Header list of 1o0l.pdb file
Complete list - t 27 2 Bytes
HEADER APOPTOSIS 22-FEB-03 1O0L
TITLE THE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL RESIDUES IN
TITLE 2 MODULATING BIOLOGICAL ACTIVITY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOPTOSIS REGULATOR BCL-W;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BCL2-LIKE 2 PROTEIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 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: BCL2L2 OR BCLW OR KIAA0271;
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_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX6P-3
KEYWDS APOPTOSIS, BCL-2, HELICAL BUNDLE, BINDING GROOVE, BH3
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.G.HINDS,M.LACKMANN,G.L.SKEA,P.J.HARRISON,D.C.S.HUANG,C.L.DAY
REVDAT 3 27-OCT-21 1O0L 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1O0L 1 VERSN
REVDAT 1 01-APR-03 1O0L 0
JRNL AUTH M.G.HINDS,M.LACKMANN,G.L.SKEA,P.J.HARRISON,D.C.S.HUANG,
JRNL AUTH 2 C.L.DAY
JRNL TITL THE STRUCTURE OF BCL-W REVEALS A ROLE FOR THE C-TERMINAL
JRNL TITL 2 RESIDUES IN MODULATING BIOLOGICAL ACTIVITY
JRNL REF EMBO J. V. 22 1497 2003
JRNL REFN ISSN 0261-4189
JRNL PMID 12660157
JRNL DOI 10.1093/EMBOJ/CDG144
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS 1.1
REMARK 3 AUTHORS : BRUKER A.G. (XWINNMR), BRUNGER ET AL. ACTA
REMARK 3 CRYSTALLOGR. D, 1998, 54, 905-921. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 3871 CONSTRAINTS.
REMARK 3 DISTANCE CONSTRAINTS: 694 INTRARESIDUE; 843 SEQUENTIAL; 912 SHORT
REMARK 3 RANGE; 993 LONG RANGE; 64 HYDROGEN BONDS
REMARK 3 DIHEDRAL ANGLE CONSTRAINTS: 136 PHI CONSTRAINTS; 101 PSI
REMARK 3 CONSTRAINTS; 34 CHI1 CONSTRAINTS; 30 CHI2 CONSTRAINTS
REMARK 4
REMARK 4 1O0L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018424.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.15; 303.15; 303.15
REMARK 210 PH : 6.7; 6.7; 6.7
REMARK 210 IONIC STRENGTH : 120MM; 120MM; 120MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM BCL-W; 1 MM, U-15N BCL-W; 1
REMARK 210 MM, U-13C, 15N, BCL-W
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.3, DYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY TORSION ANGLE
REMARK 210 DYNAMICS SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 256
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS, STRUCTURES WITH THE
REMARK 210 LOWEST ENERGY, TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HETERONUCLEAR 3D NMR.
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 HA LEU A 130 HB2 LEU A 134 1.32
REMARK 500 HH12 ARG A 56 OE2 GLU A 164 1.57
REMARK 500 HZ2 LYS A 21 OE1 GLU A 54 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 -2 -149.77 -122.88
REMARK 500 1 SER A 6 88.65 59.23
REMARK 500 1 PRO A 8 52.38 -69.13
REMARK 500 1 TYR A 27 52.96 -91.20
REMARK 500 1 PRO A 37 -158.07 -93.94
REMARK 500 1 LEU A 42 -32.32 -179.49
REMARK 500 1 THR A 60 -61.02 -120.05
REMARK 500 1 VAL A 70 -60.83 -90.88
REMARK 500 1 THR A 71 145.70 -172.70
REMARK 500 1 PRO A 72 -158.33 -78.11
REMARK 500 1 PRO A 91 41.89 -81.08
REMARK 500 1 ALA A 177 29.29 -79.67
REMARK 500 1 ALA A 182 -168.20 -109.85
REMARK 500 2 PRO A 4 37.18 -82.70
REMARK 500 2 PRO A 37 -159.87 -97.55
REMARK 500 2 PRO A 41 47.03 -80.12
REMARK 500 2 LEU A 42 -31.97 -175.07
REMARK 500 2 ARG A 56 -61.22 -92.92
REMARK 500 2 ARG A 59 46.43 -81.39
REMARK 500 2 VAL A 70 -60.11 -93.01
REMARK 500 2 THR A 71 146.96 -174.69
REMARK 500 2 SER A 74 48.96 -73.81
REMARK 500 2 PRO A 91 38.38 -80.47
REMARK 500 2 LYS A 113 -155.13 -138.27
REMARK 500 2 GLU A 114 53.64 -99.16
REMARK 500 3 LYS A 25 78.43 -153.60
REMARK 500 3 TYR A 27 56.52 -91.85
REMARK 500 3 PRO A 37 -154.63 -94.39
REMARK 500 3 PRO A 41 36.58 -71.36
REMARK 500 3 LEU A 42 -27.78 -167.81
REMARK 500 3 THR A 60 -57.43 -121.33
REMARK 500 3 VAL A 70 -63.47 -91.37
REMARK 500 3 THR A 71 144.47 -172.88
REMARK 500 3 LYS A 113 -151.45 -132.53
REMARK 500 3 GLU A 114 51.09 -108.69
REMARK 500 3 MET A 115 42.24 -146.87
REMARK 500 3 TYR A 151 30.30 -142.35
REMARK 500 4 LEU A -2 92.38 67.84
REMARK 500 4 ASP A 9 -157.58 -90.34
REMARK 500 4 LYS A 25 83.40 -154.56
REMARK 500 4 TYR A 27 54.79 -98.68
REMARK 500 4 PRO A 37 -147.34 -91.33
REMARK 500 4 PRO A 41 48.46 -80.74
REMARK 500 4 LEU A 42 -30.18 -177.27
REMARK 500 4 THR A 60 -70.94 -120.41
REMARK 500 4 VAL A 70 -68.37 -91.86
REMARK 500 4 PRO A 91 39.80 -80.50
REMARK 500 4 LYS A 113 -169.25 -126.90
REMARK 500 5 TYR A 27 51.15 -92.21
REMARK 500 5 PRO A 37 -139.15 -84.54
REMARK 500
REMARK 500 THIS ENTRY HAS 215 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1O0L A 1 183 UNP Q92843 BCLW_HUMAN 1 183
SEQADV 1O0L GLY A -4 UNP Q92843 CLONING ARTIFACT
SEQADV 1O0L PRO A -3 UNP Q92843 CLONING ARTIFACT
SEQADV 1O0L LEU A -2 UNP Q92843 CLONING ARTIFACT
SEQADV 1O0L GLY A -1 UNP Q92843 CLONING ARTIFACT
SEQADV 1O0L SER A 0 UNP Q92843 CLONING ARTIFACT
SEQADV 1O0L GLU A 128 UNP Q92843 ALA 128 ENGINEERED MUTATION
SEQRES 1 A 188 GLY PRO LEU GLY SER MET ALA THR PRO ALA SER ALA PRO
SEQRES 2 A 188 ASP THR ARG ALA LEU VAL ALA ASP PHE VAL GLY TYR LYS
SEQRES 3 A 188 LEU ARG GLN LYS GLY TYR VAL CYS GLY ALA GLY PRO GLY
SEQRES 4 A 188 GLU GLY PRO ALA ALA ASP PRO LEU HIS GLN ALA MET ARG
SEQRES 5 A 188 ALA ALA GLY ASP GLU PHE GLU THR ARG PHE ARG ARG THR
SEQRES 6 A 188 PHE SER ASP LEU ALA ALA GLN LEU HIS VAL THR PRO GLY
SEQRES 7 A 188 SER ALA GLN GLN ARG PHE THR GLN VAL SER ASP GLU LEU
SEQRES 8 A 188 PHE GLN GLY GLY PRO ASN TRP GLY ARG LEU VAL ALA PHE
SEQRES 9 A 188 PHE VAL PHE GLY ALA ALA LEU CYS ALA GLU SER VAL ASN
SEQRES 10 A 188 LYS GLU MET GLU PRO LEU VAL GLY GLN VAL GLN GLU TRP
SEQRES 11 A 188 MET VAL GLU TYR LEU GLU THR ARG LEU ALA ASP TRP ILE
SEQRES 12 A 188 HIS SER SER GLY GLY TRP ALA GLU PHE THR ALA LEU TYR
SEQRES 13 A 188 GLY ASP GLY ALA LEU GLU GLU ALA ARG ARG LEU ARG GLU
SEQRES 14 A 188 GLY ASN TRP ALA SER VAL ARG THR VAL LEU THR GLY ALA
SEQRES 15 A 188 VAL ALA LEU GLY ALA LEU
HELIX 1 1 ASP A 9 LYS A 25 1 17
HELIX 2 2 GLY A 32 GLY A 36 5 5
HELIX 3 3 LEU A 42 PHE A 57 1 16
HELIX 4 4 THR A 60 LEU A 68 1 9
HELIX 5 5 ALA A 75 PHE A 87 1 13
HELIX 6 6 ASN A 92 ASN A 112 1 21
HELIX 7 7 MET A 115 ARG A 133 1 19
HELIX 8 8 ARG A 133 GLY A 142 1 10
HELIX 9 9 GLY A 143 TYR A 151 1 9
HELIX 10 10 LEU A 156 ARG A 171 1 16
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