Header list of 1dv9.pdb file
Complete list - b 16 2 Bytes
HEADER TRANSPORT PROTEIN 20-JAN-00 1DV9
TITLE STRUCTURAL CHANGES ACCOMPANYING PH-INDUCED DISSOCIATION OF THE B-
TITLE 2 LACTOGLOBULIN DIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BETA-LACTOGLOBULIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: SMALL PROTEIN FOUND IN THE WHEY OF MILK OF RUMINANTS
COMPND 6 AND OTHER SPECIES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 VARIANT: A;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PPIC9;
SOURCE 9 OTHER_DETAILS: P.PASTORIS GS115/HIS+BLG/MUT+ CONTAINING PPIC9; PPIC9
SOURCE 10 DERIVED FROM PTTQ18BLG BY PCR
KEYWDS BETA-LACTOGLOBULIN, BETA-BARREL, LOW PH STRUCTURE, TRIPLE RESONANCE
KEYWDS 2 EXPERIMENTS, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR S.UHRINOVA,M.H.SMITH,G.B.JAMESON,D.UHRIN,L.SAWYER,P.N.BARLOW
REVDAT 5 16-FEB-22 1DV9 1 REMARK
REVDAT 4 24-FEB-09 1DV9 1 VERSN
REVDAT 3 01-APR-03 1DV9 1 JRNL
REVDAT 2 07-APR-00 1DV9 1 JRNL
REVDAT 1 09-FEB-00 1DV9 0
JRNL AUTH S.UHRINOVA,M.H.SMITH,G.B.JAMESON,D.UHRIN,L.SAWYER,P.N.BARLOW
JRNL TITL STRUCTURAL CHANGES ACCOMPANYING PH-INDUCED DISSOCIATION OF
JRNL TITL 2 THE BETA-LACTOGLOBULIN DIMER.
JRNL REF BIOCHEMISTRY V. 39 3565 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10736155
JRNL DOI 10.1021/BI992629O
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH H.DENTON,M.SMITH,H.HUSI,D.UHRIN,P.N.BARLOW,C.A.BATT,L.SAWYER
REMARK 1 TITL ISOTOPICALLY LABELLED BOVINE BETA-LACTOGLOBULIN EXPRESSED IN
REMARK 1 TITL 2 P. PASTORIS
REMARK 1 REF PROTEIN EXPR.PURIF. V. 14 97 1998
REMARK 1 REFN ISSN 1046-5928
REMARK 1 DOI 10.1006/PREP.1998.0924
REMARK 1 REFERENCE 2
REMARK 1 AUTH S.UHRINOVA,D.UHRIN,H.DENTON,M.SMITH,L.SAWYER,P.N.BARLOW
REMARK 1 TITL COMPLETE ASSIGNMENT OF 1H, 13C AND 15N CHEMICAL SHIFTS FOR
REMARK 1 TITL 2 BOVINE BETA-LACTOGLOBULIN: SECONDARY STRUCTURE AND TOPOLOGY
REMARK 1 TITL 3 OF THE NATIVE STATE IS RETAINED IN A PARTIALLY UNFOLDED
REMARK 1 TITL 4 FORM.
REMARK 1 REF J.BIOMOL.NMR V. 12 89 1998
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008268528695
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 97.0, CNS 0.9
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS (FELIX), BRUNGER ET AL.
REMARK 3 (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 2715 RESTRAINTS, OUT OF WHICH 77 ARE HYDROGEN BONDS AND 110 ARE
REMARK 3 TORSION ANGLES
REMARK 4
REMARK 4 1DV9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010403.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 2.7
REMARK 210 IONIC STRENGTH : NOT KNOWN
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM B-LACTOGLOBULINE-15N,13C;
REMARK 210 50MM PHOSPHATE BUFFER; 90% H2O,
REMARK 210 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1995, X-PLOR ARIA, CNS 0.9
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 60
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TOTAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 14
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE NMR
REMARK 210 SPECTRA
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 THR A 4 81.93 -161.18
REMARK 500 1 GLN A 5 -62.62 -148.70
REMARK 500 1 LYS A 8 154.27 59.64
REMARK 500 1 ASP A 33 -70.25 -145.94
REMARK 500 1 ARG A 40 88.52 -58.78
REMARK 500 1 GLU A 44 -44.19 -140.79
REMARK 500 1 ASN A 63 -35.97 174.06
REMARK 500 1 ASP A 64 39.24 -93.06
REMARK 500 1 GLU A 65 99.06 49.97
REMARK 500 1 CYS A 66 79.27 61.59
REMARK 500 1 THR A 76 -61.52 -121.51
REMARK 500 1 LYS A 77 -42.52 -169.80
REMARK 500 1 ALA A 86 -80.27 -145.23
REMARK 500 1 GLU A 89 113.24 -179.28
REMARK 500 1 LEU A 95 -76.35 -66.74
REMARK 500 1 TYR A 99 -80.70 61.00
REMARK 500 1 LYS A 100 56.68 -100.20
REMARK 500 1 LYS A 101 -63.96 -158.55
REMARK 500 1 PRO A 126 61.32 -65.10
REMARK 500 1 GLU A 127 154.70 167.58
REMARK 500 1 ASP A 130 -18.33 -46.66
REMARK 500 1 HIS A 146 -39.65 -177.17
REMARK 500 2 GLN A 5 -42.21 -171.73
REMARK 500 2 LYS A 8 104.98 62.55
REMARK 500 2 ILE A 12 -87.60 52.07
REMARK 500 2 ASP A 28 107.75 -161.85
REMARK 500 2 ALA A 34 -158.69 70.29
REMARK 500 2 SER A 36 29.17 -148.06
REMARK 500 2 ARG A 40 92.97 -60.97
REMARK 500 2 VAL A 43 154.44 -45.18
REMARK 500 2 GLU A 44 -47.01 -133.98
REMARK 500 2 GLU A 62 -83.73 -138.68
REMARK 500 2 ASN A 63 20.83 -147.82
REMARK 500 2 ASP A 64 58.48 -145.41
REMARK 500 2 GLU A 65 175.06 56.36
REMARK 500 2 CYS A 66 104.30 -56.77
REMARK 500 2 ALA A 86 -83.76 -129.28
REMARK 500 2 LEU A 87 -76.44 -62.51
REMARK 500 2 ASN A 88 -46.68 -151.67
REMARK 500 2 LEU A 95 -79.13 -75.03
REMARK 500 2 TYR A 99 -69.59 66.55
REMARK 500 2 LYS A 101 -45.89 -178.63
REMARK 500 2 SER A 110 77.06 -63.50
REMARK 500 2 ALA A 111 -35.30 176.46
REMARK 500 2 GLU A 112 69.31 -166.34
REMARK 500 2 THR A 125 -65.40 -161.61
REMARK 500 2 PRO A 126 99.68 -39.56
REMARK 500 2 ASP A 130 -17.87 -47.51
REMARK 500 2 LYS A 141 30.42 37.22
REMARK 500 2 PRO A 144 109.83 -44.45
REMARK 500
REMARK 500 THIS ENTRY HAS 685 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BSY RELATED DB: PDB
REMARK 900 DIMERIC BETA-GLOBULIN AT PH 7.1
REMARK 900 RELATED ID: 2BLG RELATED DB: PDB
REMARK 900 DIMER AT 8.2
REMARK 900 RELATED ID: 3BLG RELATED DB: PDB
REMARK 900 DIMER AT 6.2
REMARK 900 RELATED ID: 1B0O RELATED DB: PDB
REMARK 900 BETA-LACTOGLOBULIN COMPLEXED WITH PALMITATE
REMARK 900 RELATED ID: 1BEB RELATED DB: PDB
REMARK 900 BOVINE BETA LACTOGLOBULINE, LATTICE X
REMARK 900 RELATED ID: 1BSO RELATED DB: PDB
REMARK 900 BETA LACTOBLOBULINE WITH 12 BROMODODECANOIC ACID
DBREF 1DV9 A 1 162 UNP P02754 LACB_BOVIN 17 178
SEQADV 1DV9 ALA A 1 UNP P02754 LEU 17 SEE REMARK 999
SEQADV 1DV9 TYR A 2 UNP P02754 ILE 18 SEE REMARK 999
SEQADV 1DV9 PHE A 105 UNP P02754 VAL 121 SEE REMARK 999
SEQRES 1 A 162 ALA TYR VAL THR GLN THR MET LYS GLY LEU ASP ILE GLN
SEQRES 2 A 162 LYS VAL ALA GLY THR TRP TYR SER LEU ALA MET ALA ALA
SEQRES 3 A 162 SER ASP ILE SER LEU LEU ASP ALA GLN SER ALA PRO LEU
SEQRES 4 A 162 ARG VAL TYR VAL GLU GLU LEU LYS PRO THR PRO GLU GLY
SEQRES 5 A 162 ASP LEU GLU ILE LEU LEU GLN LYS TRP GLU ASN ASP GLU
SEQRES 6 A 162 CYS ALA GLN LYS LYS ILE ILE ALA GLU LYS THR LYS ILE
SEQRES 7 A 162 PRO ALA VAL PHE LYS ILE ASP ALA LEU ASN GLU ASN LYS
SEQRES 8 A 162 VAL LEU VAL LEU ASP THR ASP TYR LYS LYS TYR LEU LEU
SEQRES 9 A 162 PHE CYS MET GLU ASN SER ALA GLU PRO GLU GLN SER LEU
SEQRES 10 A 162 VAL CYS GLN CYS LEU VAL ARG THR PRO GLU VAL ASP ASP
SEQRES 11 A 162 GLU ALA LEU GLU LYS PHE ASP LYS ALA LEU LYS ALA LEU
SEQRES 12 A 162 PRO MET HIS ILE ARG LEU SER PHE ASN PRO THR GLN LEU
SEQRES 13 A 162 GLU GLU GLN CYS HIS ILE
HELIX 1 1 ILE A 12 ALA A 16 5 5
HELIX 2 2 ASP A 129 LYS A 141 1 13
HELIX 3 3 ASN A 152 GLU A 158 1 7
SHEET 1 A10 GLY A 17 THR A 18 0
SHEET 2 A10 TYR A 42 PRO A 48 -1 N LEU A 46 O GLY A 17
SHEET 3 A10 LEU A 54 LYS A 60 -1 O GLU A 55 N LYS A 47
SHEET 4 A10 ALA A 67 LYS A 75 -1 O ALA A 67 N LYS A 60
SHEET 5 A10 VAL A 81 LYS A 83 -1 O LYS A 83 N GLU A 74
SHEET 6 A10 LYS A 91 THR A 97 -1 O VAL A 92 N PHE A 82
SHEET 7 A10 TYR A 102 GLU A 108 -1 N LEU A 104 O ASP A 96
SHEET 8 A10 VAL A 118 VAL A 123 -1 O VAL A 118 N MET A 107
SHEET 9 A10 TYR A 20 ALA A 26 -1 O TYR A 20 N VAL A 123
SHEET 10 A10 ILE A 147 SER A 150 -1 N ILE A 147 O ALA A 26
SSBOND 1 CYS A 66 CYS A 160 1555 1555 2.03
SSBOND 2 CYS A 106 CYS A 119 1555 1555 2.03
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 - b 16 2 Bytes