Header list of 2ayj.pdb file
Complete list - r 9 2 Bytes
HEADER TRANSLATION 07-SEP-05 2AYJ
TITLE SOLUTION STRUCTURE OF 50S RIBOSOMAL PROTEIN L40E FROM SULFOLOBUS
TITLE 2 SOLFATARICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 50S RIBOSOMAL PROTEIN L40E;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;
SOURCE 3 ORGANISM_TAXID: 2287;
SOURCE 4 GENE: RPL40E;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ZN-BINDING; BETA-STRAND PROTEIN, STRUCTURAL GENOMICS, PSI, PROTEIN
KEYWDS 2 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM,
KEYWDS 3 NESG, TRANSLATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.WU,A.YEE,J.LUKIN,A.LEMAK,A.SEMESI,T.RAMELOT,M.KENNEDY,A.EDWARD,
AUTHOR 2 C.H.ARROWSMITH,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 3 09-MAR-22 2AYJ 1 REMARK LINK
REVDAT 2 23-DEC-08 2AYJ 1 JRNL VERSN
REVDAT 1 22-AUG-06 2AYJ 0
JRNL AUTH B.WU,J.LUKIN,A.YEE,A.LEMAK,A.SEMESI,T.A.RAMELOT,M.A.KENNEDY,
JRNL AUTH 2 C.H.ARROWSMITH
JRNL TITL SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN L40E, A UNIQUE C4
JRNL TITL 2 ZINC FINGER PROTEIN ENCODED BY ARCHAEON SULFOLOBUS
JRNL TITL 3 SOLFATARICUS
JRNL REF PROTEIN SCI. V. 17 589 2008
JRNL REFN ISSN 0961-8368
JRNL PMID 18218710
JRNL DOI 10.1110/PS.073273008
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.3, CNS 1.0
REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), BRUNGER, A.T. ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1081 NOE-DERIVED DISTANCE RESTRAINTS
REMARK 3 AND 34 TORSION ANGLE RESTRAINTS
REMARK 4
REMARK 4 2AYJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034456.
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 : 450 MM NACL, 25 MM PHOSPHATE
REMARK 210 BUFFER
REMARK 210 PRESSURE : AMBINET
REMARK 210 SAMPLE CONTENTS : 1MM SSO5336, U-15N,13C: 450 MM
REMARK 210 NACL, 25 MM NA2PO4, 1MM
REMARK 210 BENZAMIDINE, 1XINHIBITOR
REMARK 210 COOKTAIL, 0.01% NAN3, 95% H2O, 5%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.1
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 : 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 ALA A 7 97.79 -176.68
REMARK 500 1 GLN A 14 78.03 57.55
REMARK 500 1 ASN A 43 73.31 -106.14
REMARK 500 1 GLU A 50 -179.12 67.63
REMARK 500 1 THR A 53 -51.84 -141.89
REMARK 500 2 GLN A 10 -166.57 64.60
REMARK 500 2 GLN A 13 -70.48 -68.65
REMARK 500 2 GLN A 14 79.40 -161.82
REMARK 500 2 ASN A 43 71.78 -106.26
REMARK 500 2 LYS A 47 98.61 -58.21
REMARK 500 2 GLU A 50 92.29 65.43
REMARK 500 2 PRO A 52 97.14 -58.45
REMARK 500 2 LYS A 55 108.12 -167.46
REMARK 500 3 GLN A 10 -136.75 54.33
REMARK 500 3 GLN A 13 102.81 75.29
REMARK 500 3 GLN A 14 -22.44 76.72
REMARK 500 3 THR A 42 30.59 -86.11
REMARK 500 3 LYS A 48 165.23 67.96
REMARK 500 3 LYS A 49 -56.85 71.17
REMARK 500 3 THR A 53 123.06 76.03
REMARK 500 4 LYS A 8 -160.65 -108.28
REMARK 500 4 GLN A 13 -67.79 -123.11
REMARK 500 4 ARG A 15 90.42 60.35
REMARK 500 4 PHE A 17 -159.71 -93.60
REMARK 500 4 HIS A 40 68.82 61.64
REMARK 500 4 LEU A 51 158.44 65.56
REMARK 500 4 LYS A 54 115.31 69.63
REMARK 500 5 LEU A 3 48.43 -76.46
REMARK 500 5 LEU A 9 -152.33 53.82
REMARK 500 5 GLN A 13 75.98 -102.55
REMARK 500 5 HIS A 40 76.52 61.72
REMARK 500 6 GLN A 13 135.95 69.05
REMARK 500 6 GLN A 14 -40.83 76.06
REMARK 500 7 GLN A 14 14.13 -157.10
REMARK 500 7 LEU A 51 163.76 64.10
REMARK 500 7 THR A 53 -71.25 -99.89
REMARK 500 8 LYS A 8 -164.33 -125.39
REMARK 500 8 GLN A 10 -110.95 47.27
REMARK 500 8 ILE A 11 10.89 -141.63
REMARK 500 8 GLN A 13 133.78 74.22
REMARK 500 8 GLN A 14 -46.61 73.57
REMARK 500 9 THR A 4 88.90 77.06
REMARK 500 9 PRO A 6 -70.18 -64.38
REMARK 500 9 GLN A 13 -68.95 70.82
REMARK 500 9 ASN A 43 77.07 -110.14
REMARK 500 9 GLU A 50 74.88 49.82
REMARK 500 9 PRO A 52 -164.73 -79.70
REMARK 500 9 THR A 53 89.76 65.01
REMARK 500 10 LEU A 3 134.20 70.82
REMARK 500 10 LEU A 9 -69.43 -138.32
REMARK 500
REMARK 500 THIS ENTRY HAS 121 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 57 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 22 SG
REMARK 620 2 CYS A 25 SG 110.9
REMARK 620 3 CYS A 36 SG 105.5 112.6
REMARK 620 4 CYS A 39 SG 112.4 109.0 106.4
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 57
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6747 RELATED DB: BMRB
REMARK 900 RELATED ID: SST91 RELATED DB: TARGETDB
DBREF 2AYJ A 1 56 UNP Q980V5 RL40_SULSO 1 56
SEQRES 1 A 56 MET PRO LEU THR ASP PRO ALA LYS LEU GLN ILE VAL GLN
SEQRES 2 A 56 GLN ARG VAL PHE LEU LYS LYS VAL CYS ARG LYS CYS GLY
SEQRES 3 A 56 ALA LEU ASN PRO ILE ARG ALA THR LYS CYS ARG ARG CYS
SEQRES 4 A 56 HIS SER THR ASN LEU ARG LEU LYS LYS LYS GLU LEU PRO
SEQRES 5 A 56 THR LYS LYS GLY
HET ZN A 57 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
SHEET 1 A 3 LEU A 28 ASN A 29 0
SHEET 2 A 3 LYS A 20 CYS A 22 -1 N LYS A 20 O ASN A 29
SHEET 3 A 3 LEU A 44 LEU A 46 -1 O ARG A 45 N VAL A 21
LINK SG CYS A 22 ZN ZN A 57 1555 1555 2.32
LINK SG CYS A 25 ZN ZN A 57 1555 1555 2.32
LINK SG CYS A 36 ZN ZN A 57 1555 1555 2.30
LINK SG CYS A 39 ZN ZN A 57 1555 1555 2.32
SITE 1 AC1 4 CYS A 22 CYS A 25 CYS A 36 CYS A 39
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 9 2 Bytes