Header list of 1kqk.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE 07-JAN-02 1KQK
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF A POTENTIAL COPPER-
TITLE 2 TRANSLOCATING P-TYPE ATPASE FROM BACILLUS SUBTILIS IN THE CU(I)LOADED
TITLE 3 STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTENTIAL COPPER-TRANSPORTING ATPASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: P-TYPE ATPASE, COPA;
COMPND 6 EC: 3.6.3.4;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: YVGX;
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 COPA, FOLDING, P-TYPE ATPASE, COPPER TRANSPORTING PROTEIN, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,M.D'ONOFRIO,L.GONNELLI,
AUTHOR 2 F.C.MARHUENDA-EGEA,F.J.RUIZ-DUENAS
REVDAT 4 23-FEB-22 1KQK 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1KQK 1 VERSN
REVDAT 2 01-APR-03 1KQK 1 JRNL
REVDAT 1 17-APR-02 1KQK 0
JRNL AUTH L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,M.D'ONOFRIO,L.GONNELLI,
JRNL AUTH 2 F.C.MARHUENDA-EGEA,F.J.RUIZ-DUENAS
JRNL TITL SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF A POTENTIAL
JRNL TITL 2 COPPER-TRANSLOCATING P-TYPE ATPASE FROM BACILLUS SUBTILIS IN
JRNL TITL 3 THE APO AND CU(I) LOADED STATES.
JRNL REF J.MOL.BIOL. V. 317 415 2002
JRNL REFN ISSN 0022-2836
JRNL PMID 11922674
JRNL DOI 10.1006/JMBI.2002.5430
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CORMA, AMBER 5.0
REMARK 3 AUTHORS : BORGIAS, B.; THOMAS, P.D.; JAMES, T.L. (CORMA),
REMARK 3 PEARLMAN, D.A.; CASE, D.A.; CALDWELL, J.W.; ROSS,
REMARK 3 W.S.; CHEATHAM, T.E.; FERGUSON, D.M.; SEIBEL, G.L.;
REMARK 3 SINGH, U.C.; WEINER, P.K.; KOLLMAN, P.A. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1502 RESTRAINTS, 1415 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 87 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1KQK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-JAN-02.
REMARK 100 THE DEPOSITION ID IS D_1000015235.
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 NA
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM CU(I)COPA 15N; 100MM
REMARK 210 PHOSPHATE BUFFER NA; 90%H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNHA; 3D 15N NOESY-HSQC; 2D
REMARK 210 NOESY; 2D TOCSY
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 : DYANA 1.5, XEASY 3.2, XWINNMR
REMARK 210 2.6
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
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 : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR AND 3D HETERONUCLEAR TECHNIQUES
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: 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 26 ARG A 80 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 THR A 2 -177.11 54.41
REMARK 500 1 ALA A 34 61.13 -179.23
REMARK 500 1 ALA A 39 -57.38 -159.64
REMARK 500 1 LYS A 50 -60.08 -144.94
REMARK 500 1 GLU A 73 31.94 -166.16
REMARK 500 1 GLN A 74 54.38 -159.11
REMARK 500 1 ILE A 77 -68.24 71.05
REMARK 500 1 GLU A 78 155.70 65.37
REMARK 500 2 MET A 12 73.23 32.80
REMARK 500 2 ALA A 34 59.94 -172.28
REMARK 500 2 ALA A 39 -55.93 -138.95
REMARK 500 2 LYS A 50 -56.65 -136.30
REMARK 500 2 LYS A 71 -146.92 -125.47
REMARK 500 2 GLN A 74 72.97 52.06
REMARK 500 2 ILE A 77 90.90 -161.40
REMARK 500 3 MET A 12 45.08 -82.63
REMARK 500 3 CYS A 14 -30.29 -156.10
REMARK 500 3 ALA A 15 -55.73 74.88
REMARK 500 3 ALA A 34 67.55 -178.79
REMARK 500 3 ALA A 39 -60.96 -160.57
REMARK 500 3 LYS A 50 -19.15 -154.67
REMARK 500 3 LYS A 71 -51.73 -127.10
REMARK 500 3 SER A 76 -73.40 -88.61
REMARK 500 3 ILE A 77 80.29 54.48
REMARK 500 4 MET A 12 59.37 21.56
REMARK 500 4 ALA A 34 55.09 -169.29
REMARK 500 4 ALA A 39 -49.95 -154.18
REMARK 500 4 GLU A 41 49.91 81.58
REMARK 500 4 LYS A 50 -55.63 -135.65
REMARK 500 4 LYS A 71 -51.55 -124.49
REMARK 500 4 GLU A 73 40.14 -165.53
REMARK 500 4 GLN A 74 54.11 -162.06
REMARK 500 5 ALA A 34 57.18 -175.62
REMARK 500 5 ALA A 39 -55.74 -167.62
REMARK 500 5 GLU A 51 -67.22 -141.25
REMARK 500 5 LYS A 71 -51.07 -131.08
REMARK 500 5 GLN A 74 -47.29 177.16
REMARK 500 5 ASP A 75 -59.88 77.91
REMARK 500 5 ILE A 77 -84.75 -131.45
REMARK 500 5 GLU A 78 -97.78 -168.93
REMARK 500 6 MET A 12 64.53 33.56
REMARK 500 6 ALA A 34 56.91 -169.65
REMARK 500 6 ALA A 39 -55.30 -159.16
REMARK 500 6 GLU A 51 -61.38 -137.09
REMARK 500 6 LYS A 63 10.11 -69.46
REMARK 500 6 LYS A 71 -53.90 -121.24
REMARK 500 6 GLN A 74 123.25 68.19
REMARK 500 6 ILE A 77 105.87 -45.73
REMARK 500 7 THR A 2 172.14 66.77
REMARK 500 7 MET A 12 57.56 30.71
REMARK 500
REMARK 500 THIS ENTRY HAS 253 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 20 0.11 SIDE CHAIN
REMARK 500 4 TYR A 47 0.07 SIDE CHAIN
REMARK 500 4 TYR A 66 0.10 SIDE CHAIN
REMARK 500 5 TYR A 47 0.06 SIDE CHAIN
REMARK 500 7 TYR A 66 0.11 SIDE CHAIN
REMARK 500 9 TYR A 47 0.09 SIDE CHAIN
REMARK 500 10 TYR A 47 0.10 SIDE CHAIN
REMARK 500 12 TYR A 47 0.07 SIDE CHAIN
REMARK 500 13 TYR A 47 0.08 SIDE CHAIN
REMARK 500 14 TYR A 66 0.09 SIDE CHAIN
REMARK 500 15 TYR A 66 0.09 SIDE CHAIN
REMARK 500 15 ARG A 80 0.10 SIDE CHAIN
REMARK 500 16 TYR A 47 0.09 SIDE CHAIN
REMARK 500 18 ARG A 20 0.09 SIDE CHAIN
REMARK 500 18 TYR A 47 0.11 SIDE CHAIN
REMARK 500 18 TYR A 66 0.08 SIDE CHAIN
REMARK 500 19 TYR A 47 0.07 SIDE CHAIN
REMARK 500 19 TYR A 66 0.09 SIDE CHAIN
REMARK 500 20 TYR A 47 0.06 SIDE CHAIN
REMARK 500 22 TYR A 66 0.08 SIDE CHAIN
REMARK 500 25 TYR A 47 0.09 SIDE CHAIN
REMARK 500 25 TYR A 66 0.09 SIDE CHAIN
REMARK 500 26 TYR A 47 0.07 SIDE CHAIN
REMARK 500 26 ARG A 80 0.12 SIDE CHAIN
REMARK 500 28 TYR A 47 0.07 SIDE CHAIN
REMARK 500 29 TYR A 47 0.07 SIDE CHAIN
REMARK 500 30 TYR A 47 0.07 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 81 CU
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 14 SG
REMARK 620 2 CYS A 17 SG 117.9
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 81
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1JWW RELATED DB: PDB
REMARK 900 1JWW CONTAINS THE SAME PROTEIN IN THE APO FORM.
DBREF 1KQK A 2 76 UNP O32220 COPA_BACSU 73 147
SEQADV 1KQK MET A 1 UNP O32220 INITIATING METHIONINE
SEQADV 1KQK ILE A 77 UNP O32220 SEE REMARK 999
SEQADV 1KQK GLU A 78 UNP O32220 SEE REMARK 999
SEQADV 1KQK GLY A 79 UNP O32220 SEE REMARK 999
SEQADV 1KQK ARG A 80 UNP O32220 SEE REMARK 999
SEQRES 1 A 80 MET THR GLU LYS ALA GLU PHE ASP ILE GLU GLY MET THR
SEQRES 2 A 80 CYS ALA ALA CYS ALA ASN ARG ILE GLU LYS ARG LEU ASN
SEQRES 3 A 80 LYS ILE GLU GLY VAL ALA ASN ALA PRO VAL ASN PHE ALA
SEQRES 4 A 80 LEU GLU THR VAL THR VAL GLU TYR ASN PRO LYS GLU ALA
SEQRES 5 A 80 SER VAL SER ASP LEU LYS GLU ALA VAL ASP LYS LEU GLY
SEQRES 6 A 80 TYR LYS LEU LYS LEU LYS GLY GLU GLN ASP SER ILE GLU
SEQRES 7 A 80 GLY ARG
HET CU1 A 81 1
HETNAM CU1 COPPER (I) ION
FORMUL 2 CU1 CU 1+
HELIX 1 1 ALA A 15 LYS A 27 1 13
HELIX 2 2 SER A 53 LYS A 63 1 11
SHEET 1 A 1 GLU A 3 GLU A 10 0
SHEET 1 B 2 GLY A 30 ASN A 33 0
SHEET 2 B 2 VAL A 36 ASN A 37 -1 N ALA A 5 O VAL A 45
SHEET 1 C 1 GLU A 41 ASN A 48 0
SHEET 1 D 1 LYS A 67 GLU A 73 0
LINK SG CYS A 14 CU CU1 A 81 1555 1555 2.17
LINK SG CYS A 17 CU CU1 A 81 1555 1555 2.18
SITE 1 AC1 2 CYS A 14 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 - b 23 2 Bytes