Header list of 1oq6.pdb file
Complete list - t 27 2 Bytes
HEADER HYDROLASE 07-MAR-03 1OQ6 TITLE SOLUTION STRUCTURE OF COPPER-S46V COPA FROM BACILLUS SUBTILIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: POTENTIAL COPPER-TRANSPORTING ATPASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: COPPER FORM OF N-TERMINAL S46V OF COPA; COMPND 5 EC: 3.6.3.4; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: 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: PLSAMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET21A KEYWDS P-TYPE ATPASE, MUTATION, FOLDING, COPPER COMPLEX, STRUCTURAL KEYWDS 2 PROTEOMICS IN EUROPE, SPINE, STRUCTURAL GENOMICS, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,L.GONNELLI,X.C.SU,STRUCTURAL AUTHOR 2 PROTEOMICS IN EUROPE (SPINE) REVDAT 3 27-OCT-21 1OQ6 1 REMARK SEQADV LINK REVDAT 2 24-FEB-09 1OQ6 1 VERSN REVDAT 1 16-SEP-03 1OQ6 0 JRNL AUTH L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,L.GONNELLI,X.C.SU JRNL TITL A CORE MUTATION AFFECTING THE FOLDING PROPERTIES OF A JRNL TITL 2 SOLUBLE DOMAIN OF THE ATPASE PROTEIN COPA FROM BACILLUS JRNL TITL 3 SUBTILIS JRNL REF J.MOL.BIOL. V. 331 473 2003 JRNL REFN ISSN 0022-2836 JRNL PMID 12888353 JRNL DOI 10.1016/S0022-2836(03)00769-1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 2.6, AMBER 5.0 REMARK 3 AUTHORS : BRUKER (XWINNMR), PEARLMAN, CASE, CALDWELL, ROSS, REMARK 3 CHEATHAM, FERGUSON, SEIBEL, SINGH, WEINER, KOLLMAN REMARK 3 (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: 2913 NOE CROSS PEAKS WERE ASSIGNED AND REMARK 3 INTEGRATED, PROVIDING 1818 UNIQUE UPPER DISTANCE LIMITS, OF REMARK 3 WHICH 1357 ARE MEANINGFUL. A TOTAL OF 35 PROTON PAIRS WERE REMARK 3 STEREOSPECIFICALLY ASSIGNED. REMARK 4 REMARK 4 1OQ6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-MAR-03. REMARK 100 THE DEPOSITION ID IS D_1000018554. 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 : 20 MM PHOSPHATE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 1.2 MM CU-D1S46VCOPA, 20MM REMARK 210 PHOSPHATE, 90%H2O, 10%D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; HNHB REMARK 210 SPECTROMETER FIELD STRENGTH : 800 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, DYANA 1.5 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING, MOLECULAR DYNAMICS, REMARK 210 TORSION ANGLE DYNAMICS, REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 300 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH LOWEST ENERGY REMARK 210 VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED WITH 15N LABELED SAMPLE. 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 2 THR A 57 C - N - CA ANGL. DEV. = 16.4 DEGREES REMARK 500 3 THR A 57 C - N - CA ANGL. DEV. = 16.2 DEGREES REMARK 500 4 THR A 57 C - N - CA ANGL. DEV. = 17.1 DEGREES REMARK 500 7 THR A 57 C - N - CA ANGL. DEV. = 17.0 DEGREES REMARK 500 8 THR A 57 C - N - CA ANGL. DEV. = 16.5 DEGREES REMARK 500 9 THR A 57 C - N - CA ANGL. DEV. = 16.9 DEGREES REMARK 500 11 THR A 57 C - N - CA ANGL. DEV. = 16.0 DEGREES REMARK 500 12 THR A 57 C - N - CA ANGL. DEV. = 16.4 DEGREES REMARK 500 13 THR A 57 C - N - CA ANGL. DEV. = 16.3 DEGREES REMARK 500 15 THR A 57 C - N - CA ANGL. DEV. = 16.1 DEGREES REMARK 500 17 THR A 57 C - N - CA ANGL. DEV. = 16.4 DEGREES REMARK 500 18 THR A 57 C - N - CA ANGL. DEV. = 16.1 DEGREES REMARK 500 21 THR A 57 C - N - CA ANGL. DEV. = 16.6 DEGREES REMARK 500 24 THR A 57 C - N - CA ANGL. DEV. = 15.4 DEGREES REMARK 500 28 THR A 57 C - N - CA ANGL. DEV. = 16.8 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 LEU A 2 -74.94 -161.66 REMARK 500 1 SER A 3 93.18 48.71 REMARK 500 1 ALA A 19 -52.57 -152.60 REMARK 500 1 THR A 35 -39.24 -133.16 REMARK 500 1 ASN A 40 57.28 -99.65 REMARK 500 2 GLU A 54 -61.16 -102.52 REMARK 500 2 THR A 57 -23.25 -19.17 REMARK 500 2 ALA A 58 -62.54 -28.21 REMARK 500 3 LEU A 2 -74.90 -106.55 REMARK 500 3 ALA A 18 -68.06 64.46 REMARK 500 3 THR A 57 -17.96 -13.07 REMARK 500 3 ALA A 58 -63.48 -27.61 REMARK 500 3 ILE A 73 64.60 -102.48 REMARK 500 4 SER A 3 99.43 -64.50 REMARK 500 4 MET A 15 122.37 -38.55 REMARK 500 4 ALA A 18 -63.71 64.68 REMARK 500 4 PRO A 52 13.93 -69.26 REMARK 500 4 THR A 57 -17.44 -16.45 REMARK 500 4 ALA A 58 -63.38 -27.32 REMARK 500 5 SER A 3 89.91 75.82 REMARK 500 5 ALA A 19 -50.36 -151.49 REMARK 500 5 ASN A 40 57.61 -96.15 REMARK 500 5 ILE A 73 79.27 -107.46 REMARK 500 6 THR A 16 -72.10 -113.88 REMARK 500 6 ALA A 19 -49.09 -146.87 REMARK 500 6 ASN A 40 57.93 -94.05 REMARK 500 7 THR A 16 -45.71 -147.71 REMARK 500 7 ALA A 19 -51.90 -130.66 REMARK 500 7 THR A 43 -68.48 -98.54 REMARK 500 7 GLU A 44 43.55 159.93 REMARK 500 7 THR A 57 -18.41 -13.75 REMARK 500 7 ALA A 58 -63.36 -28.12 REMARK 500 7 ILE A 73 79.24 -114.23 REMARK 500 8 LEU A 2 -89.15 173.83 REMARK 500 8 ALA A 19 -58.53 -147.62 REMARK 500 8 GLU A 54 -60.47 -99.03 REMARK 500 8 THR A 57 -23.52 -14.31 REMARK 500 8 ALA A 58 -62.74 -27.47 REMARK 500 9 SER A 3 104.71 -59.83 REMARK 500 9 MET A 15 108.20 -53.21 REMARK 500 9 THR A 16 14.18 -155.91 REMARK 500 9 ALA A 18 -56.56 -172.86 REMARK 500 9 ALA A 19 32.10 -164.38 REMARK 500 9 THR A 43 -75.95 -102.10 REMARK 500 9 GLU A 44 26.76 179.37 REMARK 500 9 THR A 57 -18.28 -12.51 REMARK 500 9 ALA A 58 -63.05 -27.29 REMARK 500 10 THR A 16 -66.03 -108.63 REMARK 500 10 ALA A 19 -53.49 -138.42 REMARK 500 10 THR A 35 -38.94 -132.22 REMARK 500 REMARK 500 THIS ENTRY HAS 155 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 THR A 55 GLY A 56 2 -144.36 REMARK 500 GLY A 56 THR A 57 2 -147.43 REMARK 500 GLY A 56 THR A 57 3 -143.23 REMARK 500 THR A 55 GLY A 56 4 -148.59 REMARK 500 GLY A 56 THR A 57 7 -146.43 REMARK 500 THR A 55 GLY A 56 8 -144.91 REMARK 500 THR A 55 GLY A 56 9 -148.65 REMARK 500 GLY A 56 THR A 57 9 -147.08 REMARK 500 GLY A 56 THR A 57 11 -145.85 REMARK 500 GLY A 56 THR A 57 12 -143.24 REMARK 500 THR A 55 GLY A 56 13 -146.59 REMARK 500 GLY A 56 THR A 57 13 -143.79 REMARK 500 GLY A 56 THR A 57 15 -142.02 REMARK 500 GLY A 56 THR A 57 17 -143.59 REMARK 500 GLY A 56 THR A 57 18 -144.11 REMARK 500 THR A 55 GLY A 56 21 -142.46 REMARK 500 GLY A 56 THR A 57 21 -148.02 REMARK 500 GLY A 56 THR A 57 22 -136.37 REMARK 500 MET A 1 LEU A 2 23 -139.02 REMARK 500 THR A 55 GLY A 56 23 -123.94 REMARK 500 GLY A 56 THR A 57 24 -139.09 REMARK 500 THR A 55 GLY A 56 27 -148.83 REMARK 500 GLY A 56 THR A 57 28 -149.25 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 TYR A 50 0.07 SIDE CHAIN REMARK 500 1 TYR A 69 0.08 SIDE CHAIN REMARK 500 2 TYR A 50 0.08 SIDE CHAIN REMARK 500 2 TYR A 69 0.11 SIDE CHAIN REMARK 500 3 TYR A 50 0.08 SIDE CHAIN REMARK 500 3 ARG A 76 0.09 SIDE CHAIN REMARK 500 4 TYR A 50 0.09 SIDE CHAIN REMARK 500 4 TYR A 69 0.12 SIDE CHAIN REMARK 500 6 TYR A 50 0.13 SIDE CHAIN REMARK 500 6 TYR A 69 0.10 SIDE CHAIN REMARK 500 7 TYR A 50 0.09 SIDE CHAIN REMARK 500 8 TYR A 50 0.11 SIDE CHAIN REMARK 500 9 TYR A 50 0.11 SIDE CHAIN REMARK 500 9 ARG A 76 0.10 SIDE CHAIN REMARK 500 11 TYR A 50 0.15 SIDE CHAIN REMARK 500 11 ARG A 76 0.09 SIDE CHAIN REMARK 500 12 TYR A 50 0.11 SIDE CHAIN REMARK 500 13 TYR A 50 0.08 SIDE CHAIN REMARK 500 14 TYR A 50 0.09 SIDE CHAIN REMARK 500 15 TYR A 50 0.11 SIDE CHAIN REMARK 500 16 TYR A 50 0.07 SIDE CHAIN REMARK 500 17 TYR A 50 0.08 SIDE CHAIN REMARK 500 17 TYR A 69 0.07 SIDE CHAIN REMARK 500 18 TYR A 50 0.16 SIDE CHAIN REMARK 500 18 TYR A 69 0.14 SIDE CHAIN REMARK 500 20 TYR A 50 0.08 SIDE CHAIN REMARK 500 21 TYR A 50 0.11 SIDE CHAIN REMARK 500 22 TYR A 50 0.15 SIDE CHAIN REMARK 500 22 TYR A 69 0.10 SIDE CHAIN REMARK 500 23 TYR A 50 0.14 SIDE CHAIN REMARK 500 23 TYR A 69 0.07 SIDE CHAIN REMARK 500 24 TYR A 50 0.10 SIDE CHAIN REMARK 500 24 TYR A 69 0.10 SIDE CHAIN REMARK 500 25 TYR A 50 0.09 SIDE CHAIN REMARK 500 25 TYR A 69 0.07 SIDE CHAIN REMARK 500 26 TYR A 50 0.07 SIDE CHAIN REMARK 500 27 TYR A 50 0.06 SIDE CHAIN REMARK 500 28 TYR A 50 0.17 SIDE CHAIN REMARK 500 28 TYR A 69 0.08 SIDE CHAIN REMARK 500 29 TYR A 50 0.09 SIDE CHAIN REMARK 500 30 TYR A 50 0.09 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 CU A 77 CU REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 17 SG REMARK 620 2 CYS A 20 SG 130.7 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 CU A 77 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1OQ3 RELATED DB: PDB REMARK 900 THE APO FORM REMARK 900 RELATED ID: 1OPZ RELATED DB: PDB REMARK 900 THE APO FORM REMARK 900 RELATED ID: CIRMMP05 RELATED DB: TARGETDB DBREF 1OQ6 A 1 76 UNP O32220 COPA_BACSU 1 76 SEQADV 1OQ6 VAL A 46 UNP O32220 SER 46 ENGINEERED MUTATION SEQADV 1OQ6 ILE A 73 UNP O32220 THR 73 CLONING ARTIFACT SEQADV 1OQ6 GLY A 75 UNP O32220 LYS 75 CLONING ARTIFACT SEQADV 1OQ6 ARG A 76 UNP O32220 ALA 76 CLONING ARTIFACT SEQRES 1 A 76 MET LEU SER GLU GLN LYS GLU ILE ALA MET GLN VAL SER SEQRES 2 A 76 GLY MET THR CYS ALA ALA CYS ALA ALA ARG ILE GLU LYS SEQRES 3 A 76 GLY LEU LYS ARG MET PRO GLY VAL THR ASP ALA ASN VAL SEQRES 4 A 76 ASN LEU ALA THR GLU THR VAL ASN VAL ILE TYR ASP PRO SEQRES 5 A 76 ALA GLU THR GLY THR ALA ALA ILE GLN GLU LYS ILE GLU SEQRES 6 A 76 LYS LEU GLY TYR HIS VAL VAL ILE GLU GLY ARG HET CU A 77 1 HETNAM CU COPPER (II) ION FORMUL 2 CU CU 2+ HELIX 1 1 ALA A 19 LYS A 29 1 11 HELIX 2 2 LEU A 41 THR A 43 5 3 HELIX 3 3 THR A 57 GLY A 68 1 12 SHEET 1 A 4 VAL A 34 ASN A 40 0 SHEET 2 A 4 THR A 45 TYR A 50 -1 O ASN A 47 N ASN A 38 SHEET 3 A 4 LYS A 6 SER A 13 -1 N LYS A 6 O TYR A 50 SHEET 4 A 4 HIS A 70 VAL A 72 -1 O VAL A 72 N GLN A 11 LINK SG CYS A 17 CU CU A 77 1555 1555 2.18 LINK SG CYS A 20 CU CU A 77 1555 1555 2.21 SITE 1 AC1 3 CYS A 17 ALA A 19 CYS A 20 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 27 2 Bytes