Header list of 1y9j.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN TRANSPORT 15-DEC-04 1Y9J
TITLE SOLUTION STRUCTURE OF THE RAT SLY1 N-TERMINAL DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SEC1 FAMILY DOMAIN CONTAINING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 5 SYNONYM: SYNTAXIN BINDING PROTEIN 1- LIKE 2, VESICLE TRANSPORT-
COMPND 6 RELATED PROTEIN RA410, SLY1P;
COMPND 7 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 GENE: SCFD1, RA410, SLY1, STXBP1L2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 COMPETENT CELLS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-KG
KEYWDS MEMBRANE TRAFFIC, SLY1, SM PROTEINS, SNARES, PROTEIN NMR, PROTEIN
KEYWDS 2 TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.ARAC,I.DULUBOVA,J.PEI,I.HURYEVA,N.V.GRISHIN,J.RIZO
REVDAT 3 02-MAR-22 1Y9J 1 REMARK
REVDAT 2 24-FEB-09 1Y9J 1 VERSN
REVDAT 1 15-FEB-05 1Y9J 0
JRNL AUTH D.ARAC,I.DULUBOVA,J.PEI,I.HURYEVA,N.V.GRISHIN,J.RIZO
JRNL TITL THREE-DIMENSIONAL STRUCTURE OF THE RSLY1 N-TERMINAL DOMAIN
JRNL TITL 2 REVEALS A CONFORMATIONAL CHANGE INDUCED BY BINDING TO
JRNL TITL 3 SYNTAXIN 5.
JRNL REF J.MOL.BIOL. V. 346 589 2005
JRNL REFN ISSN 0022-2836
JRNL PMID 15670607
JRNL DOI 10.1016/J.JMB.2004.12.004
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CNS 0.9
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: A TOTAL OF 2493 RESTRAINTS WERE USED
REMARK 3 FOR THE FINAL CALCULATIONS, INCLUDING 2133 NOES (OF WHICH 738
REMARK 3 WERE LONG-RANGE NOES), 132 HYDROGEN BOND RESTRAINTS AND 228
REMARK 3 TORSION ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1Y9J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-DEC-04.
REMARK 100 THE DEPOSITION ID IS D_1000031286.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 5.7
REMARK 210 IONIC STRENGTH : 200 MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.2 MM SLY1 N-TERMINAL DOMAIN U
REMARK 210 -15N, 20 MM MES(PH 5.7), 200 MM
REMARK 210 KCL, 1 MM DTT; 1.2 MM SLY1 N-
REMARK 210 TERMINAL DOMAIN U-15N,13C, 20 MM
REMARK 210 MES(PH 5.7), 200 MM KCL, 1 MM
REMARK 210 DTT; 1 MM SLY1 N-TERMINAL DOMAIN
REMARK 210 U-10%13C, 20 MM MES(PH 5.7), 200
REMARK 210 MM KCL, 1 MM DTT
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 : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.3, NMRVIEW 4.1.2,
REMARK 210 TALOS 2003.027.13.05
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1400
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: THIS STRUCTURE WAS DETERMINED USING STANDARD TRIPLE
REMARK 210 RESONANCE TECHNIQUES
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -11
REMARK 465 SER A -10
REMARK 465 PRO A -9
REMARK 465 GLY A -8
REMARK 465 ILE A -7
REMARK 465 SER A -6
REMARK 465 GLY A -5
REMARK 465 GLY A -4
REMARK 465 GLY A -3
REMARK 465 GLY A -2
REMARK 465 GLY A -1
REMARK 465 ILE A 0
REMARK 465 LEU A 1
REMARK 465 VAL A 2
REMARK 465 GLY A 3
REMARK 465 SER A 4
REMARK 465 LYS A 5
REMARK 465 MET A 6
REMARK 465 ALA A 7
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 H ILE A 78 O LEU A 105 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 PHE A 24 97.51 -54.86
REMARK 500 1 PRO A 27 94.78 -42.06
REMARK 500 1 PRO A 36 -175.04 -54.04
REMARK 500 1 ASP A 44 -169.45 -113.55
REMARK 500 1 LEU A 67 136.64 -177.38
REMARK 500 1 HIS A 72 38.88 -93.71
REMARK 500 1 PRO A 89 48.76 -75.92
REMARK 500 1 TYR A 109 65.80 -152.38
REMARK 500 1 TYR A 110 93.73 -65.00
REMARK 500 2 PRO A 27 99.47 -46.25
REMARK 500 2 ASP A 44 -169.42 -103.11
REMARK 500 2 LEU A 67 136.94 -175.09
REMARK 500 2 HIS A 72 33.73 -93.74
REMARK 500 2 PRO A 89 46.47 -72.70
REMARK 500 2 TYR A 109 64.85 -150.08
REMARK 500 2 TYR A 110 90.69 -58.67
REMARK 500 2 ALA A 139 -179.94 -66.01
REMARK 500 3 ASN A 23 -44.48 -130.50
REMARK 500 3 ASP A 44 -169.26 -108.47
REMARK 500 3 LEU A 67 137.98 -175.40
REMARK 500 3 HIS A 72 38.51 -94.93
REMARK 500 3 PRO A 89 45.48 -89.65
REMARK 500 3 TYR A 109 63.44 -150.34
REMARK 500 3 TYR A 110 88.15 -59.96
REMARK 500 3 VAL A 135 107.44 -57.46
REMARK 500 3 GLN A 137 118.15 -165.16
REMARK 500 4 VAL A 29 98.20 -67.63
REMARK 500 4 PRO A 36 -163.36 -56.83
REMARK 500 4 ASP A 44 -169.04 -114.86
REMARK 500 4 LEU A 67 137.01 -173.03
REMARK 500 4 HIS A 72 33.46 -88.41
REMARK 500 4 PRO A 89 45.77 -80.03
REMARK 500 4 TYR A 109 67.43 -151.77
REMARK 500 4 TYR A 110 88.82 -59.49
REMARK 500 5 PRO A 36 -174.08 -53.29
REMARK 500 5 LEU A 67 137.69 -174.73
REMARK 500 5 HIS A 72 39.20 -93.40
REMARK 500 5 PRO A 89 43.90 -93.12
REMARK 500 5 TYR A 109 70.06 -150.02
REMARK 500 5 TYR A 110 89.61 -61.11
REMARK 500 5 GLN A 137 118.23 -162.10
REMARK 500 6 ASN A 23 -39.98 -134.04
REMARK 500 6 PRO A 27 101.43 -54.31
REMARK 500 6 ASP A 44 -169.33 -123.17
REMARK 500 6 LEU A 67 140.62 -178.85
REMARK 500 6 HIS A 72 36.84 -96.61
REMARK 500 6 PRO A 89 45.56 -87.36
REMARK 500 6 TYR A 110 89.98 -61.90
REMARK 500 6 GLN A 137 118.18 -160.54
REMARK 500 7 PRO A 27 105.79 -47.08
REMARK 500
REMARK 500 THIS ENTRY HAS 156 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1Y9J A 1 147 UNP Q62991 SCFD1_RAT 1 147
SEQADV 1Y9J GLY A -11 UNP Q62991 CLONING ARTIFACT
SEQADV 1Y9J SER A -10 UNP Q62991 CLONING ARTIFACT
SEQADV 1Y9J PRO A -9 UNP Q62991 CLONING ARTIFACT
SEQADV 1Y9J GLY A -8 UNP Q62991 CLONING ARTIFACT
SEQADV 1Y9J ILE A -7 UNP Q62991 CLONING ARTIFACT
SEQADV 1Y9J SER A -6 UNP Q62991 CLONING ARTIFACT
SEQADV 1Y9J GLY A -5 UNP Q62991 CLONING ARTIFACT
SEQADV 1Y9J GLY A -4 UNP Q62991 CLONING ARTIFACT
SEQADV 1Y9J GLY A -3 UNP Q62991 CLONING ARTIFACT
SEQADV 1Y9J GLY A -2 UNP Q62991 CLONING ARTIFACT
SEQADV 1Y9J GLY A -1 UNP Q62991 CLONING ARTIFACT
SEQADV 1Y9J ILE A 0 UNP Q62991 CLONING ARTIFACT
SEQADV 1Y9J LEU A 1 UNP Q62991 CLONING ARTIFACT
SEQRES 1 A 159 GLY SER PRO GLY ILE SER GLY GLY GLY GLY GLY ILE LEU
SEQRES 2 A 159 VAL GLY SER LYS MET ALA ALA SER ILE ARG GLU ARG GLN
SEQRES 3 A 159 THR VAL ALA LEU LYS ARG MET LEU ASN PHE ASN VAL PRO
SEQRES 4 A 159 HIS VAL LYS ASN SER PRO GLY GLU PRO VAL TRP LYS VAL
SEQRES 5 A 159 LEU ILE TYR ASP ARG PHE GLY GLN ASP ILE ILE SER PRO
SEQRES 6 A 159 LEU LEU SER VAL LYS GLU LEU ARG ASP MET GLY ILE THR
SEQRES 7 A 159 LEU HIS LEU LEU LEU HIS SER ASP ARG ASP PRO ILE ARG
SEQRES 8 A 159 ASP VAL PRO ALA VAL TYR PHE VAL MET PRO THR GLU GLU
SEQRES 9 A 159 ASN ILE ASP ARG LEU CYS GLN ASP LEU ARG ASN GLN LEU
SEQRES 10 A 159 TYR GLU SER TYR TYR LEU ASN PHE ILE SER ALA ILE SER
SEQRES 11 A 159 ARG SER LYS LEU GLU ASP ILE ALA ASN ALA ALA LEU ALA
SEQRES 12 A 159 ALA ASN ALA VAL THR GLN VAL ALA LYS VAL PHE ASP GLN
SEQRES 13 A 159 TYR LEU ASN
HELIX 1 1 ALA A 8 LEU A 22 1 15
HELIX 2 2 ASP A 44 SER A 52 1 9
HELIX 3 3 SER A 56 MET A 63 1 8
HELIX 4 4 THR A 90 GLN A 104 1 15
HELIX 5 5 SER A 118 ALA A 131 1 14
SHEET 1 A 2 LYS A 39 TYR A 43 0
SHEET 2 A 2 ILE A 65 LEU A 70 1 O LEU A 67 N LEU A 41
SHEET 1 B 3 VAL A 84 VAL A 87 0
SHEET 2 B 3 SER A 108 PHE A 113 1 O TYR A 110 N TYR A 85
SHEET 3 B 3 VAL A 135 ALA A 139 1 O ALA A 139 N LEU A 111
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