Header list of 2fz0.pdb file
Complete list - v 10 2 Bytes
HEADER MEMBRANE PROTEIN 08-FEB-06 2FZ0
TITLE IDENTIFICATION OF YEAST R-SNARE NYV1P AS A NOVEL LONGIN DOMAIN PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: V-SNARE COMPONENT OF THE VACUOLAR SNARE COMPLEX INVOLVED IN
COMPND 3 VESICLE FUSION; INHIBITS ATP-DEPENDENT CA(2+) TRANSPORT ACTIVITY OF
COMPND 4 PMC1P IN THE VACUOLAR MEMBRANE; NYV1P;
COMPND 5 CHAIN: A;
COMPND 6 FRAGMENT: LONGIN DOMAIN, RESIDUES 1-149;
COMPND 7 SYNONYM: R-SNARE NYV1P;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 4932;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PETH
KEYWDS SNARE PROTEIN, LONGIN DOMAIN, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.WEN,M.ZHANG
REVDAT 5 10-NOV-21 2FZ0 1 REMARK SEQADV
REVDAT 4 24-FEB-09 2FZ0 1 VERSN
REVDAT 3 10-OCT-06 2FZ0 1 JRNL
REVDAT 2 01-AUG-06 2FZ0 1 JRNL
REVDAT 1 07-MAR-06 2FZ0 0
JRNL AUTH W.WEN,L.CHEN,H.WU,X.SUN,M.ZHANG,D.K.BANFIELD
JRNL TITL IDENTIFICATION OF THE YEAST R-SNARE NYV1P AS A NOVEL LONGIN
JRNL TITL 2 DOMAIN-CONTAINING PROTEIN
JRNL REF MOL.CELL.BIOL. V. 17 4282 2006
JRNL REFN ISSN 0270-7306
JRNL PMID 16855025
JRNL DOI 10.1091/MBC.E06-02-0128
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 2FZ0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 10-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036480.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PROTEIN U-15N; 20MM
REMARK 210 PHOSPHATE BUFFER PH 7.0; 6MM D10-
REMARK 210 DITHIOTHRIETOL (DTT); 90% H2O,
REMARK 210 10% D2O; 1MM PROTEIN U-15N,13C;
REMARK 210 20MM PHOSPHATE BUFFER PH 7.0;
REMARK 210 6MM D10- DITHIOTHRIETOL (DTT);
REMARK 210 90% H2O, 10% D2O; 1MM PROTEIN U-
REMARK 210 15N,13C; 20MM PHOSPHATE BUFFER
REMARK 210 PH 7.0; 6MM D10- DITHIOTHRIETOL
REMARK 210 (DTT); 100% D2O; 1MM PROTEIN;
REMARK 210 20MM PHOSPHATE BUFFER PH 7.0;
REMARK 210 6MM D10- DITHIOTHRIETOL (DTT);
REMARK 210 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNCO,
REMARK 210 HNCACB, CBCA(CO)NH; 3D_13C-
REMARK 210 SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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: 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 ASN A 5 112.93 -177.49
REMARK 500 1 SER A 20 134.63 -170.59
REMARK 500 1 PRO A 24 -179.91 -58.17
REMARK 500 1 PHE A 25 -34.20 -172.29
REMARK 500 1 LYS A 27 78.66 32.11
REMARK 500 1 ASN A 28 -70.17 -73.99
REMARK 500 1 GLU A 29 32.41 -153.04
REMARK 500 1 ASN A 30 -70.15 -116.32
REMARK 500 1 THR A 33 -76.24 -165.34
REMARK 500 1 THR A 35 -31.73 171.37
REMARK 500 1 SER A 36 -51.68 -154.17
REMARK 500 1 ASN A 38 30.85 -156.58
REMARK 500 1 PRO A 56 4.62 -68.53
REMARK 500 1 LYS A 57 25.26 -150.32
REMARK 500 1 ILE A 61 131.57 52.32
REMARK 500 1 ASN A 64 -61.58 -130.07
REMARK 500 1 LYS A 65 121.14 72.51
REMARK 500 1 VAL A 66 71.27 58.92
REMARK 500 1 HIS A 86 23.14 -159.28
REMARK 500 1 ASP A 87 87.28 -152.69
REMARK 500 1 THR A 96 -169.52 -75.08
REMARK 500 1 PRO A 101 -168.65 -59.75
REMARK 500 1 LYS A 102 66.72 -106.65
REMARK 500 1 ILE A 103 -36.52 -151.14
REMARK 500 1 ASN A 118 35.92 174.02
REMARK 500 1 ASN A 121 24.48 -75.78
REMARK 500 1 GLU A 122 25.90 -165.09
REMARK 500 1 LEU A 123 -56.73 -123.75
REMARK 500 1 ARG A 143 48.19 -90.90
REMARK 500 1 ASN A 144 36.91 -176.49
REMARK 500 1 THR A 146 38.52 -160.28
REMARK 500 2 ASN A 5 107.99 -174.38
REMARK 500 2 CYS A 21 69.34 -116.93
REMARK 500 2 PHE A 25 9.06 -175.08
REMARK 500 2 GLN A 26 97.47 35.16
REMARK 500 2 ASN A 28 -83.72 57.12
REMARK 500 2 GLU A 29 -165.17 -122.12
REMARK 500 2 ASN A 30 -81.48 62.76
REMARK 500 2 THR A 33 -44.30 -152.80
REMARK 500 2 ILE A 34 153.80 -47.58
REMARK 500 2 THR A 35 -33.97 172.54
REMARK 500 2 SER A 36 -40.64 178.82
REMARK 500 2 LYS A 57 27.75 -149.86
REMARK 500 2 ILE A 61 163.10 51.60
REMARK 500 2 ASN A 64 76.36 44.22
REMARK 500 2 VAL A 66 105.99 58.64
REMARK 500 2 ASN A 72 63.49 62.79
REMARK 500 2 PHE A 77 -167.36 -120.92
REMARK 500 2 HIS A 86 23.68 -156.87
REMARK 500 2 THR A 90 68.62 -153.19
REMARK 500
REMARK 500 THIS ENTRY HAS 639 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2FZ0 A 1 149 UNP Q12255 NYV1_YEAST 1 149
SEQADV 2FZ0 ILE A 100 UNP Q12255 MET 100 ENGINEERED MUTATION
SEQRES 1 A 149 MET LYS ARG PHE ASN VAL SER TYR VAL GLU VAL ILE LYS
SEQRES 2 A 149 ASN GLY GLU THR ILE SER SER CYS PHE GLN PRO PHE GLN
SEQRES 3 A 149 LYS ASN GLU ASN TYR GLY THR ILE THR SER ALA ASN GLU
SEQRES 4 A 149 GLN ILE THR PRO VAL ILE PHE HIS ASN LEU ILE MET ASP
SEQRES 5 A 149 MET VAL LEU PRO LYS VAL VAL PRO ILE LYS GLY ASN LYS
SEQRES 6 A 149 VAL THR LYS MET SER MET ASN LEU ILE ASP GLY PHE ASP
SEQRES 7 A 149 CYS PHE TYR SER THR ASP ASP HIS ASP PRO LYS THR VAL
SEQRES 8 A 149 TYR VAL CYS PHE THR LEU VAL ASP ILE PRO LYS ILE LEU
SEQRES 9 A 149 PRO ILE ARG ILE LEU SER GLY LEU GLN GLU TYR GLU SER
SEQRES 10 A 149 ASN ALA THR ASN GLU LEU LEU SER SER HIS VAL GLY GLN
SEQRES 11 A 149 ILE LEU ASP SER PHE HIS GLU GLU LEU VAL GLU TYR ARG
SEQRES 12 A 149 ASN GLN THR LEU ASN SER
HELIX 1 1 THR A 42 MET A 53 1 12
HELIX 2 2 VAL A 54 VAL A 58 5 5
HELIX 3 3 ILE A 103 GLN A 113 1 11
HELIX 4 4 LEU A 123 TYR A 142 1 20
SHEET 1 A 5 SER A 20 PHE A 22 0
SHEET 2 A 5 TYR A 8 LYS A 13 -1 N VAL A 9 O CYS A 21
SHEET 3 A 5 THR A 90 LEU A 97 -1 O VAL A 91 N ILE A 12
SHEET 4 A 5 PHE A 77 TYR A 81 -1 N ASP A 78 O THR A 96
SHEET 5 A 5 THR A 67 LYS A 68 -1 N THR A 67 O TYR A 81
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 - v 10 2 Bytes