Header list of 1zkh.pdb file
Complete list - r 2 2 Bytes
HEADER GENE REGULATION 02-MAY-05 1ZKH
TITLE SOLUTION STRUCTURE OF A HUMAN UBIQUITIN-LIKE DOMAIN IN SF3A1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPLICING FACTOR 3 SUBUNIT 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UBIQUITIN-LIKE DOMAIN;
COMPND 5 SYNONYM: SPLICEOSOME ASSOCIATED PROTEIN 114, SAP 114, SF3A120, SF3A1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: SF3A1, SAP114;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B21 (DE3) GOLD MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11
KEYWDS UBIQUITIN, SPLICING FACTOR, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS
KEYWDS 2 CONSORTIUM, SGC, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.A.LUKIN,S.DHE-PAGANON,V.GUIDO,A.LEMAK,G.V.AVVAKUMOV,S.XUE,
AUTHOR 2 E.M.NEWMAN,F.MACKENZIE,M.SUNDSTROM,A.EDWARDS,C.H.ARROWSMITH,
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 02-MAR-22 1ZKH 1 REMARK
REVDAT 3 24-FEB-09 1ZKH 1 VERSN
REVDAT 2 07-JUN-05 1ZKH 1 AUTHOR
REVDAT 1 10-MAY-05 1ZKH 0
JRNL AUTH J.A.LUKIN,S.DHE-PAGANON,V.GUIDO,A.LEMAK,G.V.AVVAKUMOV,S.XUE,
JRNL AUTH 2 E.M.NEWMAN,F.MACKENZIE,M.SUNDSTROM,A.EDWARDS,C.H.ARROWSMITH
JRNL TITL SOLUTION STRUCTURE OF A HUMAN UBIQUITIN-LIKE DOMAIN IN SF3A1
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.6, CNS 1.1
REMARK 3 AUTHORS : BRUKER BIOSPIN, INC. (XWINNMR), BRUNGER, A. ET AL.
REMARK 3 (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZKH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000032821.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 300 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM PROTEIN, U-15N, U-13C; 300
REMARK 210 MM NACL, 1MM BENZAMIDINE, 10MM
REMARK 210 DTT, 0.01% NAN3, 10MM SODIUM
REMARK 210 ACETATE, 0.01MM ZNSO4, 90%H2O,
REMARK 210 10%D2O; 2MM PROTEIN, U-15N, U-
REMARK 210 13C; 300 MM NACL, 1MM
REMARK 210 BENZAMIDINE, 10MM DTT, 0.01%
REMARK 210 NAN3, 10MM SODIUM ACETATE,
REMARK 210 0.01MM ZNSO4, 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 : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.1, CYANA 2.0
REMARK 210 METHOD USED : 100 STRUCTURES WERE CALCULATED
REMARK 210 BY CYANA 2.0 USING 2667 NOE-
REMARK 210 DERIVED DISTANCE CONSTRAINTS,
REMARK 210 121 DIHEDRAL ANGLE CONSTRAINTS,
REMARK 210 AND 50 DISTANCE CONSTRAINTS FROM
REMARK 210 HYDROGEN BONDS. THE 20
REMARK 210 STRUCTURES WITH LOWEST TARGET
REMARK 210 FUNCTIONS WERE SUBJECTED TO
REMARK 210 REFINEMENT WITH CNS 1.1.
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 : 11
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 PHE A 60 94.31 -68.49
REMARK 500 1 MET A 72 87.46 -69.96
REMARK 500 2 MET A 72 93.28 -64.27
REMARK 500 3 ASN A 20 10.10 -146.96
REMARK 500 3 MET A 72 84.89 -69.18
REMARK 500 4 MET A 72 89.45 -67.24
REMARK 500 4 ALA A 73 -169.65 -77.06
REMARK 500 5 ASN A 20 11.84 -143.41
REMARK 500 5 MET A 72 90.29 -63.75
REMARK 500 6 MET A 72 86.30 -68.01
REMARK 500 7 LYS A 18 30.79 -94.88
REMARK 500 7 MET A 72 82.44 -66.05
REMARK 500 8 ASN A 20 15.67 -142.27
REMARK 500 8 MET A 72 97.13 -59.72
REMARK 500 8 GLU A 84 140.83 -179.94
REMARK 500 9 LYS A 18 26.82 -78.84
REMARK 500 9 ASN A 20 15.74 -140.99
REMARK 500 9 MET A 72 88.14 -65.27
REMARK 500 10 MET A 72 84.73 -67.24
REMARK 500 10 GLU A 84 -153.09 -149.42
REMARK 500 10 ARG A 85 -63.09 -109.41
REMARK 500 11 LYS A 18 31.64 -84.93
REMARK 500 11 MET A 72 92.83 -67.16
REMARK 500 11 GLU A 84 138.17 -173.05
REMARK 500 12 LYS A 18 30.46 -88.82
REMARK 500 12 MET A 72 85.40 -65.09
REMARK 500 12 ARG A 85 -58.04 -154.94
REMARK 500 13 MET A 72 92.31 -63.78
REMARK 500 13 GLU A 84 119.96 -165.01
REMARK 500 13 ARG A 85 93.86 -167.02
REMARK 500 14 ASN A 20 14.38 -142.43
REMARK 500 14 MET A 72 87.69 -63.01
REMARK 500 15 LYS A 18 30.64 -89.35
REMARK 500 15 ASN A 20 15.84 -143.12
REMARK 500 15 PHE A 60 92.75 -68.62
REMARK 500 15 MET A 72 88.03 -67.96
REMARK 500 15 LYS A 83 107.40 -49.70
REMARK 500 15 ARG A 85 -73.72 67.00
REMARK 500 17 MET A 72 87.13 -67.48
REMARK 500 17 LYS A 83 -179.75 -58.10
REMARK 500 18 MET A 72 94.27 -62.80
REMARK 500 18 ARG A 85 -31.87 -138.43
REMARK 500 19 MET A 72 87.79 -62.04
REMARK 500 19 ARG A 85 29.72 -148.78
REMARK 500 20 LYS A 18 31.43 -81.96
REMARK 500 20 ASN A 20 19.27 -147.29
REMARK 500 20 MET A 72 90.09 -69.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HS00002 RELATED DB: TARGETDB
DBREF 1ZKH A 1 86 UNP Q15459 SF3A1_HUMAN 704 789
SEQRES 1 A 86 PRO VAL SER ILE LYS VAL GLN VAL PRO ASN MET GLN ASP
SEQRES 2 A 86 LYS THR GLU TRP LYS LEU ASN GLY GLN VAL LEU VAL PHE
SEQRES 3 A 86 THR LEU PRO LEU THR ASP GLN VAL SER VAL ILE LYS VAL
SEQRES 4 A 86 LYS ILE HIS GLU ALA THR GLY MET PRO ALA GLY LYS GLN
SEQRES 5 A 86 LYS LEU GLN TYR GLU GLY ILE PHE ILE LYS ASP SER ASN
SEQRES 6 A 86 SER LEU ALA TYR TYR ASN MET ALA ASN GLY ALA VAL ILE
SEQRES 7 A 86 HIS LEU ALA LEU LYS GLU ARG GLY
HELIX 1 1 GLN A 33 THR A 45 1 13
HELIX 2 2 SER A 66 ASN A 71 1 6
SHEET 1 A 5 VAL A 23 LEU A 28 0
SHEET 2 A 5 VAL A 2 GLN A 7 -1 N ILE A 4 O PHE A 26
SHEET 3 A 5 ALA A 76 LEU A 82 1 O ILE A 78 N GLN A 7
SHEET 4 A 5 GLN A 52 TYR A 56 -1 N GLN A 55 O HIS A 79
SHEET 5 A 5 ILE A 59 ILE A 61 -1 O ILE A 59 N TYR A 56
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