Header list of 1g5j.pdb file
Complete list - 27 20 Bytes
HEADER APOPTOSIS 01-NOV-00 1G5J
TITLE COMPLEX OF BCL-XL WITH PEPTIDE FROM BAD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-X;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-209;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: BAD PROTEIN;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: RESIDUES 140-164;
COMPND 10 ENGINEERED: YES;
COMPND 11 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: BCLX;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 OTHER_DETAILS: THE BAD PEPTIDE WAS CHEMICALLY SYNTHESIZED.
KEYWDS COMPLEX, APOPTOSIS
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR A.M.PETROS,D.G.NETTESHEIM,Y.WANG,E.T.OLEJNICZAK,R.P.MEADOWS,J.MACK,
AUTHOR 2 K.SWIFT,E.D.MATAYOSHI,H.ZHANG,C.B.THOMPSON,S.W.FESIK
REVDAT 4 27-OCT-21 1G5J 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1G5J 1 VERSN
REVDAT 2 01-APR-03 1G5J 1 JRNL
REVDAT 1 07-FEB-01 1G5J 0
JRNL AUTH A.M.PETROS,D.G.NETTESHEIM,Y.WANG,E.T.OLEJNICZAK,R.P.MEADOWS,
JRNL AUTH 2 J.MACK,K.SWIFT,E.D.MATAYOSHI,H.ZHANG,C.B.THOMPSON,S.W.FESIK
JRNL TITL RATIONALE FOR BCL-XL/BAD PEPTIDE COMPLEX FORMATION FROM
JRNL TITL 2 STRUCTURE, MUTAGENESIS, AND BIOPHYSICAL STUDIES.
JRNL REF PROTEIN SCI. V. 9 2528 2000
JRNL REFN ISSN 0961-8368
JRNL PMID 11206074
JRNL DOI 10.1017/S096183680000331X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER, A.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1G5J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-NOV-00.
REMARK 100 THE DEPOSITION ID IS D_1000012259.
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 : 40 MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 15N-BCL-XL/UNLABELED BAD
REMARK 210 PEPTIDE; 15N,13C-BCL-XL/
REMARK 210 UNLABELLED BAD PEPTIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
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: 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: 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 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 32 -87.16 -114.47
REMARK 500 ASP A 33 42.73 169.48
REMARK 500 VAL A 34 83.14 -61.73
REMARK 500 GLU A 35 -74.59 -48.21
REMARK 500 GLU A 36 -178.30 -178.87
REMARK 500 ASN A 37 168.34 -48.36
REMARK 500 ARG A 38 100.55 67.87
REMARK 500 GLU A 40 155.32 61.37
REMARK 500 ALA A 41 107.26 165.98
REMARK 500 THR A 45 37.55 -169.28
REMARK 500 PHE A 109 52.34 -90.12
REMARK 500 SER A 110 -158.73 -116.61
REMARK 500 PRO A 120 106.12 -52.22
REMARK 500 ARG A 136 -75.39 -47.76
REMARK 500 ASP A 137 75.91 -115.62
REMARK 500 VAL A 139 -80.38 -130.76
REMARK 500 ASN A 140 160.23 57.60
REMARK 500 VAL A 167 -79.12 -52.96
REMARK 500 HIS A 181 -76.19 -104.11
REMARK 500 LEU A 182 77.56 -67.38
REMARK 500 GLU A 183 -69.23 -132.37
REMARK 500 ARG A 213 -61.47 75.47
REMARK 500 LEU A 214 -67.46 76.94
REMARK 500 ALA B 304 -106.75 -56.31
REMARK 500 ALA B 305 -72.79 3.04
REMARK 500 ASP B 321 -37.91 178.41
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BXL RELATED DB: PDB
REMARK 900 STRUCTURE OF BCL-XL/BAK PEPTIDE COMPLEX, NMR, MINIMIZED AVERAGE
REMARK 900 STRUCTURE
REMARK 900 RELATED ID: 1G5M RELATED DB: PDB
REMARK 900 HUMAN BCL-2, ISOFORM 1
REMARK 900 RELATED ID: 1G5O RELATED DB: PDB
REMARK 900 HUMAN BCL-2, ISOFORM 2
DBREF 1G5J A 5 48 UNP Q07817 BCLX_HUMAN 1 44
DBREF 1G5J A 89 213 UNP Q07817 BCLX_HUMAN 85 209
DBREF 1G5J B 301 325 UNP Q92934 BAD_HUMAN 140 164
SEQADV 1G5J MET A 1 UNP Q07817 CLONING ARTIFACT
SEQADV 1G5J SER A 2 UNP Q07817 CLONING ARTIFACT
SEQADV 1G5J MET A 3 UNP Q07817 CLONING ARTIFACT
SEQADV 1G5J ALA A 4 UNP Q07817 CLONING ARTIFACT
SEQADV 1G5J LEU A 214 UNP Q07817 CLONING ARTIFACT
SEQADV 1G5J GLU A 215 UNP Q07817 CLONING ARTIFACT
SEQADV 1G5J VAL B 320 UNP Q07817 GLU 159 ENGINEERED MUTATION
SEQADV 1G5J ASP B 321 UNP Q07817 GLY 160 ENGINEERED MUTATION
SEQADV 1G5J LYS B 325 UNP Q07817 GLY 164 ENGINEERED MUTATION
SEQRES 1 A 175 MET SER MET ALA MET SER GLN SER ASN ARG GLU LEU VAL
SEQRES 2 A 175 VAL ASP PHE LEU SER TYR LYS LEU SER GLN LYS GLY TYR
SEQRES 3 A 175 SER TRP SER GLN PHE SER ASP VAL GLU GLU ASN ARG THR
SEQRES 4 A 175 GLU ALA PRO GLU GLY THR GLU SER GLU ALA VAL LYS GLN
SEQRES 5 A 175 ALA LEU ARG GLU ALA GLY ASP GLU PHE GLU LEU ARG TYR
SEQRES 6 A 175 ARG ARG ALA PHE SER ASP LEU THR SER GLN LEU HIS ILE
SEQRES 7 A 175 THR PRO GLY THR ALA TYR GLN SER PHE GLU GLN VAL VAL
SEQRES 8 A 175 ASN GLU LEU PHE ARG ASP GLY VAL ASN TRP GLY ARG ILE
SEQRES 9 A 175 VAL ALA PHE PHE SER PHE GLY GLY ALA LEU CYS VAL GLU
SEQRES 10 A 175 SER VAL ASP LYS GLU MET GLN VAL LEU VAL SER ARG ILE
SEQRES 11 A 175 ALA ALA TRP MET ALA THR TYR LEU ASN ASP HIS LEU GLU
SEQRES 12 A 175 PRO TRP ILE GLN GLU ASN GLY GLY TRP ASP THR PHE VAL
SEQRES 13 A 175 GLU LEU TYR GLY ASN ASN ALA ALA ALA GLU SER ARG LYS
SEQRES 14 A 175 GLY GLN GLU ARG LEU GLU
SEQRES 1 B 25 ASN LEU TRP ALA ALA GLN ARG TYR GLY ARG GLU LEU ARG
SEQRES 2 B 25 ARG MET SER ASP GLU PHE VAL ASP SER PHE LYS LYS
HELIX 1 1 SER A 2 ALA A 4 5 3
HELIX 2 2 MET A 5 GLY A 25 1 21
HELIX 3 3 SER A 27 PHE A 31 5 5
HELIX 4 4 THR A 45 TYR A 105 1 21
HELIX 5 5 ARG A 106 SER A 110 5 5
HELIX 6 6 THR A 122 ARG A 136 1 15
HELIX 7 7 VAL A 139 LYS A 161 1 23
HELIX 8 8 GLN A 164 HIS A 181 1 18
HELIX 9 9 GLU A 183 GLY A 190 1 8
HELIX 10 10 GLY A 190 GLY A 200 1 11
HELIX 11 11 GLY A 200 GLU A 212 1 13
HELIX 12 12 TRP B 303 VAL B 320 1 18
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 - 27 20 Bytes