Header list of 1wu0.pdb file
Complete list - r 2 2 Bytes
HEADER HYDROLASE 29-NOV-04 1WU0
TITLE SOLUTION STRUCTURE OF SUBUNIT C OF F1FO-ATP SYNTHASE FROM THE
TITLE 2 THERMOPHILIC BACILLUS PS3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP SYNTHASE C CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: F1FO-ATPASE SUBUNIT C, LIPID-BINDING PROTEIN;
COMPND 5 EC: 3.6.3.14;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SP. PS3;
SOURCE 3 ORGANISM_TAXID: 2334;
SOURCE 4 GENE: ATPE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PTR19-C2
KEYWDS ATPASE, ATP SYNTHASE, MEMBRANE PROTEIN, HYDROGEN ION TRANSPORT,
KEYWDS 2 HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR T.NAKANO,T.IKEGAMI,T.SUZUKI,M.YOSHIDA,H.AKUTSU
REVDAT 3 02-MAR-22 1WU0 1 REMARK
REVDAT 2 24-FEB-09 1WU0 1 VERSN
REVDAT 1 13-DEC-05 1WU0 0
JRNL AUTH T.NAKANO,T.IKEGAMI,T.SUZUKI,M.YOSHIDA,H.AKUTSU
JRNL TITL SOLUTION STRUCTURE TF1FO SUBUNIT C
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.2, CYANA 1.0.6
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), GUENTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1WU0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000023996.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 2.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM SUBUNIT C, ORGANIC SOLVENT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N-1H-HSQC; 2D NOESY;
REMARK 210 CBCA(CO)NH; CBCANH; HNCO; HN(CA)
REMARK 210 CO; HBHANH; HBHA(CO)NH; H(CCO)NH;
REMARK 210 C(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ; 400
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.106, CYANA 1.0.6, TALOS
REMARK 210 2003.027.13.05
REMARK 210 METHOD USED : SIMULATED ANNEALING TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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: 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: 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: 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 SER A 2 -169.31 -168.67
REMARK 500 2 SER A 2 -176.12 178.91
REMARK 500 2 GLN A 37 161.49 -45.46
REMARK 500 3 GLN A 37 160.90 -43.64
REMARK 500 4 SER A 2 -169.50 176.93
REMARK 500 4 GLN A 37 162.90 -41.43
REMARK 500 4 LEU A 40 33.00 -92.66
REMARK 500 5 SER A 2 179.06 175.03
REMARK 500 6 SER A 2 -171.65 174.61
REMARK 500 7 SER A 2 -175.17 -66.15
REMARK 500 7 LEU A 40 31.58 -98.63
REMARK 500 8 SER A 2 -163.95 -161.32
REMARK 500 8 GLN A 37 163.95 -43.79
REMARK 500 9 SER A 2 -174.92 170.74
REMARK 500 9 GLN A 37 158.13 -42.35
REMARK 500 9 LEU A 40 34.06 -92.81
REMARK 500 10 SER A 2 -176.38 177.57
REMARK 500 10 GLN A 37 162.20 -42.30
REMARK 500 11 SER A 2 -174.33 169.01
REMARK 500 11 GLN A 37 166.08 -43.47
REMARK 500 12 SER A 2 -177.78 -178.14
REMARK 500 12 LEU A 40 31.70 -98.99
REMARK 500 13 SER A 2 -155.27 -168.99
REMARK 500 13 GLN A 37 159.03 -43.08
REMARK 500 14 SER A 2 -170.64 -178.67
REMARK 500 14 GLN A 37 158.85 -43.13
REMARK 500 14 LEU A 40 32.98 -93.06
REMARK 500 15 SER A 2 -165.57 -55.94
REMARK 500 16 SER A 2 -151.68 -176.40
REMARK 500 17 SER A 2 -175.67 177.54
REMARK 500 17 GLN A 37 164.14 -41.86
REMARK 500 18 SER A 2 -163.27 -160.82
REMARK 500 19 SER A 2 148.49 -175.64
REMARK 500 19 GLN A 37 161.59 -40.24
REMARK 500 20 SER A 2 -174.12 173.62
REMARK 500 20 LEU A 40 31.82 -93.85
REMARK 500 21 SER A 2 -156.79 -170.10
REMARK 500 21 GLN A 37 161.70 -40.59
REMARK 500 21 LEU A 40 33.12 -97.59
REMARK 500 22 SER A 2 -158.93 175.72
REMARK 500 22 GLN A 37 164.40 -41.94
REMARK 500 22 LEU A 40 32.66 -98.30
REMARK 500 23 GLN A 37 163.98 -49.38
REMARK 500 24 SER A 2 -164.38 -163.28
REMARK 500 24 GLN A 37 165.99 -42.75
REMARK 500 24 LEU A 40 32.23 -98.79
REMARK 500 27 SER A 2 -176.54 -174.46
REMARK 500 27 GLN A 37 157.63 -38.09
REMARK 500 28 SER A 2 -169.56 -170.13
REMARK 500 28 GLN A 37 161.14 -44.37
REMARK 500
REMARK 500 THIS ENTRY HAS 52 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1A91 RELATED DB: PDB
REMARK 900 F1FO ATPASE SUBUNIT C
REMARK 900 RELATED ID: 1C0V RELATED DB: PDB
REMARK 900 PROTEIN (F1FO ATPASE SUBUNIT C)
REMARK 900 RELATED ID: 1C99 RELATED DB: PDB
REMARK 900 PROTEOLIPID F1FO ATPASE SUBUNIT C
REMARK 900 RELATED ID: 1C17 RELATED DB: PDB
REMARK 900 ATP SYNTHASE SUBUNIT C
REMARK 900 RELATED ID: 1QO1 RELATED DB: PDB
REMARK 900 ATP SYNTHASE ALPHA CHAIN, ATP SYNTHASE BETA CHAIN, ATP SYNTHASE
REMARK 900 GAMMA CHAIN, ATP SYNTHASE DELTA CHAIN, ATP SYNTHASE PROTEIN 9
REMARK 900 RELATED ID: 1ATY RELATED DB: PDB
REMARK 900 F1FO ATP SYNTHASE (E.C.3.6.1.34) SUBUNIT C (RESIDUES 9 - 26, 52 -
REMARK 900 79) MUTANT WITH ALA 67 REPLACED BY CYS (A67C) (NMR, 9 STRUCTURES)
DBREF 1WU0 A 1 72 UNP P00845 ATPL_BACP3 1 72
SEQRES 1 A 72 MET SER LEU GLY VAL LEU ALA ALA ALA ILE ALA VAL GLY
SEQRES 2 A 72 LEU GLY ALA LEU GLY ALA GLY ILE GLY ASN GLY LEU ILE
SEQRES 3 A 72 VAL SER ARG THR ILE GLU GLY ILE ALA ARG GLN PRO GLU
SEQRES 4 A 72 LEU ARG PRO VAL LEU GLN THR THR MET PHE ILE GLY VAL
SEQRES 5 A 72 ALA LEU VAL GLU ALA LEU PRO ILE ILE GLY VAL VAL PHE
SEQRES 6 A 72 SER PHE ILE TYR LEU GLY ARG
HELIX 1 1 LEU A 3 ARG A 36 1 34
HELIX 2 2 PRO A 42 GLU A 56 1 15
HELIX 3 3 GLU A 56 GLY A 71 1 16
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