Header list of 1f16.pdb file
Complete list - b 16 2 Bytes
HEADER APOPTOSIS 18-MAY-00 1F16
TITLE SOLUTION STRUCTURE OF A PRO-APOPTOTIC PROTEIN BAX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (APOPTOSIS REGULATOR BAX, MEMBRANE ISOFORM ALPHA);
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
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
KEYWDS HELICAL PROTEIN, APOPTOSIS
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.SUZUKI,R.J.YOULE,N.TJANDRA
REVDAT 3 16-FEB-22 1F16 1 REMARK
REVDAT 2 24-FEB-09 1F16 1 VERSN
REVDAT 1 22-NOV-00 1F16 0
JRNL AUTH M.SUZUKI,R.J.YOULE,N.TJANDRA
JRNL TITL STRUCTURE OF BAX: COREGULATION OF DIMER FORMATION AND
JRNL TITL 2 INTRACELLULAR LOCALIZATION.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 103 645 2000
JRNL REFN ISSN 0092-8674
JRNL PMID 11106734
JRNL DOI 10.1016/S0092-8674(00)00167-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.840
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS BASED ON 2426 NOE
REMARK 3 RESTRAINTS, 123 DIHEDRAL, 178 HYDROGEN BONDS, 575 DIPOLAR
REMARK 3 COUPLING RESTRAINTS.
REMARK 4
REMARK 4 1F16 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011117.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305.00
REMARK 210 PH : 6.00
REMARK 210 IONIC STRENGTH : 10 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM BAX U-15N,13C; 10MM TRIS
REMARK 210 -ACETATE PH 6.0 2MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 4D_13C/15N-SEPARATED_ NOESY;
REMARK 210 4D_13C-SEPARATED_ NOESY; 3D_15N-
REMARK 210 SEPARATED_ NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7 REV 1999.039.11.31,
REMARK 210 PIPP 4.1.5, UXNMR 2.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY. EXPERIMENTAL DIPOLAR COUPLING RESTRAINTS WERE USED
REMARK 210 IN STRUCTURE DETERMINATION.
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 HD21 ASN A 104 H PHE A 105 1.24
REMARK 500 O GLY A 40 H ALA A 42 1.56
REMARK 500 O LYS A 119 H LYS A 123 1.56
REMARK 500 O TYR A 115 HG SER A 118 1.58
REMARK 500 O VAL A 177 H LEU A 181 1.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 17 THR A 127 CA - CB - CG2 ANGL. DEV. = -8.4 DEGREES
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 ASP A 2 63.40 -169.63
REMARK 500 1 GLU A 6 -71.35 -167.63
REMARK 500 1 PRO A 13 174.53 -59.25
REMARK 500 1 SER A 16 -2.01 -52.08
REMARK 500 1 ARG A 37 -94.57 -83.33
REMARK 500 1 GLU A 41 -41.83 66.86
REMARK 500 1 ALA A 42 74.25 31.21
REMARK 500 1 GLU A 44 -102.09 -74.56
REMARK 500 1 LEU A 45 74.13 -67.05
REMARK 500 1 ALA A 46 -83.69 -69.82
REMARK 500 1 LEU A 47 80.21 -68.16
REMARK 500 1 PRO A 49 -170.25 -59.39
REMARK 500 1 GLN A 52 98.99 -172.66
REMARK 500 1 ASP A 53 122.52 164.07
REMARK 500 1 VAL A 83 -127.16 -82.63
REMARK 500 1 ASP A 84 168.21 159.51
REMARK 500 1 THR A 85 -86.06 -92.38
REMARK 500 1 ASP A 86 -67.96 59.46
REMARK 500 1 ASN A 104 -49.09 -162.87
REMARK 500 1 ASN A 106 -141.95 -140.68
REMARK 500 1 LYS A 128 38.45 74.02
REMARK 500 1 MET A 137 -26.36 -38.33
REMARK 500 1 LEU A 148 34.86 -83.09
REMARK 500 1 TRP A 158 -6.16 -56.11
REMARK 500 1 PHE A 165 -119.12 -62.57
REMARK 500 1 TRP A 188 -16.73 -39.79
REMARK 500 1 LYS A 189 -72.36 -42.00
REMARK 500 1 LYS A 190 -54.73 -153.81
REMARK 500 1 MET A 191 -72.55 178.47
REMARK 500 2 SER A 4 99.90 52.24
REMARK 500 2 GLU A 6 -59.35 -170.41
REMARK 500 2 PRO A 8 103.64 -59.43
REMARK 500 2 THR A 14 41.08 -84.86
REMARK 500 2 PRO A 43 75.65 -59.03
REMARK 500 2 GLU A 44 -67.85 -172.17
REMARK 500 2 LEU A 45 46.72 -78.46
REMARK 500 2 ALA A 46 75.47 -69.09
REMARK 500 2 LEU A 47 35.16 -167.89
REMARK 500 2 ASP A 48 74.17 -155.65
REMARK 500 2 PRO A 49 53.23 -66.89
REMARK 500 2 PRO A 51 -70.84 -61.57
REMARK 500 2 GLN A 52 134.17 -173.82
REMARK 500 2 SER A 72 -109.85 -57.76
REMARK 500 2 ASN A 73 113.70 -11.42
REMARK 500 2 ASP A 86 -45.96 -174.20
REMARK 500 2 SER A 87 88.41 -155.84
REMARK 500 2 SER A 101 -79.07 33.16
REMARK 500 2 ASN A 104 -86.00 58.41
REMARK 500 2 TRP A 107 -48.93 -138.72
REMARK 500 2 LYS A 128 42.23 70.11
REMARK 500
REMARK 500 THIS ENTRY HAS 516 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1F16 A 1 192 UNP Q07812 BAXA_HUMAN 1 192
SEQRES 1 A 192 MET ASP GLY SER GLY GLU GLN PRO ARG GLY GLY GLY PRO
SEQRES 2 A 192 THR SER SER GLU GLN ILE MET LYS THR GLY ALA LEU LEU
SEQRES 3 A 192 LEU GLN GLY PHE ILE GLN ASP ARG ALA GLY ARG MET GLY
SEQRES 4 A 192 GLY GLU ALA PRO GLU LEU ALA LEU ASP PRO VAL PRO GLN
SEQRES 5 A 192 ASP ALA SER THR LYS LYS LEU SER GLU CYS LEU LYS ARG
SEQRES 6 A 192 ILE GLY ASP GLU LEU ASP SER ASN MET GLU LEU GLN ARG
SEQRES 7 A 192 MET ILE ALA ALA VAL ASP THR ASP SER PRO ARG GLU VAL
SEQRES 8 A 192 PHE PHE ARG VAL ALA ALA ASP MET PHE SER ASP GLY ASN
SEQRES 9 A 192 PHE ASN TRP GLY ARG VAL VAL ALA LEU PHE TYR PHE ALA
SEQRES 10 A 192 SER LYS LEU VAL LEU LYS ALA LEU CYS THR LYS VAL PRO
SEQRES 11 A 192 GLU LEU ILE ARG THR ILE MET GLY TRP THR LEU ASP PHE
SEQRES 12 A 192 LEU ARG GLU ARG LEU LEU GLY TRP ILE GLN ASP GLN GLY
SEQRES 13 A 192 GLY TRP ASP GLY LEU LEU SER TYR PHE GLY THR PRO THR
SEQRES 14 A 192 TRP GLN THR VAL THR ILE PHE VAL ALA GLY VAL LEU THR
SEQRES 15 A 192 ALA SER LEU THR ILE TRP LYS LYS MET GLY
HELIX 1 1 SER A 15 GLY A 36 1 22
HELIX 2 2 ASP A 53 SER A 72 1 20
HELIX 3 3 ASN A 73 ALA A 81 1 9
HELIX 4 4 SER A 87 PHE A 100 1 14
HELIX 5 5 TRP A 107 LYS A 128 1 22
HELIX 6 6 VAL A 129 ARG A 147 1 19
HELIX 7 7 LEU A 149 GLN A 155 1 7
HELIX 8 8 TRP A 158 PHE A 165 1 8
HELIX 9 9 TRP A 170 LYS A 189 1 20
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