Header list of 1ss6.pdb file
Complete list - r 2 2 Bytes
HEADER SIGNALING PROTEIN 23-MAR-04 1SS6
TITLE SOLUTION STRUCTURE OF SEP DOMAIN FROM HUMAN P47
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NSFL1 COFACTOR P47;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEP DOMAIN;
COMPND 5 SYNONYM: P47; P47 PROTEIN ISOFORM A; P47 PROTEIN; P97 COFACTOR P47;
COMPND 6 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 NMR; P47; SEP, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.SOUKENIK,M.LEIDERT,V.SIEVERT,K.BUESSOW,D.LEITNER,D.LABUDDE,
AUTHOR 2 L.J.BALL,H.OSCHKINAT
REVDAT 3 02-MAR-22 1SS6 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1SS6 1 VERSN
REVDAT 1 09-NOV-04 1SS6 0
JRNL AUTH M.SOUKENIK,A.DIEHL,M.LEIDERT,V.SIEVERT,K.BUESSOW,D.LEITNER,
JRNL AUTH 2 D.LABUDDE,L.J.BALL,A.LECHNER,D.K.NAGLER,H.OSCHKINAT
JRNL TITL THE SEP DOMAIN OF P47 ACTS AS A REVERSIBLE COMPETITIVE
JRNL TITL 2 INHIBITOR OF CATHEPSIN L
JRNL REF FEBS LETT. V. 576 358 2004
JRNL REFN ISSN 0014-5793
JRNL PMID 15498563
JRNL DOI 10.1016/J.FEBSLET.2004.09.037
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, ARIA/CNS 1.2
REMARK 3 AUTHORS : BRUKER (XWINNMR), NILGES. M. (ARIA/CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SS6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000021957.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300; 300
REMARK 210 PH : 5.6; 5.6; 5.6
REMARK 210 IONIC STRENGTH : 20MM PHOSPHATE BUFFER NA, 150MM
REMARK 210 SODIUM CHLORIDE; 20MM PHOSPHATE
REMARK 210 BUFFER NA, 150MM SODIUM CHLORIDE;
REMARK 210 20MM PHOSPHATE BUFFER NA, 150MM
REMARK 210 SODIUM CHLORIDE
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM SEP DOMAIN U-15N;20MM
REMARK 210 PHOSPHATE BUFFER NA; 150MM
REMARK 210 SODIUM CHLORIDE; 90% H2O, 10%
REMARK 210 D2O; 1MM SEP DOMAIN U-15N,13C;
REMARK 210 20MM PHOSPHATE BUFFER NA; 150MM
REMARK 210 SODIUM CHLORIDE; 90% H2O, 10%
REMARK 210 D2O; 1MM SEP DOMAIN U-15N,13C;
REMARK 210 20MM PHOSPHATE BUFFER NA; 150MM
REMARK 210 SODIUM CHLORIDE; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PASTE/PAPST 1.4, PLATON 2.0,
REMARK 210 SPARKY 3.1, ARIA/CNS 1.2
REMARK 210 METHOD USED : DISTANCE GEOMETRY
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: 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 HB1 ALA A 58 HG22 VAL A 63 1.33
REMARK 500 OE1 GLU A 73 HZ3 LYS A 91 1.54
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 GLU A 3 -75.38 67.95
REMARK 500 1 LYS A 4 79.12 -154.40
REMARK 500 1 ARG A 5 -74.62 -137.79
REMARK 500 1 SER A 8 109.14 -39.06
REMARK 500 1 ASP A 11 88.42 56.39
REMARK 500 1 TYR A 33 44.75 -74.82
REMARK 500 1 GLN A 34 -43.10 -140.38
REMARK 500 1 GLN A 62 87.00 -66.59
REMARK 500 1 HIS A 70 -44.22 -138.36
REMARK 500 1 ARG A 71 -94.34 57.44
REMARK 500 1 ASP A 74 -100.60 61.45
REMARK 500 1 LYS A 77 -65.06 -138.77
REMARK 500 1 ALA A 81 -169.64 62.04
REMARK 500 1 LYS A 83 -7.59 64.90
REMARK 500 1 PHE A 85 72.41 66.04
REMARK 500 1 GLU A 88 79.15 52.35
REMARK 500 1 LYS A 91 -40.07 72.96
REMARK 500 2 ARG A 5 -86.88 68.72
REMARK 500 2 GLN A 6 -103.89 52.95
REMARK 500 2 HIS A 7 -77.27 66.38
REMARK 500 2 GLU A 29 -167.08 -77.76
REMARK 500 2 ARG A 56 44.90 -83.03
REMARK 500 2 LEU A 57 -58.14 -137.03
REMARK 500 2 ASP A 72 -29.49 177.32
REMARK 500 2 ASP A 74 164.22 65.95
REMARK 500 2 LYS A 77 144.84 80.90
REMARK 500 2 PRO A 78 -76.69 -68.86
REMARK 500 2 LYS A 79 -76.07 66.02
REMARK 500 2 ALA A 81 -34.75 72.71
REMARK 500 2 PHE A 85 59.24 -90.33
REMARK 500 2 THR A 86 74.49 -114.45
REMARK 500 2 GLN A 98 178.87 59.40
REMARK 500 2 SER A 101 -161.34 62.38
REMARK 500 3 SER A 2 -173.83 65.13
REMARK 500 3 GLN A 6 174.38 65.60
REMARK 500 3 SER A 8 -50.76 69.93
REMARK 500 3 SER A 9 44.60 -74.01
REMARK 500 3 ASP A 11 165.58 62.25
REMARK 500 3 TRP A 19 -167.83 -109.87
REMARK 500 3 ARG A 56 36.42 -88.13
REMARK 500 3 LEU A 57 -56.43 -120.70
REMARK 500 3 ASP A 72 -18.48 74.07
REMARK 500 3 ASP A 74 165.28 69.88
REMARK 500 3 PHE A 75 90.00 -66.80
REMARK 500 3 LYS A 77 143.74 77.51
REMARK 500 3 ALA A 84 -67.16 66.66
REMARK 500 3 GLN A 90 43.22 -176.39
REMARK 500 3 LYS A 91 -141.64 63.88
REMARK 500 3 LEU A 92 -71.60 71.97
REMARK 500 3 ALA A 96 84.15 66.25
REMARK 500
REMARK 500 THIS ENTRY HAS 342 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1SS6 A 3 102 UNP Q9UNZ2 NSF1C_HUMAN 171 270
SEQADV 1SS6 GLY A 1 UNP Q9UNZ2 CLONING ARTIFACT
SEQADV 1SS6 SER A 2 UNP Q9UNZ2 CLONING ARTIFACT
SEQRES 1 A 102 GLY SER GLU LYS ARG GLN HIS SER SER GLN ASP VAL HIS
SEQRES 2 A 102 VAL VAL LEU LYS LEU TRP LYS SER GLY PHE SER LEU ASP
SEQRES 3 A 102 ASN GLY GLU LEU ARG SER TYR GLN ASP PRO SER ASN ALA
SEQRES 4 A 102 GLN PHE LEU GLU SER ILE ARG ARG GLY GLU VAL PRO ALA
SEQRES 5 A 102 GLU LEU ARG ARG LEU ALA HIS GLY GLY GLN VAL ASN LEU
SEQRES 6 A 102 ASP MET GLU ASP HIS ARG ASP GLU ASP PHE VAL LYS PRO
SEQRES 7 A 102 LYS GLY ALA PHE LYS ALA PHE THR GLY GLU GLY GLN LYS
SEQRES 8 A 102 LEU GLY SER THR ALA PRO GLN VAL LEU SER THR
HELIX 1 1 ASN A 38 GLY A 48 1 11
HELIX 2 2 PRO A 51 ARG A 56 1 6
HELIX 3 3 LYS A 91 THR A 95 5 5
SHEET 1 A 4 LEU A 30 SER A 32 0
SHEET 2 A 4 GLY A 22 LEU A 25 -1 N PHE A 23 O ARG A 31
SHEET 3 A 4 VAL A 12 TRP A 19 -1 N TRP A 19 O GLY A 22
SHEET 4 A 4 VAL A 63 ARG A 71 1 O ASN A 64 N VAL A 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 - r 2 2 Bytes