Header list of 1yws.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 18-FEB-05 1YWS
TITLE SOLUTION STRUCTURE OF YBL071W-A FROM SACCHAROMYCES CEREVISIAE.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN YBL071W-A;
COMPND 3 CHAIN: A;
COMPND 4 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 GENE: YBL071W-A, KTI11;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3) GOLD MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11
KEYWDS ZINC FINGER, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, ONTARIO CENTRE FOR
KEYWDS 3 STRUCTURAL PROTEOMICS, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.A.LUKIN,V.GUIDO,C.H.ARROWSMITH,NORTHEAST STRUCTURAL GENOMICS
AUTHOR 2 CONSORTIUM (NESG)
REVDAT 3 02-MAR-22 1YWS 1 REMARK LINK
REVDAT 2 24-FEB-09 1YWS 1 VERSN
REVDAT 1 08-MAR-05 1YWS 0
JRNL AUTH J.A.LUKIN,V.GUIDO,C.H.ARROWSMITH
JRNL TITL SOLUTION STRUCTURE OF YBL071W-A FROM SACCHAROMYCES
JRNL TITL 2 CEREVISIAE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, CNS 1.1
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), BRUNGER, A. ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 100 STRUCTURES WERE CALCULATED BY CYANA 2.0 USING 1294 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS,
REMARK 3 122 DIHEDRAL ANGLE CONSTRAINTS, AND 54 DISTANCE CONSTRAINTS FROM
REMARK 3 HYDROGEN BONDS. THE 20
REMARK 3 STRUCTURES WITH LOWEST TARGET FUNCTIONS WERE SUBJECTED TO
REMARK 3 REFINEMENT WITH CNS 1.1.
REMARK 4
REMARK 4 1YWS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032010.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 450MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM YBL071W-A, U-15N, U-13C;
REMARK 210 450MM NACL, 1MM BENZAMIDINE,
REMARK 210 0.01% NAN3, 10MM MOPS, 0.01MM
REMARK 210 ZNSO4, 90% H2O, 10% D2O; 1MM
REMARK 210 YBL071W-A, U-15N, U-13C; 450MM
REMARK 210 NACL, 1MM BENZAMIDINE, 0.01%
REMARK 210 NAN3, 10MM MOPS, 0.01MM ZNSO4,
REMARK 210 99.9% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 19
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 CYS A 27 -43.99 175.54
REMARK 500 1 SER A 49 -55.80 84.73
REMARK 500 1 SER A 51 64.07 67.42
REMARK 500 2 CYS A 27 -46.71 -177.09
REMARK 500 2 SER A 49 -59.36 89.93
REMARK 500 2 SER A 51 74.53 69.01
REMARK 500 3 SER A 2 -165.33 63.24
REMARK 500 3 PRO A 24 109.83 -56.97
REMARK 500 3 CYS A 27 -52.72 -179.40
REMARK 500 3 SER A 49 -55.75 85.50
REMARK 500 3 ALA A 80 29.78 -149.61
REMARK 500 4 CYS A 27 -40.29 -176.71
REMARK 500 4 SER A 49 -56.72 86.97
REMARK 500 4 SER A 51 72.78 69.05
REMARK 500 5 CYS A 27 -44.38 177.83
REMARK 500 5 SER A 49 -54.40 78.09
REMARK 500 5 SER A 51 42.91 70.49
REMARK 500 6 CYS A 27 -41.27 179.52
REMARK 500 6 SER A 49 -58.39 89.28
REMARK 500 7 CYS A 27 -41.50 175.15
REMARK 500 7 SER A 49 -53.89 83.22
REMARK 500 8 CYS A 27 -54.05 -178.55
REMARK 500 8 SER A 49 -53.53 85.78
REMARK 500 8 PRO A 74 107.13 -34.62
REMARK 500 9 CYS A 27 -47.07 -176.56
REMARK 500 9 SER A 49 -58.43 90.90
REMARK 500 9 SER A 51 73.25 69.65
REMARK 500 9 ALA A 81 106.72 -57.17
REMARK 500 10 PRO A 24 107.96 -56.82
REMARK 500 10 CYS A 27 -46.58 178.36
REMARK 500 10 SER A 49 -57.37 89.58
REMARK 500 10 SER A 51 73.23 70.38
REMARK 500 11 SER A 2 -158.04 -102.29
REMARK 500 11 CYS A 27 -39.72 177.61
REMARK 500 11 SER A 49 -60.42 86.51
REMARK 500 11 ALA A 80 112.13 -165.83
REMARK 500 12 CYS A 27 -40.52 174.93
REMARK 500 12 SER A 49 -51.29 79.78
REMARK 500 12 PRO A 74 108.13 -35.17
REMARK 500 13 CYS A 27 -43.71 -175.63
REMARK 500 13 SER A 49 -55.88 88.85
REMARK 500 13 SER A 51 74.02 68.49
REMARK 500 13 ALA A 80 -162.53 55.53
REMARK 500 14 CYS A 27 -43.65 178.83
REMARK 500 14 SER A 49 -57.46 88.66
REMARK 500 14 SER A 51 70.13 66.92
REMARK 500 15 CYS A 27 -46.17 177.14
REMARK 500 15 SER A 49 -60.38 86.79
REMARK 500 15 SER A 51 79.61 64.48
REMARK 500 15 ALA A 81 -48.79 -132.55
REMARK 500
REMARK 500 THIS ENTRY HAS 65 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 83 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 25 SG
REMARK 620 2 CYS A 27 SG 110.2
REMARK 620 3 CYS A 47 SG 109.3 109.8
REMARK 620 4 CYS A 50 SG 109.8 110.0 107.7
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 83
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: YT655 RELATED DB: TARGETDB
DBREF 1YWS A 1 82 GB 21648335 NP_660100 1 82
SEQRES 1 A 82 MET SER THR TYR ASP GLU ILE GLU ILE GLU ASP MET THR
SEQRES 2 A 82 PHE GLU PRO GLU ASN GLN MET PHE THR TYR PRO CYS PRO
SEQRES 3 A 82 CYS GLY ASP ARG PHE GLN ILE TYR LEU ASP ASP MET PHE
SEQRES 4 A 82 GLU GLY GLU LYS VAL ALA VAL CYS PRO SER CYS SER LEU
SEQRES 5 A 82 MET ILE ASP VAL VAL PHE ASP LYS GLU ASP LEU ALA GLU
SEQRES 6 A 82 TYR TYR GLU GLU ALA GLY ILE HIS PRO PRO GLU PRO ILE
SEQRES 7 A 82 ALA ALA ALA ALA
HET ZN A 83 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 LEU A 35 GLU A 40 1 6
HELIX 2 2 ASP A 59 GLY A 71 1 13
SHEET 1 A 3 GLU A 6 GLU A 8 0
SHEET 2 A 3 LEU A 52 VAL A 57 1 O ASP A 55 N ILE A 7
SHEET 3 A 3 VAL A 44 CYS A 47 -1 N ALA A 45 O ILE A 54
SHEET 1 B 3 THR A 13 GLU A 15 0
SHEET 2 B 3 MET A 20 TYR A 23 -1 O THR A 22 N THR A 13
SHEET 3 B 3 PHE A 31 TYR A 34 -1 O ILE A 33 N PHE A 21
LINK SG CYS A 25 ZN ZN A 83 1555 1555 2.32
LINK SG CYS A 27 ZN ZN A 83 1555 1555 2.32
LINK SG CYS A 47 ZN ZN A 83 1555 1555 2.31
LINK SG CYS A 50 ZN ZN A 83 1555 1555 2.32
SITE 1 AC1 5 CYS A 25 CYS A 27 ASP A 29 CYS A 47
SITE 2 AC1 5 CYS A 50
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