Header list of 2b8a.pdb file
Complete list - r 9 2 Bytes
HEADER HORMONE/GROWTH FACTOR 06-OCT-05 2B8A
TITLE HIGH RESOLUTION STRUCTURE OF THE HDGF PWWP DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATOMA-DERIVED GROWTH FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PWWP DOMAIN;
COMPND 5 SYNONYM: HDGF;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: HDGF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PHIS PARALLEL II
KEYWDS PWWP, HDGF, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 26
AUTHOR S.M.LUKASIK,T.CIERPICKI,M.BORLOZ,J.GREMBECKA,A.EVERETT,J.H.BUSHWELLER
REVDAT 4 09-MAR-22 2B8A 1 REMARK
REVDAT 3 24-FEB-09 2B8A 1 VERSN
REVDAT 2 21-MAR-06 2B8A 1 JRNL
REVDAT 1 06-DEC-05 2B8A 0
JRNL AUTH S.M.LUKASIK,T.CIERPICKI,M.BORLOZ,J.GREMBECKA,A.EVERETT,
JRNL AUTH 2 J.H.BUSHWELLER
JRNL TITL HIGH RESOLUTION STRUCTURE OF THE HDGF PWWP DOMAIN: A
JRNL TITL 2 POTENTIAL DNA BINDING DOMAIN.
JRNL REF PROTEIN SCI. V. 15 314 2006
JRNL REFN ISSN 0961-8368
JRNL PMID 16384999
JRNL DOI 10.1110/PS.051751706
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.3, CNS 1.1
REMARK 3 AUTHORS : DELAGLIO ET AL (NMRPIPE), BRUNGER ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BAED ON 1415 DISTANCE
REMARK 3 RESTRAINTS, 79 DIHEDRAL ANGLES, 23 HYDROGEN BONDS, 54 JHNHA
REMARK 3 COUPLINGS AND 258 RDCS
REMARK 4
REMARK 4 2B8A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034799.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301; 301
REMARK 210 PH : 6.5; 6.5
REMARK 210 IONIC STRENGTH : 50 MM; 200 MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : HDGF U-15N,13C; 20 MM PHOSPHATE
REMARK 210 BUFFER 6.5; 50 MM KCL; 1 MM DTT;
REMARK 210 HDGF U-15N,13C; 20 MM PHOSPHATE
REMARK 210 BUFFER 6.5; 200 MM NACL; 1 MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; TROSY-
REMARK 210 HNCO WITH HN COUPLINGS; TROSY-
REMARK 210 HNCO WITH NCO COUPLINGS; TROSY-
REMARK 210 HNCO WITH COCA COUPLINGS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.110, CYANA 1.0.5
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 26
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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: 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 ARG A 3 78.85 -118.45
REMARK 500 1 SER A 4 93.00 58.15
REMARK 500 1 GLU A 35 -80.24 -60.73
REMARK 500 1 ALA A 36 -63.02 -169.94
REMARK 500 1 ALA A 37 26.20 -166.36
REMARK 500 1 LYS A 39 -164.65 41.58
REMARK 500 1 SER A 40 56.09 -90.44
REMARK 500 1 ASN A 43 56.11 -153.98
REMARK 500 1 PHE A 50 178.53 -56.47
REMARK 500 1 PRO A 76 158.59 -48.26
REMARK 500 1 LYS A 80 141.28 66.34
REMARK 500 1 LYS A 96 159.92 62.52
REMARK 500 1 SER A 103 108.49 60.90
REMARK 500 2 SER A 2 -36.41 179.17
REMARK 500 2 ARG A 3 98.49 64.27
REMARK 500 2 SER A 4 -58.73 -136.68
REMARK 500 2 GLU A 35 -78.31 -84.21
REMARK 500 2 ALA A 36 -40.31 -168.76
REMARK 500 2 ALA A 37 86.19 -160.74
REMARK 500 2 VAL A 38 19.01 -150.17
REMARK 500 2 LYS A 39 -172.01 46.05
REMARK 500 2 THR A 41 89.78 -165.12
REMARK 500 2 ALA A 42 -75.18 -75.29
REMARK 500 2 ASN A 43 52.81 -156.64
REMARK 500 2 LYS A 80 144.15 63.37
REMARK 500 2 ASN A 92 87.43 -155.30
REMARK 500 2 CYS A 108 101.50 60.53
REMARK 500 3 GLN A 7 172.03 69.55
REMARK 500 3 GLU A 35 -86.05 -66.40
REMARK 500 3 ALA A 36 -54.58 -173.80
REMARK 500 3 ALA A 37 65.67 -170.30
REMARK 500 3 LYS A 39 -72.04 67.54
REMARK 500 3 SER A 40 40.56 176.31
REMARK 500 3 ASN A 43 56.65 -156.44
REMARK 500 3 PHE A 50 179.32 -57.57
REMARK 500 3 LYS A 80 141.22 62.70
REMARK 500 3 ASN A 92 84.09 -156.24
REMARK 500 3 TYR A 100 77.12 58.36
REMARK 500 3 GLN A 101 -46.86 -163.38
REMARK 500 3 CYS A 108 109.44 60.54
REMARK 500 4 ARG A 3 105.65 61.56
REMARK 500 4 SER A 4 141.49 -170.40
REMARK 500 4 GLU A 35 -94.54 -55.29
REMARK 500 4 ALA A 36 -48.69 -174.33
REMARK 500 4 ALA A 37 80.76 179.06
REMARK 500 4 VAL A 38 14.36 -146.78
REMARK 500 4 LYS A 39 -60.60 -166.05
REMARK 500 4 SER A 40 43.05 171.98
REMARK 500 4 ASN A 43 56.52 -156.06
REMARK 500 4 LYS A 80 144.56 63.65
REMARK 500
REMARK 500 THIS ENTRY HAS 404 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2B8A A 1 110 UNP Q8VHK7 HDGF_RAT 1 110
SEQRES 1 A 110 MET SER ARG SER ASN ARG GLN LYS GLU TYR LYS CYS GLY
SEQRES 2 A 110 ASP LEU VAL PHE ALA LYS MET LYS GLY TYR PRO HIS TRP
SEQRES 3 A 110 PRO ALA ARG ILE ASP GLU MET PRO GLU ALA ALA VAL LYS
SEQRES 4 A 110 SER THR ALA ASN LYS TYR GLN VAL PHE PHE PHE GLY THR
SEQRES 5 A 110 HIS GLU THR ALA PHE LEU GLY PRO LYS ASP LEU PHE PRO
SEQRES 6 A 110 TYR GLU GLU SER LYS GLU LYS PHE GLY LYS PRO ASN LYS
SEQRES 7 A 110 ARG LYS GLY PHE SER GLU GLY LEU TRP GLU ILE GLU ASN
SEQRES 8 A 110 ASN PRO THR VAL LYS ALA SER GLY TYR GLN SER SER GLN
SEQRES 9 A 110 LYS LYS SER CYS ALA GLU
HELIX 1 1 GLY A 59 LYS A 61 5 3
HELIX 2 2 TYR A 66 GLY A 74 1 9
HELIX 3 3 GLY A 81 ASN A 92 1 12
SHEET 1 A 5 GLU A 54 LEU A 58 0
SHEET 2 A 5 TYR A 45 PHE A 49 -1 N PHE A 49 O GLU A 54
SHEET 3 A 5 TYR A 23 GLU A 32 -1 N ARG A 29 O PHE A 48
SHEET 4 A 5 LEU A 15 MET A 20 -1 N VAL A 16 O ALA A 28
SHEET 5 A 5 LEU A 63 PRO A 65 -1 O PHE A 64 N PHE A 17
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