES
REMARK 500 4 CYS A 17 N - CA - CB ANGL. DEV. = -12.5 DEGREES
REMARK 500 5 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 6 CYS A 17 N - CA - CB ANGL. DEV. = -13.3 DEGREES
REMARK 500 6 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 6 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 7 CYS A 17 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 8 CYS A 17 N - CA - CB ANGL. DEV. = -12.1 DEGREES
REMARK 500 9 CYS A 17 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 9 VAL A 35 CA - CB - CG1 ANGL. DEV. = 13.5 DEGREES
REMARK 500 11 VAL A 18 CA - CB - CG1 ANGL. DEV. = 13.3 DEGREES
REMARK 500 11 ARG A 58 CD - NE - CZ ANGL. DEV. = 8.4 DEGREES
REMARK 500 11 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 11 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 13 CYS A 17 N - CA - CB ANGL. DEV. = -13.5 DEGREES
REMARK 500 14 VAL A 18 CA - CB - CG1 ANGL. DEV. = 9.1 DEGREES
REMARK 500 14 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 15 CYS A 17 CA - CB - SG ANGL. DEV. = 7.6 DEGREES
REMARK 500 15 VAL A 18 CA - CB - CG1 ANGL. DEV. = 12.3 DEGREES
REMARK 500 15 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 16 VAL A 18 CA - CB - CG1 ANGL. DEV. = 9.6 DEGREES
REMARK 500 17 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 18 CYS A 17 CA - CB - SG ANGL. DEV. = 8.6 DEGREES
REMARK 500 19 CYS A 17 N - CA - CB ANGL. DEV. = -13.1 DEGREES
REMARK 500 19 TYR A 69 CB - CG - CD2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 20 CYS A 17 N - CA - CB ANGL. DEV. = -10.9 DEGREES
REMARK 500 20 TYR A 30 CB - CG - CD2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 20 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 20 ARG A 70 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 20 ARG A 70 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES
REMARK 500 21 TYR A 69 CB - CG - CD2 ANGL. DEV. = -4.5 DEGREES
REMARK 500 21 TYR A 69 CB - CG - CD1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 22 CYS A 17 CA - CB - SG ANGL. DEV. = 7.8 DEGREES
REMARK 500 23 CYS A 17 N - CA - CB ANGL. DEV. = -11.2 DEGREES
REMARK 500 23 ARG A 58 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 24 CYS A 17 N - CA - CB ANGL. DEV. = -12.5 DEGREES
REMARK 500 24 VAL A 35 CA - CB - CG1 ANGL. DEV. = 11.6 DEGREES
REMARK 500 24 TYR A 69 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 25 CYS A 17 N - CA - CB ANGL. DEV. = -14.2 DEGREES
REMARK 500 25 ARG A 58 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 25 TYR A 69 CB - CG - CD2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 26 CYS A 17 N - CA - CB ANGL. DEV. = -12.9 DEGREES
REMARK 500 27 CYS A 17 CA - CB - SG ANGL. DEV. = 6.8 DEGREES
REMARK 500 27 ARG A 41 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 68 ANGLE DEVIATIONS.
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 MET A 12 -169.38 68.46
REMARK 500 1 SER A 16 -36.18 -39.15
REMARK 500 1 CYS A 17 -39.78 -30.11
REMARK 500 1 GLN A 29 45.07 -80.55
REMARK 500 1 TYR A 30 28.72 -172.53
REMARK 500 1 VAL A 35 38.39 -153.14
REMARK 500 1 ASN A 40 -106.48 -76.13
REMARK 500 1 ARG A 41 37.92 171.39
REMARK 500 1 SER A 50 -87.78 144.96
REMARK 500 1 SER A 51 30.56 -72.51
REMARK 500 1 LEU A 68 -61.14 -109.36
REMARK 500 1 ARG A 70 37.91 -71.02
REMARK 500 1 GLU A 76 76.36 -157.86
REMARK 500 2 ASP A 10 78.76 -115.03
REMARK 500 2 CYS A 17 -34.80 -34.68
REMARK 500 2 VAL A 35 48.37 -158.89
REMARK 500 2 SER A 50 14.42 -69.80
REMARK 500 2 GLU A 55 -33.63 -39.99
REMARK 500 2 SER A 65 90.90 -166.38
REMARK 500 2 ARG A 70 42.01 -66.25
REMARK 500 3 LYS A 15 -9.38 48.60
REMARK 500 3 CYS A 17 -32.66 -36.63
REMARK 500 3 LEU A 28 38.98 -73.16
REMARK 500 3 GLN A 29 -93.63 73.92
REMARK 500 3 TYR A 30 38.02 -75.58
REMARK 500 3 VAL A 35 50.81 -154.30
REMARK 500 3 ASN A 40 -108.99 -89.05
REMARK 500 3 ARG A 41 22.81 -162.14
REMARK 500 3 VAL A 52 35.21 -73.17
REMARK 500 3 SER A 65 69.15 -170.02
REMARK 500 3 ARG A 70 63.16 -67.98
REMARK 500 3 SER A 75 149.57 178.79
REMARK 500 4 MET A 12 164.56 75.76
REMARK 500 4 LYS A 15 10.12 50.18
REMARK 500 4 SER A 16 -37.44 -38.34
REMARK 500 4 CYS A 17 -42.87 -29.28
REMARK 500 4 TYR A 30 -5.05 58.83
REMARK 500 4 VAL A 35 36.51 -160.46
REMARK 500 4 ASN A 40 -115.78 -82.52
REMARK 500 4 ARG A 41 14.06 -158.33
REMARK 500 4 ALA A 49 61.52 -113.07
REMARK 500 4 VAL A 52 47.41 -80.30
REMARK 500 4 SER A 65 69.80 -162.16
REMARK 500 5 HIS A 13 -38.84 80.83
REMARK 500 5 GLN A 29 -7.14 -59.55
REMARK 500 5 TYR A 30 31.59 -160.58
REMARK 500 5 VAL A 35 51.47 -160.63
REMARK 500 5 VAL A 52 44.48 -75.08
REMARK 500 6 ASP A 2 -157.27 -87.27
REMARK 500 6 SER A 16 -36.82 -38.02
REMARK 500
REMARK 500 THIS ENTRY HAS 331 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 3 PHE A 7 0.08 SIDE CHAIN
REMARK 500 3 ARG A 41 0.13 SIDE CHAIN
REMARK 500 3 TYR A 47 0.06 SIDE CHAIN
REMARK 500 4 ARG A 41 0.10 SIDE CHAIN
REMARK 500 4 TYR A 47 0.08 SIDE CHAIN
REMARK 500 5 ARG A 41 0.16 SIDE CHAIN
REMARK 500 6 TYR A 47 0.09 SIDE CHAIN
REMARK 500 6 ARG A 58 0.12 SIDE CHAIN
REMARK 500 7 PHE A 7 0.08 SIDE CHAIN
REMARK 500 8 ARG A 58 0.09 SIDE CHAIN
REMARK 500 10 PHE A 7 0.08 SIDE CHAIN
REMARK 500 11 TYR A 69 0.06 SIDE CHAIN
REMARK 500 12 TYR A 69 0.08 SIDE CHAIN
REMARK 500 14 PHE A 7 0.09 SIDE CHAIN
REMARK 500 14 TYR A 47 0.07 SIDE CHAIN
REMARK 500 15 PHE A 7 0.07 SIDE CHAIN
REMARK 500 15 ARG A 58 0.22 SIDE CHAIN
REMARK 500 16 TYR A 47 0.11 SIDE CHAIN
REMARK 500 17 TYR A 47 0.07 SIDE CHAIN
REMARK 500 18 ARG A 41 0.16 SIDE CHAIN
REMARK 500 18 TYR A 47 0.10 SIDE CHAIN
REMARK 500 19 PHE A 7 0.08 SIDE CHAIN
REMARK 500 19 TYR A 47 0.07 SIDE CHAIN
REMARK 500 20 TYR A 47 0.08 SIDE CHAIN
REMARK 500 21 TYR A 30 0.10 SIDE CHAIN
REMARK 500 21 TYR A 47 0.07 SIDE CHAIN
REMARK 500 23 TYR A 47 0.10 SIDE CHAIN
REMARK 500 24 PHE A 7 0.09 SIDE CHAIN
REMARK 500 24 TYR A 47 0.07 SIDE CHAIN
REMARK 500 24 ARG A 58 0.09 SIDE CHAIN
REMARK 500 25 ARG A 41 0.09 SIDE CHAIN
REMARK 500 26 TYR A 47 0.08 SIDE CHAIN
REMARK 500 27 PHE A 7 0.10 SIDE CHAIN
REMARK 500 27 ARG A 41 0.16 SIDE CHAIN
REMARK 500 28 TYR A 30 0.10 SIDE CHAIN
REMARK 500 28 TYR A 47 0.08 SIDE CHAIN
REMARK 500 29 ARG A 58 0.08 SIDE CHAIN
REMARK 500 30 PHE A 7 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 23 SER A 50 10.65
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 178 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 14 SG
REMARK 620 2 CYS A 17 SG 172.6
REMARK 620 N 1
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 178
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2G9O RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE APO FORM OF THE THIRD METAL-BINDING
REMARK 900 DOMAIN OF ATP7A PROTEIN (MENKES DISEASE PROTEIN)
REMARK 900 RELATED ID: CIRMMP50 RELATED DB: TARGETDB
DBREF 2GA7 A 1 78 UNP Q04656 ATP7A_HUMAN 275 352
SEQADV 2GA7 VAL A 46 UNP Q04656 LYS 320 ENGINEERED MUTATION
SEQADV 2GA7 ILE A 79 UNP Q04656 CLONING ARTIFACT
SEQADV 2GA7 GLU A 80 UNP Q04656 CLONING ARTIFACT
SEQADV 2GA7 GLY A 81 UNP Q04656 CLONING ARTIFACT
SEQADV 2GA7 ARG A 82 UNP Q04656 CLONING ARTIFACT
SEQADV 2GA7 LEU A 83 UNP Q04656 CLONING ARTIFACT
SEQADV 2GA7 GLU A 84 UNP Q04656 CLONING ARTIFACT
SEQADV 2GA7 HIS A 85 UNP Q04656 EXPRESSION TAG
SEQADV 2GA7 HIS A 86 UNP Q04656 EXPRESSION TAG
SEQADV 2GA7 HIS A 87 UNP Q04656 EXPRESSION TAG
SEQADV 2GA7 HIS A 88 UNP Q04656 EXPRESSION TAG
SEQADV 2GA7 HIS A 89 UNP Q04656 EXPRESSION TAG
SEQADV 2GA7 HIS A 90 UNP Q04656 EXPRESSION TAG
SEQRES 1 A 90 ASN ASP SER THR ALA THR PHE ILE ILE ASP GLY MET HIS
SEQRES 2 A 90 CYS LYS SER CYS VAL SER ASN ILE GLU SER THR LEU SER
SEQRES 3 A 90 ALA LEU GLN TYR VAL SER SER ILE VAL VAL SER LEU GLU
SEQRES 4 A 90 ASN ARG SER ALA ILE VAL VAL TYR ASN ALA SER SER VAL
SEQRES 5 A 90 THR PRO GLU SER LEU ARG LYS ALA ILE GLU ALA VAL SER
SEQRES 6 A 90 PRO GLY LEU TYR ARG VAL SER ILE THR SER GLU VAL GLU
SEQRES 7 A 90 ILE GLU GLY ARG LEU GLU HIS HIS HIS HIS HIS HIS
HET CU1 A 178 1
HETNAM CU1 COPPER (I) ION
FORMUL 2 CU1 CU 1+
HELIX 1 1 SER A 16 SER A 26 1 11
HELIX 2 2 THR A 53 SER A 56 5 4
HELIX 3 3 LEU A 57 SER A 65 1 9
SHEET 1 A 4 VAL A 31 ILE A 34 0
SHEET 2 A 4 SER A 42 TYR A 47 -1 O VAL A 46 N SER A 33
SHEET 3 A 4 SER A 3 ILE A 8 -1 N PHE A 7 O ALA A 43
SHEET 4 A 4 SER A 72 ILE A 73 -1 O SER A 72 N ILE A 8
LINK SG CYS A 14 CU CU1 A 178 1555 1555 2.26
LINK SG CYS A 17 CU CU1 A 178 1555 1555 2.26
SITE 1 AC1 5 MET A 12 CYS A 14 LYS A 15 SER A 16
SITE 2 AC1 5 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 - t 20 2 Bytes