Header list of 1jzu.pdb file
Complete list - t 27 2 Bytes
HEADER LIPID BINDING PROTEIN 17-SEP-01 1JZU
TITLE CELL TRANSFORMATION BY THE MYC ONCOGENE ACTIVATES EXPRESSION OF A
TITLE 2 LIPOCALIN: ANALYSIS OF THE GENE (Q83) AND SOLUTION STRUCTURE OF ITS
TITLE 3 PROTEIN PRODUCT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LIPOCALIN Q83;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: COTURNIX COTURNIX;
SOURCE 3 ORGANISM_COMMON: COMMON QUAIL;
SOURCE 4 ORGANISM_TAXID: 9091;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET3D-Q83
KEYWDS BETA BARREL, LIPOCALIN, LIPID BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.HARTL,T.MATT,W.SCHUELER,G.SIEMEISTER,G.KONTAXIS,K.KLOIBER,R.KONRAT,
AUTHOR 2 K.BISTER
REVDAT 4 27-OCT-21 1JZU 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1JZU 1 VERSN
REVDAT 2 07-OCT-03 1JZU 1 AUTHOR JRNL
REVDAT 1 15-JUL-03 1JZU 0
JRNL AUTH M.HARTL,T.MATT,W.SCHUELER,G.SIEMEISTER,G.KONTAXIS,K.KLOIBER,
JRNL AUTH 2 R.KONRAT,K.BISTER
JRNL TITL CELL TRANSFORMATION BY THE V-MYC ONCOGENE ABROGATES
JRNL TITL 2 C-MYC/MAX-MEDIATED SUPPRESSION OF A C/EBPBETA-DEPENDENT
JRNL TITL 3 LIPOCALIN GENE.
JRNL REF J.MOL.BIOL. V. 333 33 2003
JRNL REFN ISSN 0022-2836
JRNL PMID 14516741
JRNL DOI 10.1016/J.JMB.2003.08.018
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.KONTAXIS,T.MATT,W.SCHUELER,B.KRAEUTLER,K.BISTER,R.KONRAT
REMARK 1 TITL SEQUENCE-SPECIFIC RESONANCE ASSIGNMENTS OF Q83, A LIPOCALIN
REMARK 1 TITL 2 HIGHLY EXPRESSED IN V-MYC-TRANSFORMED AVIAN FIBROBLASTS
REMARK 1 REF J.BIOMOL.NMR V. 17 177 2000
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1008386018430
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1 REV B, CNS 1.0
REMARK 3 AUTHORS : VARIAN ASSOCIATES, INC. (VNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JZU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014382.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 299
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : 20MM POTASSIUM PHOSPHATE; 50MM
REMARK 210 POTASSIUM CHLORIDE; 0.5MM
REMARK 210 DITHIOTHREITOL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM LIPOCALIN Q83 U-15N,13C; 20
REMARK 210 MM POTASSIUM PHOSPHATE; 50 MM
REMARK 210 POTASSIUM CHLORIDE; 0.5MM
REMARK 210 DITHIOTHREITOL; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HCCH-TOCSY; 3D_CCH-TOCSY-NNH;
REMARK 210 3D_NOESY-HSQC:(TWO_13C,CA/METHYL-CENTERED,15N); 3D HNHA; CROSS-
REMARK 210 CORRELATED_RELAXATION_RATES_CA(I)HA(I)-DD/C'(I)-CSA; CROSS-
REMARK 210 CORRELATED_RELAXATION_RATES_CA(I)HA(I)-DD/C'(I-1)-CSA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.8 REV 2001.030.21.27,
REMARK 210 ANSIG 3.3, NMRVIEW 4.1.3, ARIA/
REMARK 210 CNS 1.0
REMARK 210 METHOD USED : ARIA/CNS AUTOMATED REFINEMENT
REMARK 210 USING ALSO AMBIGUOUS NOE
REMARK 210 DISTANCE CONSTRAINTS; SIMULATED
REMARK 210 ANNEALING (TORSION ANGLE
REMARK 210 DYNAMICS)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 15
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 O ALA A 19 H MET A 112 1.52
REMARK 500 O ALA A 127 H LYS A 131 1.53
REMARK 500 O ILE A 128 H LEU A 132 1.58
REMARK 500 O ILE A 98 H ARG A 113 1.58
REMARK 500 O LYS A 84 H THR A 101 1.59
REMARK 500 O LEU A 18 O ALA A 144 2.10
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 2 -45.10 -178.31
REMARK 500 1 ASP A 5 125.21 -173.62
REMARK 500 1 VAL A 16 -41.63 -135.57
REMARK 500 1 GLU A 44 36.51 -160.35
REMARK 500 1 LYS A 55 54.15 178.70
REMARK 500 1 CYS A 59 -70.81 -151.13
REMARK 500 1 ARG A 60 -134.89 175.28
REMARK 500 1 LYS A 68 -114.14 178.76
REMARK 500 1 GLU A 74 -137.33 -121.17
REMARK 500 1 GLU A 79 54.88 -160.79
REMARK 500 1 GLU A 80 151.09 61.76
REMARK 500 1 LEU A 88 -155.15 -118.29
REMARK 500 1 ASP A 89 -111.76 70.81
REMARK 500 1 THR A 90 69.48 -151.10
REMARK 500 1 ASP A 91 39.62 -77.66
REMARK 500 1 SER A 94 -26.01 -171.57
REMARK 500 1 GLU A 120 71.94 -69.62
REMARK 500 1 ASN A 137 -50.45 -171.50
REMARK 500 1 TYR A 138 -177.41 176.61
REMARK 500 1 THR A 139 -68.17 -103.82
REMARK 500 1 ALA A 144 141.16 -173.76
REMARK 500 1 LEU A 146 127.71 -33.85
REMARK 500 1 ARG A 148 60.47 -163.71
REMARK 500 1 GLN A 149 -142.21 -138.31
REMARK 500 1 GLU A 150 -123.31 -45.35
REMARK 500 1 GLU A 151 -120.21 -75.45
REMARK 500 1 GLU A 156 133.64 -176.22
REMARK 500 2 ASP A 5 131.40 -173.36
REMARK 500 2 ILE A 9 59.34 -141.45
REMARK 500 2 VAL A 16 -50.27 -127.41
REMARK 500 2 ALA A 19 126.03 -174.52
REMARK 500 2 THR A 22 -39.49 -166.72
REMARK 500 2 LYS A 31 -157.19 -59.92
REMARK 500 2 MET A 32 105.26 54.05
REMARK 500 2 LYS A 33 134.84 -170.33
REMARK 500 2 GLU A 44 44.59 -158.32
REMARK 500 2 ASN A 57 86.12 -49.44
REMARK 500 2 ASP A 72 156.84 89.68
REMARK 500 2 GLU A 74 -133.83 -87.74
REMARK 500 2 GLU A 80 -173.36 57.22
REMARK 500 2 ALA A 81 -73.87 -57.78
REMARK 500 2 ASP A 89 -133.55 62.00
REMARK 500 2 THR A 90 97.99 -161.09
REMARK 500 2 SER A 94 -56.34 -178.81
REMARK 500 2 ASP A 105 -136.17 61.99
REMARK 500 2 GLU A 120 62.20 -68.32
REMARK 500 2 ARG A 136 32.60 -89.09
REMARK 500 2 ASN A 137 120.34 58.94
REMARK 500 2 ALA A 144 131.73 -170.75
REMARK 500 2 GLU A 151 -85.37 -94.64
REMARK 500
REMARK 500 THIS ENTRY HAS 603 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4664 RELATED DB: BMRB
REMARK 900 PRELIMINARY SEQUENCE-SPECIFIC RESONANCE ASSIGNMENTS OF Q83
DBREF 1JZU A 1 157 UNP Q9I9P7 EXFAB_COTJA 22 178
SEQADV 1JZU MET A 1 UNP Q9I9P7 ALA 22 ENGINEERED MUTATION
SEQRES 1 A 157 MET THR VAL PRO ASP ARG SER GLU ILE ALA GLY LYS TRP
SEQRES 2 A 157 TYR VAL VAL ALA LEU ALA SER ASN THR GLU PHE PHE LEU
SEQRES 3 A 157 ARG GLU LYS ASP LYS MET LYS MET ALA MET ALA ARG ILE
SEQRES 4 A 157 SER PHE LEU GLY GLU ASP GLU LEU LYS VAL SER TYR ALA
SEQRES 5 A 157 VAL PRO LYS PRO ASN GLY CYS ARG LYS TRP GLU THR THR
SEQRES 6 A 157 PHE LYS LYS THR SER ASP ASP GLY GLU VAL TYR TYR SER
SEQRES 7 A 157 GLU GLU ALA LYS LYS LYS VAL GLU VAL LEU ASP THR ASP
SEQRES 8 A 157 TYR LYS SER TYR ALA VAL ILE TYR ALA THR ARG VAL LYS
SEQRES 9 A 157 ASP GLY ARG THR LEU HIS MET MET ARG LEU TYR SER ARG
SEQRES 10 A 157 SER PRO GLU VAL SER PRO ALA ALA THR ALA ILE PHE ARG
SEQRES 11 A 157 LYS LEU ALA GLY GLU ARG ASN TYR THR ASP GLU MET VAL
SEQRES 12 A 157 ALA MET LEU PRO ARG GLN GLU GLU CYS THR VAL ASP GLU
SEQRES 13 A 157 VAL
HELIX 1 1 ASP A 5 ILE A 9 5 5
HELIX 2 2 THR A 22 LEU A 26 5 5
HELIX 3 3 ARG A 27 MET A 32 1 6
HELIX 4 4 SER A 122 ASN A 137 1 16
HELIX 5 5 THR A 139 VAL A 143 5 5
SHEET 1 A10 GLY A 11 ASN A 21 0
SHEET 2 A10 ALA A 35 LEU A 42 -1 N ALA A 35 O VAL A 15
SHEET 3 A10 GLU A 46 LYS A 55 -1 N GLU A 46 O LEU A 42
SHEET 4 A10 ARG A 60 SER A 70 -1 O ARG A 60 N LYS A 55
SHEET 5 A10 VAL A 75 GLU A 79 -1 O SER A 78 N THR A 69
SHEET 6 A10 LYS A 83 ASP A 89 -1 N LYS A 83 O GLU A 79
SHEET 7 A10 TYR A 95 LYS A 104 -1 O VAL A 97 N LEU A 88
SHEET 8 A10 ARG A 107 SER A 116 -1 O ARG A 107 N LYS A 104
SHEET 9 A10 GLY A 11 ASN A 21 -1 O TYR A 14 N SER A 116
SHEET 10 A10 ALA A 144 MET A 145 -1 O ALA A 144 N LEU A 18
SSBOND 1 CYS A 59 CYS A 152 1555 1555 2.03
CRYST1 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 - t 27 2 Bytes