Header list of 1l6t.pdb file
Complete list - 27 20 Bytes
HEADER HYDROLASE 13-MAR-02 1L6T
TITLE STRUCTURE OF ALA24/ASP61 TO ASP24/ASN61 SUBSTITUTED SUBUNIT C OF
TITLE 2 ESCHERICHIA COLI ATP SYNTHASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATP SYNTHASE C CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SUBUNIT C, LIPID-BINDING PROTEIN;
COMPND 5 EC: 3.6.3.34;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: UNCE;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JH618;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBR322 DERIVATIVE
KEYWDS TRANSMEMBRANE HELIX, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR O.Y.DMITRIEV,F.ABILDGAARD,J.L.MARKLEY,R.H.FILLINGAME
REVDAT 4 27-OCT-21 1L6T 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1L6T 1 VERSN
REVDAT 2 01-APR-03 1L6T 1 JRNL
REVDAT 1 24-JUL-02 1L6T 0
JRNL AUTH O.Y.DMITRIEV,F.ABILDGAARD,J.L.MARKLEY,R.H.FILLINGAME
JRNL TITL STRUCTURE OF ALA24/ASP61 --> ASP24/ASN61 SUBSTITUTED SUBUNIT
JRNL TITL 2 C OF ESCHERICHIA COLI ATP SYNTHASE: IMPLICATIONS FOR THE
JRNL TITL 3 MECHANISM OF PROTON TRANSPORT AND ROTARY MOVEMENT IN THE F0
JRNL TITL 4 COMPLEX.
JRNL REF BIOCHEMISTRY V. 41 5537 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11969414
JRNL DOI 10.1021/BI012198L
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : P.GUENTERT, C.MUMENTHALER, K.WUETHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1L6T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-02.
REMARK 100 THE DEPOSITION ID IS D_1000015697.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300.00
REMARK 210 PH : 5.00
REMARK 210 IONIC STRENGTH : 50 MM NACL
REMARK 210 PRESSURE : ATMOSPHERIC ATM
REMARK 210 SAMPLE CONTENTS : 2.0 MM SUBUNIT C, 50 MM NACL, PH
REMARK 210 5.0
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HSQC; HNCA; CBCA(CO)NH; HCACO;
REMARK 210 HN(CO)CACB; HCCH-TOCSY; HC(CO)NH;
REMARK 210 3D_13C-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 4D_13C/15N-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, XWINNMR 2.0, FELIX
REMARK 210 95.0, CHIFIT 2.0
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 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 O PHE A 35 H ALA A 39 1.51
REMARK 500 O PRO A 47 HG1 THR A 51 1.52
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 ALA A 13 -71.73 -69.95
REMARK 500 1 LEU A 19 -70.59 -60.29
REMARK 500 1 ALA A 67 -71.04 -67.56
REMARK 500 2 TYR A 10 -33.32 -37.93
REMARK 500 2 ALA A 13 -71.49 -67.03
REMARK 500 2 ALA A 67 -71.07 -61.86
REMARK 500 3 ALA A 13 -72.30 -76.23
REMARK 500 3 LEU A 48 -61.39 -95.57
REMARK 500 4 ASN A 3 32.06 -155.51
REMARK 500 4 LEU A 4 -62.63 -139.49
REMARK 500 4 ALA A 13 -78.06 -60.67
REMARK 500 4 ALA A 67 -72.55 -68.04
REMARK 500 5 ASN A 5 -64.48 -106.01
REMARK 500 5 ALA A 13 -73.81 -58.70
REMARK 500 5 LEU A 48 -65.72 -107.53
REMARK 500 5 ARG A 50 -70.19 -59.16
REMARK 500 5 ALA A 67 -70.71 -65.40
REMARK 500 6 ASN A 3 42.05 -179.00
REMARK 500 6 LEU A 4 -45.50 -164.77
REMARK 500 6 ARG A 50 -71.31 -57.91
REMARK 500 6 ALA A 67 -71.12 -70.24
REMARK 500 6 ALA A 77 -70.42 -47.44
REMARK 500 7 ASN A 3 25.02 -157.10
REMARK 500 7 ALA A 13 -71.66 -71.93
REMARK 500 7 LEU A 19 -70.75 -58.48
REMARK 500 7 LEU A 36 -33.67 -39.50
REMARK 500 7 LEU A 49 -71.43 -52.92
REMARK 500 7 ALA A 67 -71.50 -59.05
REMARK 500 8 ALA A 13 -79.28 -76.47
REMARK 500 8 LEU A 48 -63.36 -100.10
REMARK 500 9 ASN A 3 30.28 -163.12
REMARK 500 9 LEU A 4 -57.27 -143.57
REMARK 500 9 LEU A 8 -71.32 -52.53
REMARK 500 9 ALA A 13 -72.54 -59.41
REMARK 500 9 LEU A 48 -64.73 -97.42
REMARK 500 10 ALA A 13 -74.37 -57.75
REMARK 500 10 LEU A 45 15.99 -142.03
REMARK 500 10 LEU A 48 -65.39 -93.20
REMARK 500 10 ARG A 50 -71.24 -60.61
REMARK 500 10 ALA A 67 -70.60 -69.65
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1C0V RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE WILD TYPE SUBUNIT C OF E.COLI ATP
REMARK 900 SYNTHASE AT PH 5.0
REMARK 900 RELATED ID: 1C99 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE WILD TYPE SUBUNIT C OF E.COLI ATP
REMARK 900 SYNTHASE AT PH 8.0
DBREF 1L6T A 1 79 UNP P68699 ATPL_ECOLI 1 79
SEQADV 1L6T ASP A 24 UNP P68699 ALA 24 ENGINEERED MUTATION
SEQADV 1L6T ASN A 61 UNP P68699 ASP 61 ENGINEERED MUTATION
SEQRES 1 A 79 MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA
SEQRES 2 A 79 ALA VAL MET MET GLY LEU ALA ALA ILE GLY ASP ALA ILE
SEQRES 3 A 79 GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA
SEQRES 4 A 79 ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN
SEQRES 5 A 79 PHE PHE ILE VAL MET GLY LEU VAL ASN ALA ILE PRO MET
SEQRES 6 A 79 ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL
SEQRES 7 A 79 ALA
HELIX 1 1 LEU A 4 ALA A 40 1 37
HELIX 2 2 LEU A 45 VAL A 78 1 34
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 - 27 20 Bytes