Header list of 1jww.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE 05-SEP-01 1JWW TITLE NMR CHARACTERIZATION OF THE N-TERMINAL DOMAIN OF A POTENTIAL COPPER- TITLE 2 TRANSLOCATING P-TYPE ATPASE FROM BACILLUS SUBTILIS COMPND MOL_ID: 1; COMPND 2 MOLECULE: POTENTIAL COPPER-TRANSPORTING ATPASE; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN; COMPND 5 EC: 3.6.3.4; COMPND 6 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 BETA-ALPHA-BETA-BETA-ALPHA-BETA, HYDROLASE EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR L.BANCI,I.BERTINI,S.CIOFI-BAFFONI,M.D'ONOFRIO,L.GONNELLI,F.MARHUENDA- AUTHOR 2 EGEA,F.J.RUIZ-DUENAS REVDAT 4 23-FEB-22 1JWW 1 REMARK REVDAT 3 24-FEB-09 1JWW 1 VERSN REVDAT 2 01-APR-03 1JWW 1 JRNL REVDAT 1 10-APR-02 1JWW 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 : XWINNMR, AMBER 5.0 REMARK 3 AUTHORS : PEARLMAN, D.A., CASE, D.A. ET AL. (AMBER) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON: 95 REMARK 3 DIHEDRAL ANGLE RESTRAINTS AND 1278 NOE-DERIVED DISTANCE REMARK 3 CONSTRAINTS REMARK 4 REMARK 4 1JWW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-01. REMARK 100 THE DEPOSITION ID IS D_1000014279. 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 : 100MM PHOSPHATE BUFFER REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 2MM N-TERMINAL DOMAIN OF COPA REMARK 210 15N,13C; 100MM PHOSPATE BUFFER; REMARK 210 90% H2O, 10% D2O; 2MM N-TERMINAL REMARK 210 DOMAIN OF COPA 100MM PHOSPATE REMARK 210 BUFFER; 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; HCCH- REMARK 210 TOCSY; 2D-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 700 MHZ; 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 3.0, DYANA 1.5, CORMA REMARK 210 METHOD USED : SIMULATED ANNEALING 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: 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 6 ARG A 80 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES REMARK 500 13 ARG A 80 NE - CZ - NH2 ANGL. DEV. = -4.1 DEGREES REMARK 500 27 ARG A 80 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES REMARK 500 29 ARG A 80 CD - NE - CZ ANGL. DEV. = 8.6 DEGREES REMARK 500 29 ARG A 80 NE - CZ - NH2 ANGL. DEV. = -3.9 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 86.18 -153.02 REMARK 500 1 ALA A 39 -41.31 -176.26 REMARK 500 1 GLU A 41 44.15 72.91 REMARK 500 1 LYS A 71 -60.94 -108.34 REMARK 500 1 ASP A 75 -176.30 67.27 REMARK 500 1 ILE A 77 -119.39 -128.24 REMARK 500 1 GLU A 78 64.74 33.09 REMARK 500 2 THR A 13 86.18 -153.02 REMARK 500 2 ALA A 39 -41.31 -176.26 REMARK 500 2 GLU A 41 44.15 72.91 REMARK 500 2 LYS A 71 -60.94 -108.34 REMARK 500 2 ASP A 75 -176.30 67.27 REMARK 500 2 ILE A 77 -119.39 -128.24 REMARK 500 2 GLU A 78 64.74 33.09 REMARK 500 3 THR A 13 30.06 -149.16 REMARK 500 3 CYS A 14 -65.39 -90.40 REMARK 500 3 ALA A 15 -67.92 -172.19 REMARK 500 3 PHE A 38 60.86 -115.38 REMARK 500 3 ALA A 39 -32.63 168.83 REMARK 500 3 LYS A 50 -45.55 -139.35 REMARK 500 3 SER A 76 -175.48 73.00 REMARK 500 4 MET A 12 74.73 -66.78 REMARK 500 4 THR A 13 45.68 -105.14 REMARK 500 4 CYS A 14 59.52 -146.33 REMARK 500 4 ALA A 15 -77.62 47.54 REMARK 500 4 PHE A 38 43.30 -71.77 REMARK 500 4 ALA A 39 -36.32 -176.86 REMARK 500 4 LYS A 50 -47.54 -130.48 REMARK 500 4 LYS A 71 -65.91 -127.44 REMARK 500 4 ASP A 75 74.18 71.32 REMARK 500 5 THR A 13 50.48 -160.06 REMARK 500 5 PHE A 38 43.25 -95.00 REMARK 500 5 ALA A 39 -39.76 -172.55 REMARK 500 5 SER A 76 170.52 67.08 REMARK 500 5 ILE A 77 -146.38 -137.73 REMARK 500 5 GLU A 78 172.08 70.56 REMARK 500 6 CYS A 14 -132.81 -129.48 REMARK 500 6 ALA A 15 -49.19 -131.02 REMARK 500 6 ALA A 39 -40.72 -174.65 REMARK 500 6 GLU A 41 37.35 75.40 REMARK 500 6 GLU A 51 -65.15 -142.02 REMARK 500 6 ASP A 75 78.34 42.18 REMARK 500 7 THR A 13 -99.68 -76.25 REMARK 500 7 CYS A 14 49.51 165.03 REMARK 500 7 ALA A 15 -87.61 -148.44 REMARK 500 7 ALA A 32 -61.51 -109.50 REMARK 500 7 ALA A 34 58.01 -151.47 REMARK 500 7 ALA A 39 -40.22 -175.13 REMARK 500 7 GLU A 51 -60.95 -91.49 REMARK 500 7 GLU A 73 146.22 72.51 REMARK 500 REMARK 500 THIS ENTRY HAS 200 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 TYR A 47 0.10 SIDE CHAIN REMARK 500 2 TYR A 47 0.10 SIDE CHAIN REMARK 500 3 TYR A 47 0.09 SIDE CHAIN REMARK 500 3 TYR A 66 0.19 SIDE CHAIN REMARK 500 4 TYR A 47 0.09 SIDE CHAIN REMARK 500 5 TYR A 47 0.08 SIDE CHAIN REMARK 500 6 TYR A 47 0.08 SIDE CHAIN REMARK 500 6 TYR A 66 0.08 SIDE CHAIN REMARK 500 7 TYR A 66 0.07 SIDE CHAIN REMARK 500 8 TYR A 47 0.09 SIDE CHAIN REMARK 500 9 ARG A 20 0.07 SIDE CHAIN REMARK 500 11 TYR A 47 0.13 SIDE CHAIN REMARK 500 12 TYR A 47 0.09 SIDE CHAIN REMARK 500 13 TYR A 47 0.08 SIDE CHAIN REMARK 500 14 TYR A 66 0.12 SIDE CHAIN REMARK 500 16 TYR A 47 0.09 SIDE CHAIN REMARK 500 19 TYR A 47 0.08 SIDE CHAIN REMARK 500 20 TYR A 47 0.10 SIDE CHAIN REMARK 500 21 TYR A 47 0.11 SIDE CHAIN REMARK 500 21 TYR A 66 0.17 SIDE CHAIN REMARK 500 22 TYR A 47 0.10 SIDE CHAIN REMARK 500 23 TYR A 47 0.07 SIDE CHAIN REMARK 500 25 TYR A 47 0.12 SIDE CHAIN REMARK 500 26 TYR A 47 0.08 SIDE CHAIN REMARK 500 27 TYR A 47 0.09 SIDE CHAIN REMARK 500 29 ARG A 24 0.08 SIDE CHAIN REMARK 500 29 TYR A 47 0.15 SIDE CHAIN REMARK 500 30 TYR A 47 0.07 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 1JWW A 1 80 UNP O32220 COPA_BACSU 72 150 SEQADV 1JWW ILE A 77 UNP O32220 GLU 148 SEE REMARK 999 SEQADV 1JWW GLY A 79 UNP O32220 ALA 150 SEE REMARK 999 SEQADV 1JWW ARG A 80 UNP O32220 ALA 151 SEE REMARK 999 SEQADV 1JWW GLU A 78 UNP O32220 ALA 149 SEE REMARK 999 SEQRES 1 A 80 VAL 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 HELIX 1 1 CYS A 14 LYS A 27 1 14 HELIX 2 2 SER A 53 GLY A 65 1 13 SHEET 1 A 4 VAL A 31 ASN A 33 0 SHEET 2 A 4 THR A 42 TYR A 47 -1 O GLU A 46 N ASN A 33 SHEET 3 A 4 GLU A 3 GLU A 10 -1 N GLU A 3 O TYR A 47 SHEET 4 A 4 LYS A 67 LEU A 70 -1 O LYS A 69 N ASP A 8 CRYST1 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