Header list of 1cl3.pdb file
Complete list - b 16 2 Bytes
HEADER GENE REGULATION 04-MAY-99 1CL3
TITLE MOLECULAR INSIGHTS INTO PEBP2/CBF-SMMHC ASSOCIATED ACUTE LEUKEMIA
TITLE 2 REVEALED FROM THE THREE-DIMENSIONAL STRUCTURE OF PEBP2/CBF BETA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POLYOMAVIRUS ENHANCER BINDING PROTEIN 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BETA SUBUNIT;
COMPND 5 SYNONYM: PEBP2/CBF;
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 CELLULAR_LOCATION: NUCLEUS;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3A
KEYWDS STRUCTURE FROM MOLMOL, CORE-BINDING FACTOR, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR M.GOGER,V.GUPTA,W.Y.KIM,K.SHIGESADA,Y.ITO,M.H.WERNER
REVDAT 4 16-FEB-22 1CL3 1 REMARK
REVDAT 3 24-FEB-09 1CL3 1 VERSN
REVDAT 2 01-APR-03 1CL3 1 JRNL
REVDAT 1 01-JAN-00 1CL3 0
JRNL AUTH M.GOGER,V.GUPTA,W.Y.KIM,K.SHIGESADA,Y.ITO,M.H.WERNER
JRNL TITL MOLECULAR INSIGHTS INTO PEBP2/CBF BETA-SMMHC ASSOCIATED
JRNL TITL 2 ACUTE LEUKEMIA REVEALED FROM THE STRUCTURE OF PEBP2/CBF BETA
JRNL REF NAT.STRUCT.BIOL. V. 6 620 1999
JRNL REFN ISSN 1072-8368
JRNL PMID 10404215
JRNL DOI 10.1038/10664
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.843
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: SEE JRNL CITATION
REMARK 4
REMARK 4 1CL3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY NDB.
REMARK 100 THE DEPOSITION ID IS D_1000000999.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 96% WATER/4% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : CBCACONH; HNCACB; 15N-EDITED
REMARK 210 NOESY; 13C-EDITED NOESY; 15N-
REMARK 210 HSQC; DIPSI(CO)NH; HDIPSI(CO)NH;
REMARK 210 HCCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500; DMX600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.843
REMARK 210 METHOD USED : DYNAMICAL SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST CONSTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 LEU A 103 H GLY A 105 1.53
REMARK 500 O ARG A 49 H ALA A 71 1.60
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 LEU A 21 -31.92 -135.64
REMARK 500 1 PRO A 36 161.07 -35.35
REMARK 500 1 HIS A 37 -12.36 -46.72
REMARK 500 1 PHE A 68 -72.93 -94.13
REMARK 500 1 SER A 72 156.90 179.41
REMARK 500 1 TRP A 73 -81.11 -85.52
REMARK 500 1 GLN A 77 -158.68 -59.66
REMARK 500 1 GLU A 91 -106.18 -76.02
REMARK 500 1 ALA A 92 -5.92 -58.52
REMARK 500 1 ASN A 104 70.86 -63.08
REMARK 500 1 LEU A 119 51.97 -90.67
REMARK 500 1 ASP A 128 13.71 -148.21
REMARK 500 2 ASP A 7 31.17 -89.83
REMARK 500 2 LEU A 21 -35.39 -138.54
REMARK 500 2 PRO A 36 177.69 -40.66
REMARK 500 2 PHE A 68 -73.46 -89.94
REMARK 500 2 SER A 72 -178.68 -171.58
REMARK 500 2 TRP A 73 -133.33 -82.63
REMARK 500 2 GLU A 76 46.84 -80.58
REMARK 500 2 GLN A 77 -176.83 -61.64
REMARK 500 2 GLN A 79 25.80 -74.96
REMARK 500 2 GLU A 91 -103.23 -75.29
REMARK 500 2 ASN A 104 63.95 -64.68
REMARK 500 2 HIS A 117 -80.80 -96.61
REMARK 500 2 ASP A 128 22.29 -149.90
REMARK 500 3 PRO A 6 3.19 -51.25
REMARK 500 3 GLN A 8 -70.52 -89.24
REMARK 500 3 PRO A 36 176.81 -41.53
REMARK 500 3 HIS A 37 -18.91 -47.37
REMARK 500 3 THR A 60 143.13 63.41
REMARK 500 3 PHE A 68 -78.94 -89.80
REMARK 500 3 SER A 72 128.17 -170.00
REMARK 500 3 TRP A 73 -78.62 -82.60
REMARK 500 3 GLU A 91 -108.01 -77.03
REMARK 500 3 ALA A 92 -7.79 -56.69
REMARK 500 3 ASN A 104 67.54 -65.85
REMARK 500 3 ASP A 120 46.27 -95.55
REMARK 500 3 ASP A 128 15.38 -143.29
REMARK 500 4 LEU A 21 -32.24 -132.97
REMARK 500 4 PRO A 36 -171.27 -43.96
REMARK 500 4 PHE A 68 -72.78 -91.38
REMARK 500 4 SER A 72 152.54 178.88
REMARK 500 4 TRP A 73 -79.87 -83.59
REMARK 500 4 GLN A 77 -144.85 -61.43
REMARK 500 4 GLN A 79 36.24 -81.56
REMARK 500 4 GLU A 91 -98.83 -75.85
REMARK 500 4 ALA A 92 -9.81 -58.53
REMARK 500 4 ASP A 120 58.50 -101.81
REMARK 500 4 ASP A 128 20.38 -154.25
REMARK 500 5 PRO A 36 -168.09 -49.23
REMARK 500
REMARK 500 THIS ENTRY HAS 267 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CL3 A 4 141 UNP Q13951 PEBB_HUMAN 4 141
SEQADV 1CL3 THR A 42 UNP Q13951 ALA 42 CONFLICT
SEQADV 1CL3 HIS A 117 UNP Q13951 GLN 117 CONFLICT
SEQRES 1 A 138 VAL VAL PRO ASP GLN ARG SER LYS PHE GLU ASN GLU GLU
SEQRES 2 A 138 PHE PHE ARG LYS LEU SER ARG GLU CYS GLU ILE LYS TYR
SEQRES 3 A 138 THR GLY PHE ARG ASP ARG PRO HIS GLU GLU ARG GLN THR
SEQRES 4 A 138 ARG PHE GLN ASN ALA CYS ARG ASP GLY ARG SER GLU ILE
SEQRES 5 A 138 ALA PHE VAL ALA THR GLY THR ASN LEU SER LEU GLN PHE
SEQRES 6 A 138 PHE PRO ALA SER TRP GLN GLY GLU GLN ARG GLN THR PRO
SEQRES 7 A 138 SER ARG GLU TYR VAL ASP LEU GLU ARG GLU ALA GLY LYS
SEQRES 8 A 138 VAL TYR LEU LYS ALA PRO MET ILE LEU ASN GLY VAL CYS
SEQRES 9 A 138 VAL ILE TRP LYS GLY TRP ILE ASP LEU HIS ARG LEU ASP
SEQRES 10 A 138 GLY MET GLY CYS LEU GLU PHE ASP GLU GLU ARG ALA GLN
SEQRES 11 A 138 GLN GLU ASP ALA LEU ALA GLN GLN
HELIX 1 H1 GLN A 8 ASN A 14 1 7
HELIX 2 H2 GLU A 16 LEU A 21 1 6
HELIX 3 H3 HIS A 37 ASP A 50 1 14
HELIX 4 H4 ARG A 83 ARG A 90 5 8
HELIX 5 H5 GLU A 129 GLN A 140 5 12
SHEET 1 S1 1 GLU A 24 THR A 30 0
SHEET 1 S2 1 ARG A 52 VAL A 58 0
SHEET 1 S3 1 THR A 62 PHE A 68 0
SHEET 1 S4 1 LYS A 94 ILE A 102 0
SHEET 1 S5 1 CYS A 107 LEU A 116 0
SHEET 1 S6 1 LEU A 119 PHE A 127 0
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