Header list of 2bid.pdb file
Complete list - t 27 2 Bytes
HEADER APOPTOSIS 27-JAN-99 2BID
TITLE HUMAN PRO-APOPTOTIC PROTEIN BID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (BID);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 OTHER_DETAILS: AFTER THROMBIN CLEAVAGE, BID HAS TWO EXTRA RESIDUES,
COMPND 6 GLY AND SER, AT ITS N- TERMINUS BEFORE MET.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX-2T;
SOURCE 8 OTHER_DETAILS: BID WAS EXPRESSED IN E. COLI WITH GST FUSED AT THE N-
SOURCE 9 TERMINUS.
KEYWDS PROGRAMMED CELL DEATH, APOPTOSIS REGULATION AND AMPLIFICATION,
KEYWDS 2 APOPTOSIS
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR J.J.CHOU,H.LI,G.S.SALVESEN,J.YUAN,G.WAGNER
REVDAT 3 27-OCT-21 2BID 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2BID 1 VERSN
REVDAT 1 02-FEB-00 2BID 0
JRNL AUTH J.J.CHOU,H.LI,G.S.SALVESEN,J.YUAN,G.WAGNER
JRNL TITL SOLUTION STRUCTURE OF BID, AN INTRACELLULAR AMPLIFIER OF
JRNL TITL 2 APOPTOTIC SIGNALING.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 96 615 1999
JRNL REFN ISSN 0092-8674
JRNL PMID 10089877
JRNL DOI 10.1016/S0092-8674(00)80572-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 2BID COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JAN-99.
REMARK 100 THE DEPOSITION ID IS D_1000000399.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : SEE ARTICLE FOR DETAILS
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY; UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1, DYANA, XEASY, FELIX
REMARK 210 97
REMARK 210 METHOD USED : DISTANCE GEOMETRY
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : ZERO VIOLATION AND LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: SEE ARTICLE FOR DETAILS.
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 SER A 121 H ARG A 125 1.37
REMARK 500 O VAL A 161 H THR A 165 1.42
REMARK 500 O HIS A 174 H ASN A 178 1.47
REMARK 500 O LYS A 146 H MET A 150 1.53
REMARK 500 O VAL A 23 H LEU A 27 1.54
REMARK 500 O LEU A 129 H LEU A 133 1.56
REMARK 500 O LEU A 184 H TYR A 187 1.56
REMARK 500 O GLU A 147 H LEU A 151 1.57
REMARK 500 O TYR A 187 H SER A 190 1.58
REMARK 500 O ARG A 120 H ASP A 124 1.58
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 SER A 2 178.96 68.99
REMARK 500 1 ASP A 4 30.75 -144.28
REMARK 500 1 GLU A 6 -58.82 70.65
REMARK 500 1 VAL A 7 103.53 -58.72
REMARK 500 1 CYS A 17 -28.52 -39.44
REMARK 500 1 ASP A 32 -159.79 54.66
REMARK 500 1 ASN A 33 -159.10 -58.80
REMARK 500 1 PHE A 35 35.31 177.75
REMARK 500 1 ARG A 37 -32.13 -39.60
REMARK 500 1 GLU A 45 17.97 -149.94
REMARK 500 1 PRO A 47 -165.17 -72.59
REMARK 500 1 ALA A 50 160.28 60.31
REMARK 500 1 GLN A 52 176.86 179.67
REMARK 500 1 GLU A 54 54.76 -164.14
REMARK 500 1 TYR A 56 -80.47 -43.67
REMARK 500 1 LEU A 59 -152.74 -79.15
REMARK 500 1 ASP A 62 73.80 40.70
REMARK 500 1 ARG A 65 138.48 67.94
REMARK 500 1 SER A 66 176.24 79.23
REMARK 500 1 SER A 67 -173.37 -53.96
REMARK 500 1 SER A 78 55.32 27.03
REMARK 500 1 HIS A 91 -75.14 -71.03
REMARK 500 1 ARG A 101 -31.18 -37.91
REMARK 500 1 SER A 102 52.45 -97.88
REMARK 500 1 ILE A 103 131.82 -39.99
REMARK 500 1 PRO A 104 -169.59 -58.04
REMARK 500 1 PRO A 105 94.95 -58.20
REMARK 500 1 ARG A 116 -67.11 -28.73
REMARK 500 1 ASN A 117 55.67 16.34
REMARK 500 1 THR A 118 -129.71 31.91
REMARK 500 1 SER A 121 -82.14 -19.69
REMARK 500 1 GLU A 123 -62.14 -90.90
REMARK 500 1 LEU A 133 -72.56 -66.77
REMARK 500 1 ARG A 142 -92.29 -98.28
REMARK 500 1 ASP A 143 -55.91 71.58
REMARK 500 1 MET A 144 -82.51 -75.47
REMARK 500 1 GLU A 147 -70.63 -30.88
REMARK 500 1 LYS A 148 -80.96 -47.84
REMARK 500 1 LEU A 153 -81.82 -70.65
REMARK 500 1 ALA A 158 -75.41 -55.49
REMARK 500 1 LYS A 159 -31.83 -37.70
REMARK 500 1 LEU A 169 -78.52 -32.87
REMARK 500 1 ASN A 178 -72.47 -88.36
REMARK 500 1 PHE A 179 -30.47 -35.75
REMARK 500 1 ASN A 183 -37.76 -160.33
REMARK 500 1 MET A 196 -58.98 -129.73
REMARK 500 2 SER A 2 97.51 -38.70
REMARK 500 2 MET A 3 144.30 163.83
REMARK 500 2 CYS A 5 -159.46 -97.53
REMARK 500 2 GLU A 6 67.24 180.00
REMARK 500
REMARK 500 THIS ENTRY HAS 753 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2BID A 3 197 UNP P55957 BID_HUMAN 1 195
SEQADV 2BID GLY A 1 UNP P55957 INSERTION
SEQADV 2BID SER A 2 UNP P55957 INSERTION
SEQRES 1 A 197 GLY SER MET ASP CYS GLU VAL ASN ASN GLY SER SER LEU
SEQRES 2 A 197 ARG ASP GLU CYS ILE THR ASN LEU LEU VAL PHE GLY PHE
SEQRES 3 A 197 LEU GLN SER CYS SER ASP ASN SER PHE ARG ARG GLU LEU
SEQRES 4 A 197 ASP ALA LEU GLY HIS GLU LEU PRO VAL LEU ALA PRO GLN
SEQRES 5 A 197 TRP GLU GLY TYR ASP GLU LEU GLN THR ASP GLY ASN ARG
SEQRES 6 A 197 SER SER HIS SER ARG LEU GLY ARG ILE GLU ALA ASP SER
SEQRES 7 A 197 GLU SER GLN GLU ASP ILE ILE ARG ASN ILE ALA ARG HIS
SEQRES 8 A 197 LEU ALA GLN VAL GLY ASP SER MET ASP ARG SER ILE PRO
SEQRES 9 A 197 PRO GLY LEU VAL ASN GLY LEU ALA LEU GLN LEU ARG ASN
SEQRES 10 A 197 THR SER ARG SER GLU GLU ASP ARG ASN ARG ASP LEU ALA
SEQRES 11 A 197 THR ALA LEU GLU GLN LEU LEU GLN ALA TYR PRO ARG ASP
SEQRES 12 A 197 MET GLU LYS GLU LYS THR MET LEU VAL LEU ALA LEU LEU
SEQRES 13 A 197 LEU ALA LYS LYS VAL ALA SER HIS THR PRO SER LEU LEU
SEQRES 14 A 197 ARG ASP VAL PHE HIS THR THR VAL ASN PHE ILE ASN GLN
SEQRES 15 A 197 ASN LEU ARG THR TYR VAL ARG SER LEU ALA ARG ASN GLY
SEQRES 16 A 197 MET ASP
HELIX 1 H1 GLU A 16 SER A 31 1 16
HELIX 2 H2 PHE A 35 GLY A 43 1 9
HELIX 3 H3 GLN A 81 ARG A 101 1 21
HELIX 4 H4 LEU A 107 ARG A 116 1 10
HELIX 5 H5 SER A 121 GLN A 138 1 18
HELIX 6 H6 GLU A 147 HIS A 164 1 18
HELIX 7 H7 LEU A 169 GLN A 182 1 14
HELIX 8 H8 ARG A 185 ASN A 194 1 10
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 - t 27 2 Bytes