HEADER HYDROLASE 13-NOV-06 2NVJ
TITLE NMR STRUCTURES OF TRANSMEMBRANE SEGMENT FROM SUBUNIT A FROM THE YEAST
TITLE 2 PROTON V-ATPASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 25MER PEPTIDE FROM VACUOLAR ATP SYNTHASE SUBUNIT A,
COMPND 3 VACUOLAR ISOFORM;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: SMTM7, V-ATPASE, V-ATPASE A SUBUNIT, VACUOLAR PROTON PUMP A
COMPND 6 SUBUNIT, V-ATPASE 95 KDA SUBUNIT, VACUOLAR PH PROTEIN 1;
COMPND 7 EC: 3.6.3.14;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS SEQUENCE
SOURCE 4 OCCURS NATURALLY IN THE YEAST.
KEYWDS ALFA HELIX, 3, 10 HELIX, PI HELIX, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.A.HEMMINGA,C.P.VAN MIERLO,R.WECHSELBERGER,E.R.DE JONG,A.M.DUARTE
REVDAT 4 27-DEC-23 2NVJ 1 REMARK
REVDAT 3 16-MAR-22 2NVJ 1 REMARK
REVDAT 2 24-FEB-09 2NVJ 1 VERSN
REVDAT 1 02-OCT-07 2NVJ 0
JRNL AUTH A.M.DUARTE,E.R.DE JONG,R.WECHSELBERGER,C.P.VAN MIERLO,
JRNL AUTH 2 M.A.HEMMINGA
JRNL TITL SEGMENT TM7 FROM THE CYTOPLASMIC HEMI-CHANNEL FROM
JRNL TITL 2 V(O)-H(+)-V-ATPASE INCLUDES A FLEXIBLE REGION THAT HAS A
JRNL TITL 3 POTENTIAL ROLE IN PROTON TRANSLOCATION
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1768 2263 2007
JRNL REFN ISSN 0006-3002
JRNL PMID 17573038
JRNL DOI 10.1016/J.BBAMEM.2007.05.014
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,
REMARK 3 SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2NVJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000040353.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM SMTM7 PEPTIDE (NATURAL
REMARK 210 ABUNDANCE LABELING); 100% D6-DMSO
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR, ARIA 1.2, SPARKY
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 18 TYR A 13 CE1 TYR A 13 CZ 0.088
REMARK 500 18 TYR A 13 CZ TYR A 13 CE2 -0.089
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 4 -5.92 63.21
REMARK 500 1 ASN A 5 -54.75 -145.41
REMARK 500 1 ALA A 11 -58.74 65.80
REMARK 500 1 LEU A 19 31.08 -149.59
REMARK 500 1 ALA A 22 -35.08 -146.04
REMARK 500 2 ASN A 5 -51.58 -151.69
REMARK 500 2 THR A 10 -64.15 -148.03
REMARK 500 2 ALA A 11 -45.85 70.79
REMARK 500 2 TRP A 17 94.46 -67.58
REMARK 500 2 ALA A 18 -58.59 -175.97
REMARK 500 3 ASN A 5 -49.52 170.38
REMARK 500 3 ALA A 11 -66.08 62.94
REMARK 500 3 ALA A 22 -38.23 -148.43
REMARK 500 4 ASN A 5 -51.00 -176.40
REMARK 500 4 ALA A 11 -46.86 67.97
REMARK 500 4 LEU A 16 -70.19 -89.57
REMARK 500 4 TRP A 17 85.98 53.33
REMARK 500 4 LEU A 21 -58.15 -152.03
REMARK 500 4 ALA A 22 -42.05 -141.43
REMARK 500 5 CYS A 3 -85.78 -114.32
REMARK 500 5 LEU A 4 25.00 177.01
REMARK 500 5 ASN A 5 -46.61 171.42
REMARK 500 5 ALA A 11 -47.61 66.87
REMARK 500 5 LEU A 21 176.12 68.01
REMARK 500 5 ALA A 22 -40.67 -138.11
REMARK 500 6 ASN A 5 -47.36 170.91
REMARK 500 6 ALA A 11 2.39 59.88
REMARK 500 6 LEU A 16 -63.58 74.27
REMARK 500 7 ASN A 5 -55.94 176.39
REMARK 500 7 VAL A 7 -60.48 -104.76
REMARK 500 7 ALA A 11 -65.91 69.80
REMARK 500 7 LEU A 16 90.37 -67.30
REMARK 500 7 ALA A 18 -78.34 70.10
REMARK 500 7 LEU A 19 47.98 -89.49
REMARK 500 8 ASN A 5 -46.10 -178.78
REMARK 500 8 THR A 10 -60.79 -95.22
REMARK 500 8 ALA A 11 -63.80 65.79
REMARK 500 9 ASN A 5 -44.96 169.10
REMARK 500 9 THR A 10 -42.81 -145.84
REMARK 500 9 ALA A 11 -9.99 69.43
REMARK 500 9 TRP A 17 -42.76 72.29
REMARK 500 9 LEU A 21 157.36 72.46
REMARK 500 10 ASN A 5 -67.40 178.60
REMARK 500 10 SER A 8 -63.68 -92.71
REMARK 500 10 THR A 10 -47.52 -166.05
REMARK 500 10 SER A 12 -54.83 -140.66
REMARK 500 10 TRP A 17 -28.86 -145.26
REMARK 500 10 LEU A 21 -81.81 -94.52
REMARK 500 11 ASN A 5 -51.50 175.58
REMARK 500 12 ASN A 5 -52.15 165.11
REMARK 500
REMARK 500 THIS ENTRY HAS 93 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2NVJ A 1 25 UNP P32563 VPH1_YEAST 720 744
SEQRES 1 A 25 GLU PHE CYS LEU ASN CYS VAL SER HIS THR ALA SER TYR
SEQRES 2 A 25 LEU ARG LEU TRP ALA LEU SER LEU ALA HIS ALA GLN
HELIX 1 1 ALA A 11 LEU A 16 1 6
HELIX 2 2 TRP A 17 LEU A 19 5 3
SSBOND 1 CYS A 3 CYS A 6 1555 1555 2.03
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
(ATOM LINES ARE NOT SHOWN.)
END