Header list of 1f96.pdb file
Complete list - b 23 2 Bytes
HEADER INHIBITOR/OXIDOREDUCTASE 07-JUL-00 1F96
TITLE SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND NNOS PEPTIDE
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DYNEIN LIGHT CHAIN 8;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DLC8 BINDING REGION;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PROTEIN (NNOS, NEURONAL NITRIC OXIDE SYNTHASE);
COMPND 8 CHAIN: C, D;
COMPND 9 FRAGMENT: DLC8-BINDING DOMAIN OF NNOS;
COMPND 10 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_VECTOR: PET14B;
SOURCE 9 MOL_ID: 2;
SOURCE 10 SYNTHETIC: YES;
SOURCE 11 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.
KEYWDS DYNEIN, LIGHT CHAIN, DLC8, NNOS, INHIBITOR-OXIDOREDUCTASE COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.S.FAN,Q.ZHANG,H.TOCHIO,M.LI,M.ZHANG
REVDAT 4 23-FEB-22 1F96 1 REMARK
REVDAT 3 24-FEB-09 1F96 1 VERSN
REVDAT 2 01-APR-03 1F96 1 JRNL
REVDAT 1 28-FEB-01 1F96 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 : VNMR 6.1B, CNS 1.0
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER, A (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1F96 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000011397.
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/NNOS PPETIDE COMPLEX
REMARK 210 15N; 100MM PHOSPHATE BUFFER;
REMARK 210 10MM DTT; 90%H2O AND 10% D2O;
REMARK 210 1.5MM DLC8/NNOS PPETIDE COMPLEX
REMARK 210 15N,13C; 100MM PHOSPHATE BUFFER;
REMARK 210 10MM DTT; 90%H2O AND 10% D2O;
REMARK 210 1.5MM DLC8/NNOS PPETIDE COMPLEX ;
REMARK 210 100MM PHOSPHATE BUFFER; 10MM
REMARK 210 DTT; 99.9% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_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 : NMRPIPE 1.7, X-PLOR 3.8
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ASP C 9 CA
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
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 CYS A 2 -44.63 -178.85
REMARK 500 1 ARG A 4 134.91 -170.22
REMARK 500 1 LYS A 5 -80.39 -62.73
REMARK 500 1 ALA A 6 120.72 60.48
REMARK 500 1 LYS A 9 -44.93 -137.33
REMARK 500 1 ASP A 12 52.48 -161.55
REMARK 500 1 ASN A 51 138.26 96.63
REMARK 500 1 ARG A 60 37.56 -178.35
REMARK 500 1 ASN A 61 79.39 170.62
REMARK 500 1 LEU A 78 145.29 -170.24
REMARK 500 1 PHE A 86 127.50 -175.15
REMARK 500 1 LYS B 5 -134.32 -73.02
REMARK 500 1 ALA B 6 127.14 63.73
REMARK 500 1 LYS B 9 -41.23 -137.73
REMARK 500 1 ASP B 12 62.59 -178.71
REMARK 500 1 ASN B 51 141.21 88.83
REMARK 500 1 ARG B 60 28.70 -160.48
REMARK 500 1 ASN B 61 82.34 167.33
REMARK 500 1 HIS B 72 69.55 -164.82
REMARK 500 1 PHE B 86 129.74 -177.40
REMARK 500 1 GLN C 7 69.48 -163.52
REMARK 500 1 HIS C 17 133.23 67.85
REMARK 500 1 GLN D 7 74.97 -159.14
REMARK 500 1 ASP D 9 43.07 -178.93
REMARK 500 1 ASP D 11 48.81 -86.50
REMARK 500 1 SER D 16 -133.63 -67.57
REMARK 500 1 HIS D 17 131.25 -172.58
REMARK 500 2 CYS A 2 145.06 -176.42
REMARK 500 2 ARG A 4 48.45 -79.71
REMARK 500 2 ASN A 10 59.73 -155.03
REMARK 500 2 ASP A 12 52.28 -175.47
REMARK 500 2 TYR A 32 -45.64 -145.51
REMARK 500 2 ASN A 51 143.73 93.62
REMARK 500 2 ARG A 60 35.15 -174.19
REMARK 500 2 ASN A 61 81.43 165.46
REMARK 500 2 HIS A 72 54.77 -150.25
REMARK 500 2 GLN A 80 37.11 178.90
REMARK 500 2 PHE A 86 131.57 -179.57
REMARK 500 2 CYS B 2 134.21 62.72
REMARK 500 2 ARG B 4 130.87 -176.64
REMARK 500 2 LYS B 5 -126.46 -166.33
REMARK 500 2 ALA B 6 132.27 62.30
REMARK 500 2 LYS B 9 -42.83 -139.55
REMARK 500 2 ASN B 10 51.61 -115.62
REMARK 500 2 ASP B 12 53.08 -153.00
REMARK 500 2 MET B 13 -174.67 -176.54
REMARK 500 2 TYR B 32 -43.98 -145.04
REMARK 500 2 ASN B 33 54.02 70.48
REMARK 500 2 LYS B 49 -70.19 -84.29
REMARK 500 2 ASN B 51 141.82 96.56
REMARK 500
REMARK 500 THIS ENTRY HAS 665 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F3C RELATED DB: PDB
REMARK 900 THIS IS A SOLUTION STRUCTURE OF DLC8 COMPLEXED WITH ITS BINDING
REMARK 900 TARGET, NNOS
DBREF 1F96 A 1 89 UNP P63170 DYL1_RAT 1 89
DBREF 1F96 B 1 89 UNP P63170 DYL1_RAT 1 89
DBREF 1F96 C 1 18 PDB 1F96 1F96 1 18
DBREF 1F96 D 1 18 PDB 1F96 1F96 1 18
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 18 MET LYS ASP THR GLY ILE GLN VAL ASP ARG ASP LEU ASP
SEQRES 2 C 18 GLY LYS SER HIS LYS
SEQRES 1 D 18 MET LYS ASP THR GLY ILE GLN VAL ASP ARG ASP LEU ASP
SEQRES 2 D 18 GLY LYS SER HIS LYS
HELIX 1 1 SER A 14 TYR A 32 1 19
HELIX 2 2 ILE A 34 ASN A 51 1 18
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 6 VAL A 7 ILE A 8 0
SHEET 2 A 6 ILE A 74 LEU A 78 -1 O TYR A 77 N VAL A 7
SHEET 3 A 6 VAL A 81 LYS A 87 -1 O VAL A 81 N LEU A 78
SHEET 4 A 6 TRP A 54 GLY A 59 -1 N HIS A 55 O PHE A 86
SHEET 5 A 6 PHE B 62 HIS B 68 -1 N GLY B 63 O VAL A 58
SHEET 6 A 6 LYS D 2 VAL D 8 -1 N LYS D 2 O HIS B 68
SHEET 1 B 6 VAL B 7 ILE B 8 0
SHEET 2 B 6 ILE B 74 LEU B 78 -1 O TYR B 77 N VAL B 7
SHEET 3 B 6 VAL B 81 LYS B 87 -1 O VAL B 81 N LEU B 78
SHEET 4 B 6 TRP B 54 GLY B 59 -1 N HIS B 55 O PHE B 86
SHEET 5 B 6 ASN A 61 VAL A 66 -1 O GLY A 63 N VAL B 58
SHEET 6 B 6 THR C 4 ASP C 9 -1 N THR C 4 O VAL A 66
CISPEP 1 PRO A 52 THR A 53 1 0.39
CISPEP 2 PRO B 52 THR B 53 1 0.39
CISPEP 3 PRO A 52 THR A 53 2 0.29
CISPEP 4 PRO B 52 THR B 53 2 0.55
CISPEP 5 PRO A 52 THR A 53 3 0.38
CISPEP 6 PRO B 52 THR B 53 3 0.00
CISPEP 7 PRO A 52 THR A 53 4 0.26
CISPEP 8 PRO B 52 THR B 53 4 0.23
CISPEP 9 PRO A 52 THR A 53 5 0.07
CISPEP 10 PRO B 52 THR B 53 5 0.19
CISPEP 11 PRO A 52 THR A 53 6 0.30
CISPEP 12 PRO B 52 THR B 53 6 0.38
CISPEP 13 PRO A 52 THR A 53 7 0.13
CISPEP 14 PRO B 52 THR B 53 7 0.41
CISPEP 15 PRO A 52 THR A 53 8 0.14
CISPEP 16 PRO B 52 THR B 53 8 0.05
CISPEP 17 PRO A 52 THR A 53 9 0.17
CISPEP 18 PRO B 52 THR B 53 9 0.41
CISPEP 19 PRO A 52 THR A 53 10 -0.09
CISPEP 20 PRO B 52 THR B 53 10 0.07
CISPEP 21 PRO A 52 THR A 53 11 0.05
CISPEP 22 PRO B 52 THR B 53 11 0.15
CISPEP 23 PRO A 52 THR A 53 12 0.14
CISPEP 24 PRO B 52 THR B 53 12 0.32
CISPEP 25 PRO A 52 THR A 53 13 0.05
CISPEP 26 PRO B 52 THR B 53 13 0.27
CISPEP 27 PRO A 52 THR A 53 14 0.06
CISPEP 28 PRO B 52 THR B 53 14 0.44
CISPEP 29 PRO A 52 THR A 53 15 0.18
CISPEP 30 PRO B 52 THR B 53 15 0.01
CISPEP 31 PRO A 52 THR A 53 16 0.23
CISPEP 32 PRO B 52 THR B 53 16 0.35
CISPEP 33 PRO A 52 THR A 53 17 0.04
CISPEP 34 PRO B 52 THR B 53 17 -0.13
CISPEP 35 PRO A 52 THR A 53 18 0.00
CISPEP 36 PRO B 52 THR B 53 18 0.18
CISPEP 37 PRO A 52 THR A 53 19 0.20
CISPEP 38 PRO B 52 THR B 53 19 0.37
CISPEP 39 PRO A 52 THR A 53 20 0.12
CISPEP 40 PRO B 52 THR B 53 20 0.14
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 23 2 Bytes