Header list of 1kot.pdb file
Complete list - b 23 2 Bytes
HEADER TRANSPORT PROTEIN 22-DEC-01 1KOT
TITLE SOLUTION STRUCTURE OF HUMAN GABA RECEPTOR ASSOCIATED PROTEIN GABARAP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GABARAP;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GABA-A RECEPTOR-ASSOCIATED PROTEIN;
COMPND 5 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 BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PGEX-GABARAP
KEYWDS HUMAN GABA RECEPTOR TARGETING GABARAP, TRANSPORT PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR T.STANGLER,C.LUGE,L.M.MAYR,D.WILLBOLD
REVDAT 3 23-FEB-22 1KOT 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1KOT 1 VERSN
REVDAT 1 16-JAN-02 1KOT 0
JRNL AUTH T.STANGLER,L.M.MAYR,D.WILLBOLD
JRNL TITL SOLUTION STRUCTURE OF HUMAN GABA(A) RECEPTOR-ASSOCIATED
JRNL TITL 2 PROTEIN GABARAP: IMPLICATIONS FOR BIOLGOICAL FUNCRION AND
JRNL TITL 3 ITS REGULATION.
JRNL REF J.BIOL.CHEM. V. 277 13363 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11875056
JRNL DOI 10.1074/JBC.C200050200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 5.3, ARIA 1.0, CNS 1.0
REMARK 3 AUTHORS : VARIAN (VNMR), NILGES (ARIA), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KOT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000015180.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.9
REMARK 210 IONIC STRENGTH : 100MM NACL 100MM KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM GABARAP U-15N,13C; 25MM
REMARK 210 SODIUM OXALATE, PH 6.9 100MM
REMARK 210 NACL 100MM KCL 100UM PMSF 0.02%
REMARK 210 SODIUM AZIDE 50UM EDTA 5% D2O,
REMARK 210 95% H2O; 0.8MM GABARAP U-15N,13C;
REMARK 210 25MM SODIUM PHOSPHATE, PH 6.9
REMARK 210 100MM NACL 100MM KCL 100UM PMSF
REMARK 210 0.02% SODIUM AZIDE 50UM EDTA 100%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 3D_13C_-SEPERATED(AROMATICS)_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; DMX
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5.0.3
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
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: 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 H ILE A 34 O LEU A 107 1.56
REMARK 500 O VAL A 116 H GLY A 118 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 SER A 2 54.85 -163.76
REMARK 500 1 VAL A 6 -47.57 -134.07
REMARK 500 1 HIS A 11 101.86 -46.79
REMARK 500 1 PRO A 12 170.65 -39.94
REMARK 500 1 ILE A 34 72.13 -115.04
REMARK 500 1 ALA A 38 148.38 -36.62
REMARK 500 1 LYS A 40 -8.04 66.88
REMARK 500 1 ARG A 42 36.72 -91.18
REMARK 500 1 LYS A 49 -55.32 68.43
REMARK 500 1 PRO A 54 -169.48 -55.30
REMARK 500 1 HIS A 71 55.89 82.95
REMARK 500 1 LEU A 78 108.45 -169.64
REMARK 500 1 ASN A 84 4.61 88.88
REMARK 500 1 HIS A 100 9.86 -154.83
REMARK 500 1 GLU A 103 -162.96 57.13
REMARK 500 1 PHE A 105 24.81 47.74
REMARK 500 1 TYR A 117 69.30 -60.47
REMARK 500 2 SER A 2 86.86 -158.55
REMARK 500 2 VAL A 6 -75.31 -142.98
REMARK 500 2 HIS A 11 100.35 -46.55
REMARK 500 2 PRO A 12 172.71 -42.48
REMARK 500 2 ALA A 38 134.56 -30.42
REMARK 500 2 PRO A 39 162.07 -49.85
REMARK 500 2 LYS A 40 -34.10 64.48
REMARK 500 2 ALA A 41 131.70 -35.55
REMARK 500 2 ARG A 42 36.42 -90.82
REMARK 500 2 LYS A 49 -60.57 66.51
REMARK 500 2 PRO A 54 -171.57 -55.33
REMARK 500 2 HIS A 71 51.85 75.59
REMARK 500 2 ARG A 73 43.71 -86.55
REMARK 500 2 ALA A 74 -46.14 75.77
REMARK 500 2 LEU A 78 117.47 -170.39
REMARK 500 2 GLU A 103 -173.74 56.61
REMARK 500 2 PHE A 105 15.20 55.64
REMARK 500 2 TYR A 117 96.32 -44.36
REMARK 500 3 SER A 2 -158.68 -149.14
REMARK 500 3 VAL A 6 -77.41 -124.75
REMARK 500 3 PRO A 12 176.20 -43.59
REMARK 500 3 SER A 18 -73.52 -48.39
REMARK 500 3 ALA A 38 166.55 -39.05
REMARK 500 3 LYS A 40 -0.57 52.26
REMARK 500 3 ARG A 42 36.29 -90.21
REMARK 500 3 PRO A 54 -172.55 -54.17
REMARK 500 3 PHE A 64 -34.49 -39.86
REMARK 500 3 HIS A 71 54.70 80.22
REMARK 500 3 ALA A 74 -67.05 64.98
REMARK 500 3 LEU A 78 107.13 -164.17
REMARK 500 3 ASN A 84 7.66 88.58
REMARK 500 3 HIS A 100 -30.44 -144.36
REMARK 500 3 GLU A 102 63.42 -69.49
REMARK 500
REMARK 500 THIS ENTRY HAS 280 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1KOT A 3 119 UNP O95166 GBRAP_HUMAN 1 117
SEQADV 1KOT GLY A 1 UNP O95166 CLONING ARTIFACT
SEQADV 1KOT SER A 2 UNP O95166 CLONING ARTIFACT
SEQRES 1 A 119 GLY SER MET LYS PHE VAL TYR LYS GLU GLU HIS PRO PHE
SEQRES 2 A 119 GLU LYS ARG ARG SER GLU GLY GLU LYS ILE ARG LYS LYS
SEQRES 3 A 119 TYR PRO ASP ARG VAL PRO VAL ILE VAL GLU LYS ALA PRO
SEQRES 4 A 119 LYS ALA ARG ILE GLY ASP LEU ASP LYS LYS LYS TYR LEU
SEQRES 5 A 119 VAL PRO SER ASP LEU THR VAL GLY GLN PHE TYR PHE LEU
SEQRES 6 A 119 ILE ARG LYS ARG ILE HIS LEU ARG ALA GLU ASP ALA LEU
SEQRES 7 A 119 PHE PHE PHE VAL ASN ASN VAL ILE PRO PRO THR SER ALA
SEQRES 8 A 119 THR MET GLY GLN LEU TYR GLN GLU HIS HIS GLU GLU ASP
SEQRES 9 A 119 PHE PHE LEU TYR ILE ALA TYR SER ASP GLU SER VAL TYR
SEQRES 10 A 119 GLY LEU
HELIX 1 1 VAL A 6 HIS A 11 1 6
HELIX 2 2 PRO A 12 TYR A 27 1 16
HELIX 3 3 THR A 58 HIS A 71 1 14
HELIX 4 4 THR A 92 HIS A 101 1 10
SHEET 1 A 3 LYS A 50 PRO A 54 0
SHEET 2 A 3 ARG A 30 ILE A 34 -1 N VAL A 31 O VAL A 53
SHEET 3 A 3 LEU A 107 TYR A 108 1 O LEU A 107 N ILE A 34
SHEET 1 B 2 PHE A 79 PHE A 81 0
SHEET 2 B 2 ALA A 110 SER A 112 -1 O SER A 112 N PHE A 79
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