Header list of 1yop.pdb file
Complete list - r 2 2 Bytes
HEADER METAL BINDING PROTEIN 28-JAN-05 1YOP
TITLE THE SOLUTION STRUCTURE OF KTI11P
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KTI11P;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)GOLD;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A+
KEYWDS ZINC FINGER, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.SUN,J.ZHANG,F.WU,C.XU,S.LI,W.ZHAO,Z.WU,J.WU,C.-Z.ZHOU,Y.SHI
REVDAT 4 02-MAR-22 1YOP 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1YOP 1 VERSN
REVDAT 2 05-JUL-05 1YOP 1 JRNL
REVDAT 1 05-APR-05 1YOP 0
JRNL AUTH J.SUN,J.ZHANG,F.WU,C.XU,S.LI,W.ZHAO,Z.WU,J.WU,C.Z.ZHOU,Y.SHI
JRNL TITL SOLUTION STRUCTURE OF KTI11P FROM SACCHAROMYCES CEREVISIAE
JRNL TITL 2 REVEALS A NOVEL ZINC-BINDING MODULE.
JRNL REF BIOCHEMISTRY V. 44 8801 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15952786
JRNL DOI 10.1021/BI0504714
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
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 1YOP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-FEB-05.
REMARK 100 THE DEPOSITION ID IS D_1000031757.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 20MM TRIS BUFFER, 50MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 19
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: 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 ASP A 12 37.62 -96.70
REMARK 500 1 GLU A 18 -46.45 -141.95
REMARK 500 1 PRO A 25 99.35 -50.95
REMARK 500 1 ASP A 30 -168.24 -114.09
REMARK 500 1 GLU A 41 41.04 -90.96
REMARK 500 1 SER A 50 -59.53 -129.81
REMARK 500 1 GLU A 62 -62.52 -99.69
REMARK 500 1 GLU A 77 149.70 68.62
REMARK 500 2 THR A 4 172.67 60.40
REMARK 500 2 ASP A 12 37.29 -96.46
REMARK 500 2 GLN A 20 73.75 52.27
REMARK 500 2 SER A 50 -56.25 -128.45
REMARK 500 2 GLU A 62 -70.27 -99.15
REMARK 500 2 GLU A 77 -60.12 -167.11
REMARK 500 2 ALA A 80 75.27 57.76
REMARK 500 2 ALA A 81 -174.37 62.95
REMARK 500 2 ALA A 82 136.13 -170.26
REMARK 500 3 ASP A 12 36.89 -97.01
REMARK 500 3 ASN A 19 25.32 -143.17
REMARK 500 3 GLN A 20 72.25 53.35
REMARK 500 3 SER A 50 -57.67 -128.01
REMARK 500 3 GLU A 77 82.54 57.64
REMARK 500 3 ALA A 80 90.79 60.32
REMARK 500 3 ALA A 82 80.86 56.89
REMARK 500 4 ASP A 12 36.14 -95.09
REMARK 500 4 GLU A 18 82.99 -66.17
REMARK 500 4 GLN A 20 78.07 53.49
REMARK 500 4 ASP A 30 -165.20 -122.42
REMARK 500 4 SER A 52 36.40 72.96
REMARK 500 4 PRO A 78 85.37 -57.62
REMARK 500 5 SER A 3 80.25 -167.79
REMARK 500 5 THR A 4 -171.51 56.61
REMARK 500 5 ASP A 12 39.00 -98.52
REMARK 500 5 SER A 50 -57.19 -129.15
REMARK 500 5 HIS A 74 85.90 59.98
REMARK 500 5 ILE A 79 30.47 -151.04
REMARK 500 5 ALA A 81 159.00 67.22
REMARK 500 6 VAL A 2 43.58 -106.86
REMARK 500 6 SER A 3 82.71 56.05
REMARK 500 6 THR A 4 173.11 63.13
REMARK 500 6 GLU A 18 82.53 -69.03
REMARK 500 6 GLN A 20 77.54 54.14
REMARK 500 6 LYS A 44 -47.99 -149.37
REMARK 500 6 SER A 50 -55.72 -128.71
REMARK 500 6 PRO A 78 95.69 -68.31
REMARK 500 6 ALA A 80 90.80 60.12
REMARK 500 7 THR A 4 177.48 63.23
REMARK 500 7 TYR A 5 -76.40 -105.58
REMARK 500 7 ASP A 12 37.37 -96.91
REMARK 500 7 ASN A 19 33.64 -146.55
REMARK 500
REMARK 500 THIS ENTRY HAS 162 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 84 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 26 SG
REMARK 620 2 CYS A 28 SG 108.2
REMARK 620 3 CYS A 48 SG 110.3 110.0
REMARK 620 4 CYS A 51 SG 110.0 109.4 108.9
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 84
DBREF 1YOP A 1 83 UNP Q3E840 DPH3_YEAST 1 82
SEQADV 1YOP VAL A 2 UNP Q3E840 INSERTION
SEQRES 1 A 83 MET VAL SER THR TYR ASP GLU ILE GLU ILE GLU ASP MET
SEQRES 2 A 83 THR PHE GLU PRO GLU ASN GLN MET PHE THR TYR PRO CYS
SEQRES 3 A 83 PRO CYS GLY ASP ARG PHE GLN ILE TYR LEU ASP ASP MET
SEQRES 4 A 83 PHE GLU GLY GLU LYS VAL ALA VAL CYS PRO SER CYS SER
SEQRES 5 A 83 LEU MET ILE ASP VAL VAL PHE ASP LYS GLU ASP LEU ALA
SEQRES 6 A 83 GLU TYR TYR GLU GLU ALA GLY ILE HIS PRO PRO GLU PRO
SEQRES 7 A 83 ILE ALA ALA ALA ALA
HET ZN A 84 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 GLU A 9 MET A 13 5 5
HELIX 2 2 LEU A 36 GLU A 41 1 6
HELIX 3 3 GLU A 62 ALA A 71 1 10
SHEET 1 A 3 THR A 14 GLU A 16 0
SHEET 2 A 3 MET A 21 CYS A 26 -1 O MET A 21 N GLU A 16
SHEET 3 A 3 ASP A 30 TYR A 35 -1 O ILE A 34 N PHE A 22
SHEET 1 B 2 VAL A 45 VAL A 47 0
SHEET 2 B 2 MET A 54 ASP A 56 -1 O ILE A 55 N ALA A 46
LINK SG CYS A 26 ZN ZN A 84 1555 1555 2.41
LINK SG CYS A 28 ZN ZN A 84 1555 1555 2.41
LINK SG CYS A 48 ZN ZN A 84 1555 1555 2.40
LINK SG CYS A 51 ZN ZN A 84 1555 1555 2.41
SITE 1 AC1 4 CYS A 26 CYS A 28 CYS A 48 CYS A 51
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