Header list of 1f95.pdb file
Complete list - 25 20 Bytes
HEADER CONTRACTILE PROTEIN/PEPTIDE 07-JUL-00 1F95
TITLE SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DYNEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: 8KDA LIGHT CHAIN;
COMPND 5 SYNONYM: PROTEIN INHIBITOR OF NEURONAL NITRIC OXIDE SYNTHASE, DLC8;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: BCL2-LIKE 11 (APOPTOSIS FACILITATOR);
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: DLC8 BINDING REGION;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET14B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THIS
SOURCE 12 SEQUENCE OCCURS NATURALLY IN HUMANS (HOMO SAPIENS)
KEYWDS DYNEIN, LIGHT CHAIN, DLC8, BIM, APOPTOSIS, CONTRACTILE PROTEIN-
KEYWDS 2 PEPTIDE COMPLEX
EXPDTA SOLUTION NMR
AUTHOR J.-S.FAN,Q.ZHANG,H.TOCHIO,M.LI,M.ZHANG
REVDAT 4 13-JUL-11 1F95 1 VERSN
REVDAT 3 24-FEB-09 1F95 1 VERSN
REVDAT 2 01-APR-03 1F95 1 JRNL
REVDAT 1 28-FEB-01 1F95 0
JRNL AUTH J.FAN,Q.ZHANG,H.TOCHIO,M.LI,M.ZHANG
JRNL TITL STRUCTURAL BASIS OF DIVERSE SEQUENCE-DEPENDENT TARGET
JRNL TITL 2 RECOGNITION BY THE 8 KDA DYNEIN LIGHT CHAIN.
JRNL REF J.MOL.BIOL. V. 306 97 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11178896
JRNL DOI 10.1006/JMBI.2000.4374
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,
REMARK 3 JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F95 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-AUG-00.
REMARK 100 THE RCSB ID CODE IS RCSB011396.
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 : 100MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM DLC8/BIM PEPTIDE COMPLEX
REMARK 210 15N; 100MM PHOSPHATE BUFFER; 10MM
REMARK 210 DTT; 90% H2O AND 10% D2O; 1.5MM
REMARK 210 DLC8/BIM PEPTIDE COMPLEX 15N,13C;
REMARK 210 100MM PHOSPHATE BUFFER; 10MM DTT;
REMARK 210 90% H2O AND 10% D2O; 1.5MM DLC8/
REMARK 210 BIM PEPTIDE COMPLEX ; 100MM
REMARK 210 PHOSPHATE BUFFER; 10MM DTT; 99.9%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, NMRPIPE 1.7, X-PLOR
REMARK 210 3.8
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: TETRAMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
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 THR A 70 HD1 HIS A 72 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 ASP A 3 -138.71 43.23
REMARK 500 ASP A 12 70.07 -150.07
REMARK 500 ASN A 33 32.22 -94.37
REMARK 500 ASN A 51 141.02 84.33
REMARK 500 ASN A 61 134.47 -171.16
REMARK 500 PHE A 62 -170.98 179.20
REMARK 500 GLU A 69 -122.79 -85.28
REMARK 500 GLN A 80 -26.80 82.68
REMARK 500 PHE A 86 140.38 -177.11
REMARK 500 SER A 88 43.45 -154.62
REMARK 500 CYS B 2 46.01 -177.92
REMARK 500 ARG B 4 130.12 -177.02
REMARK 500 VAL B 7 66.53 -156.82
REMARK 500 ASN B 10 144.42 -174.84
REMARK 500 ASN B 51 139.94 78.46
REMARK 500 PHE B 62 144.79 178.35
REMARK 500 HIS B 68 -169.85 -128.93
REMARK 500 GLU B 69 -125.65 -81.95
REMARK 500 GLN B 80 42.73 -90.37
REMARK 500 PHE B 86 141.95 -178.50
REMARK 500 SER B 88 44.78 -153.31
REMARK 500 CYS C 3 145.60 174.73
REMARK 500 SER D 2 112.56 -169.09
REMARK 500 CYS D 3 127.50 -170.59
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN C OF BCL2-LIKE 11
REMARK 800 (APOPTOSIS FACILITATOR)
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN D OF BCL2-LIKE 11
REMARK 800 (APOPTOSIS FACILITATOR)
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F3C RELATED DB: PDB
REMARK 900 THIS IS A SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8)
REMARK 900 COMPLEXED WITH ONE TARGET, BIM.
DBREF 1F95 A 1 89 UNP P63170 DYL1_RAT 1 89
DBREF 1F95 B 1 89 UNP P63170 DYL1_RAT 1 89
DBREF 1F95 C 1 9 UNP O43521 B2L11_HUMAN 108 116
DBREF 1F95 D 1 9 UNP O43521 B2L11_HUMAN 108 116
SEQRES 1 A 89 MET CYS ASP ARG LYS ALA VAL ILE LYS ASN ALA ASP MET
SEQRES 2 A 89 SER GLU GLU MET GLN GLN ASP SER VAL GLU CYS ALA THR
SEQRES 3 A 89 GLN ALA LEU GLU LYS TYR ASN ILE GLU LYS ASP ILE ALA
SEQRES 4 A 89 ALA HIS ILE LYS LYS GLU PHE ASP LYS LYS TYR ASN PRO
SEQRES 5 A 89 THR TRP HIS CYS ILE VAL GLY ARG ASN PHE GLY SER TYR
SEQRES 6 A 89 VAL THR HIS GLU THR LYS HIS PHE ILE TYR PHE TYR LEU
SEQRES 7 A 89 GLY GLN VAL ALA ILE LEU LEU PHE LYS SER GLY
SEQRES 1 B 89 MET CYS ASP ARG LYS ALA VAL ILE LYS ASN ALA ASP MET
SEQRES 2 B 89 SER GLU GLU MET GLN GLN ASP SER VAL GLU CYS ALA THR
SEQRES 3 B 89 GLN ALA LEU GLU LYS TYR ASN ILE GLU LYS ASP ILE ALA
SEQRES 4 B 89 ALA HIS ILE LYS LYS GLU PHE ASP LYS LYS TYR ASN PRO
SEQRES 5 B 89 THR TRP HIS CYS ILE VAL GLY ARG ASN PHE GLY SER TYR
SEQRES 6 B 89 VAL THR HIS GLU THR LYS HIS PHE ILE TYR PHE TYR LEU
SEQRES 7 B 89 GLY GLN VAL ALA ILE LEU LEU PHE LYS SER GLY
SEQRES 1 C 9 MET SER CYS ASP LYS SER THR GLN THR
SEQRES 1 D 9 MET SER CYS ASP LYS SER THR GLN THR
HELIX 1 1 SER A 14 TYR A 32 1 19
HELIX 2 2 ILE A 34 TYR A 50 1 17
HELIX 3 3 SER B 14 TYR B 32 1 19
HELIX 4 4 ILE B 34 TYR B 50 1 17
SHEET 1 A 5 ALA A 6 MET A 13 0
SHEET 2 A 5 HIS A 72 LEU A 78 -1 O PHE A 73 N ASP A 12
SHEET 3 A 5 VAL A 81 LYS A 87 -1 O VAL A 81 N LEU A 78
SHEET 4 A 5 TRP A 54 VAL A 66 -1 N HIS A 55 O PHE A 86
SHEET 5 A 5 LYS C 5 GLN C 8 -1 N LYS C 5 O VAL A 66
SHEET 6 A 5 TRP A 54 VAL A 66 0
SHEET 7 A 5 TRP B 54 HIS B 68 -1 N CYS B 56 O TYR A 65
SHEET 8 A 5 VAL B 81 LYS B 87 -1 N ALA B 82 O GLY B 59
SHEET 9 A 5 HIS B 72 LEU B 78 -1 O HIS B 72 N LYS B 87
SHEET 10 A 5 ALA B 6 MET B 13 -1 O VAL B 7 N TYR B 77
SHEET 11 A 5 TRP A 54 VAL A 66 0
SHEET 12 A 5 LYS C 5 GLN C 8 -1 N LYS C 5 O VAL A 66
SHEET 13 A 5 TRP B 54 HIS B 68 0
SHEET 14 A 5 CYS D 3 GLN D 8 -1 O CYS D 3 N HIS B 68
CISPEP 1 PRO A 52 THR A 53 0 0.80
CISPEP 2 PRO B 52 THR B 53 0 0.54
SITE 1 AC1 16 ASN A 61 PHE A 62 GLY A 63 SER A 64
SITE 2 AC1 16 TYR A 65 VAL A 66 THR A 67 HIS A 68
SITE 3 AC1 16 GLU A 69 THR A 70 PHE A 73 TYR A 75
SITE 4 AC1 16 TYR A 77 ALA A 82 LEU A 84 LYS B 36
SITE 1 AC2 18 ILE A 34 GLU A 35 LYS A 36 ASN B 10
SITE 2 AC2 18 GLY B 59 ASN B 61 PHE B 62 GLY B 63
SITE 3 AC2 18 SER B 64 TYR B 65 VAL B 66 THR B 67
SITE 4 AC2 18 HIS B 68 GLU B 69 THR B 70 TYR B 75
SITE 5 AC2 18 ALA B 82 LEU B 84
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 - 25 20 Bytes