Header list of 1bxl.pdb file
Complete list - 16 20 Bytes
HEADER COMPLEX (APOPTOSIS/PEPTIDE) 16-OCT-96 1BXL
TITLE STRUCTURE OF BCL-XL/BAK PEPTIDE COMPLEX, NMR, MINIMIZED AVERAGE
TITLE 2 STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BCL-XL;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: BAK PEPTIDE;
COMPND 7 CHAIN: B;
COMPND 8 FRAGMENT: RESIDUES 572 - 587 OF BAK PROTEIN;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: HMS174 (DE3);
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET29B;
SOURCE 8 EXPRESSION_SYSTEM_GENE: HUMAN BCL-XL, RESIDUES 1-44, 85-205,
SOURCE 9 DELETION MUTANT LACKING A FLEXIBLE LOOP (RESIDUES 45-84) AND THE C-
SOURCE 10 TERMINAL HYDROPHOBIC REGION, WITH A C-TERMINAL HIS-TAG;
SOURCE 11 MOL_ID: 2
KEYWDS APOPTOSIS, ALTERNATIVE SPLICING, COMPLEX (APOPTOSIS-PEPTIDE), COMPLEX
KEYWDS 2 (APOPTOSIS-PEPTIDE) COMPLEX
EXPDTA SOLUTION NMR
AUTHOR M.SATTLER,H.LIANG,D.NETTESHEIM,R.P.MEADOWS,J.E.HARLAN,M.EBERSTADT,
AUTHOR 2 H.YOON,S.B.SHUKER,B.S.CHANG,A.J.MINN,C.B.THOMPSON,S.W.FESIK
REVDAT 3 16-FEB-22 1BXL 1 REMARK
REVDAT 2 24-FEB-09 1BXL 1 VERSN
REVDAT 1 29-OCT-97 1BXL 0
JRNL AUTH M.SATTLER,H.LIANG,D.NETTESHEIM,R.P.MEADOWS,J.E.HARLAN,
JRNL AUTH 2 M.EBERSTADT,H.S.YOON,S.B.SHUKER,B.S.CHANG,A.J.MINN,
JRNL AUTH 3 C.B.THOMPSON,S.W.FESIK
JRNL TITL STRUCTURE OF BCL-XL-BAK PEPTIDE COMPLEX: RECOGNITION BETWEEN
JRNL TITL 2 REGULATORS OF APOPTOSIS.
JRNL REF SCIENCE V. 275 983 1997
JRNL REFN ISSN 0036-8075
JRNL PMID 9020082
JRNL DOI 10.1126/SCIENCE.275.5302.983
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: NULL
REMARK 4
REMARK 4 1BXL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172135.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NMR SPECTRA WERE RECORDED ON 1-3 MM SOLUTIONS OF BCL-XL
REMARK 210 COMPLEXED WITH A BAK PEPTIDE IN 10 MM SODIUM PHOSPHATE BUFFER
REMARK 210 (PH 6.5) AT 303K.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 MET A 45
REMARK 465 GLU A 46
REMARK 465 THR A 47
REMARK 465 PRO A 48
REMARK 465 SER A 49
REMARK 465 ALA A 50
REMARK 465 ILE A 51
REMARK 465 ASN A 52
REMARK 465 GLY A 53
REMARK 465 ASN A 54
REMARK 465 PRO A 55
REMARK 465 SER A 56
REMARK 465 TRP A 57
REMARK 465 HIS A 58
REMARK 465 LEU A 59
REMARK 465 ALA A 60
REMARK 465 ASP A 61
REMARK 465 SER A 62
REMARK 465 PRO A 63
REMARK 465 ALA A 64
REMARK 465 VAL A 65
REMARK 465 ASN A 66
REMARK 465 GLY A 67
REMARK 465 ALA A 68
REMARK 465 THR A 69
REMARK 465 GLY A 70
REMARK 465 HIS A 71
REMARK 465 SER A 72
REMARK 465 SER A 73
REMARK 465 SER A 74
REMARK 465 LEU A 75
REMARK 465 ASP A 76
REMARK 465 ALA A 77
REMARK 465 ARG A 78
REMARK 465 GLU A 79
REMARK 465 VAL A 80
REMARK 465 ILE A 81
REMARK 465 PRO A 82
REMARK 465 MET A 83
REMARK 465 ALA A 84
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 SER A -2 -179.96 -68.64
REMARK 500 MET A -1 -36.93 175.91
REMARK 500 ALA A 0 37.94 -166.28
REMARK 500 LYS A 20 -76.04 -55.72
REMARK 500 GLU A 32 -159.66 -62.29
REMARK 500 ASN A 33 77.46 66.94
REMARK 500 GLU A 36 -34.74 80.83
REMARK 500 ALA A 37 162.57 67.41
REMARK 500 GLU A 39 -38.80 -177.08
REMARK 500 GLU A 44 -78.06 -57.25
REMARK 500 PHE A 105 -73.41 -152.21
REMARK 500 SER A 106 -163.17 -178.08
REMARK 500 LEU A 108 -64.33 -100.45
REMARK 500 ILE A 114 135.35 65.03
REMARK 500 THR A 115 148.17 173.93
REMARK 500 PHE A 131 96.74 -63.09
REMARK 500 ASP A 133 -44.35 -160.14
REMARK 500 ASP A 176 -70.40 -122.47
REMARK 500 ASN A 185 54.81 -142.18
REMARK 500 GLU A 208 -83.73 57.88
REMARK 500 ARG A 209 -90.26 -39.36
REMARK 500 HIS A 212 -31.36 172.71
REMARK 500 HIS A 213 109.84 4.01
REMARK 500 HIS A 215 23.40 -152.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 6 0.25 SIDE CHAIN
REMARK 500 ARG A 34 0.32 SIDE CHAIN
REMARK 500 ARG A 91 0.31 SIDE CHAIN
REMARK 500 ARG A 100 0.23 SIDE CHAIN
REMARK 500 ARG A 102 0.32 SIDE CHAIN
REMARK 500 ARG A 103 0.31 SIDE CHAIN
REMARK 500 ARG A 132 0.21 SIDE CHAIN
REMARK 500 ARG A 139 0.32 SIDE CHAIN
REMARK 500 ARG A 165 0.23 SIDE CHAIN
REMARK 500 ARG A 204 0.29 SIDE CHAIN
REMARK 500 ARG A 209 0.31 SIDE CHAIN
REMARK 500 ARG B 576 0.25 SIDE CHAIN
REMARK 500 ARG B 587 0.29 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BXL A 1 209 UNP Q07817 BCLX_HUMAN 1 209
DBREF 1BXL B 572 587 UNP Q16611 BAK_HUMAN 72 87
SEQRES 1 A 221 MET SER MET ALA MET SER GLN SER ASN ARG GLU LEU VAL
SEQRES 2 A 221 VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY TYR
SEQRES 3 A 221 SER TRP SER GLN PHE SER ASP VAL GLU GLU ASN ARG THR
SEQRES 4 A 221 GLU ALA PRO GLU GLY THR GLU SER GLU MET GLU THR PRO
SEQRES 5 A 221 SER ALA ILE ASN GLY ASN PRO SER TRP HIS LEU ALA ASP
SEQRES 6 A 221 SER PRO ALA VAL ASN GLY ALA THR GLY HIS SER SER SER
SEQRES 7 A 221 LEU ASP ALA ARG GLU VAL ILE PRO MET ALA ALA VAL LYS
SEQRES 8 A 221 GLN ALA LEU ARG GLU ALA GLY ASP GLU PHE GLU LEU ARG
SEQRES 9 A 221 TYR ARG ARG ALA PHE SER ASP LEU THR SER GLN LEU HIS
SEQRES 10 A 221 ILE THR PRO GLY THR ALA TYR GLN SER PHE GLU GLN VAL
SEQRES 11 A 221 VAL ASN GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY ARG
SEQRES 12 A 221 ILE VAL ALA PHE PHE SER PHE GLY GLY ALA LEU CYS VAL
SEQRES 13 A 221 GLU SER VAL ASP LYS GLU MET GLN VAL LEU VAL SER ARG
SEQRES 14 A 221 ILE ALA ALA TRP MET ALA THR TYR LEU ASN ASP HIS LEU
SEQRES 15 A 221 GLU PRO TRP ILE GLN GLU ASN GLY GLY TRP ASP THR PHE
SEQRES 16 A 221 VAL GLU LEU TYR GLY ASN ASN ALA ALA ALA GLU SER ARG
SEQRES 17 A 221 LYS GLY GLN GLU ARG LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 16 GLY GLN VAL GLY ARG GLN LEU ALA ILE ILE GLY ASP ASP
SEQRES 2 B 16 ILE ASN ARG
HELIX 1 1 GLN A 3 LYS A 20 1 18
HELIX 2 2 SER A 25 PHE A 27 5 3
HELIX 3 3 GLU A 42 ALA A 104 1 23
HELIX 4 4 ALA A 119 LEU A 130 1 12
HELIX 5 5 ARG A 139 LYS A 157 1 19
HELIX 6 6 GLN A 160 ASP A 176 1 17
HELIX 7 7 GLU A 179 ASN A 185 1 7
HELIX 8 8 GLY A 187 LEU A 194 1 8
HELIX 9 9 ALA A 199 ARG A 204 1 6
HELIX 10 10 ARG B 576 ASP B 584 1 9
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
Complete list - 16 20 Bytes