Header list of 1klv.pdb file
Complete list - b 23 2 Bytes
HEADER PROTEIN BINDING 13-DEC-01 1KLV
TITLE SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF GABARAP, GABAA RECEPTOR
TITLE 2 ASSOCIATED PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GABA(A) RECEPTOR ASSOCIATED PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 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-2T
KEYWDS UBIQUITIN-LIKE FOLD, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.KOUNO,K.MIURA,M.TADA,T.KANEMATSU,S.TATE,M.SHIRAKAWA,M.HIRATA,
AUTHOR 2 K.KAWANO
REVDAT 3 23-FEB-22 1KLV 1 REMARK
REVDAT 2 24-FEB-09 1KLV 1 VERSN
REVDAT 1 07-OCT-03 1KLV 0
JRNL AUTH T.KOUNO,K.MIURA,T.KANEMATSU,M.SHIRAKAWA,M.HIRATA,K.KAWANO
JRNL TITL 1H, 13C AND '5N RESONANCE ASSIGNMENTS OF GABARAP, GABAA
JRNL TITL 2 RECEPTOR ASSOCIATED PROTEIN.
JRNL REF J.BIOMOL.NMR V. 22 97 2002
JRNL REFN ISSN 0925-2738
JRNL PMID 11885988
JRNL DOI 10.1023/A:1013884402033
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, X-PLOR 3.1
REMARK 3 AUTHORS : DELAGLIO, F., GRZESIEK, S., VUISTER, G.W., ZHU,
REMARK 3 G., PFEIFER, J. AND BAX, A. (NMRPIPE), BRUNGER,
REMARK 3 A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THIS STRUCTURE ARE BASED ON A TOTAL OF 976 RESTRAINTS, 861 ARE NOE-
REMARK 3 DERIVED DISTANCE
REMARK 3 CONSTRAINTS, 59 DIHEDRAL ANGLE RESTRAINTS, 56 DISTANCE RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS.
REMARK 4
REMARK 4 1KLV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-DEC-01.
REMARK 100 THE DEPOSITION ID IS D_1000015089.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 340
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1MM GABARAP, 20MM PHOSPHATE
REMARK 210 BUFFER NA, 50MM NACL, 0.02MM
REMARK 210 NAN3, 90% H2O, 10% D2O; 1MM
REMARK 210 GABARAP, 20MM PHOSPHATE BUFFER
REMARK 210 NA, 50MM NACL, 0.02MM NAN3, 100%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA; 2D
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PIPP
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
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 : NULL
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR 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 MET A 1
REMARK 465 LYS A 2
REMARK 465 PHE A 3
REMARK 465 VAL A 4
REMARK 465 TYR A 5
REMARK 465 LYS A 6
REMARK 465 GLU A 7
REMARK 465 GLU A 8
REMARK 465 HIS A 9
REMARK 465 PRO A 10
REMARK 465 PHE A 11
REMARK 465 GLU A 12
REMARK 465 LYS A 13
REMARK 465 ARG A 14
REMARK 465 ARG A 15
REMARK 465 SER A 16
REMARK 465 GLU A 17
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 TYR A 25 63.68 -113.65
REMARK 500 1 ALA A 36 -174.30 -65.01
REMARK 500 1 ALA A 39 -179.82 -57.47
REMARK 500 1 ARG A 40 35.11 -150.06
REMARK 500 1 ALA A 72 -88.90 56.95
REMARK 500 1 GLU A 73 24.17 -146.01
REMARK 500 1 ASP A 74 176.86 -49.09
REMARK 500 1 ILE A 84 67.70 -155.19
REMARK 500 1 SER A 88 43.15 -96.99
REMARK 500 1 HIS A 98 38.23 -99.44
REMARK 500 1 GLU A 100 -92.45 46.46
REMARK 500 1 PHE A 103 -57.27 -179.38
REMARK 500 1 SER A 113 34.82 -158.06
REMARK 500 1 VAL A 114 167.71 -43.54
REMARK 500 2 TYR A 25 71.38 -114.44
REMARK 500 2 ALA A 36 -172.66 -64.36
REMARK 500 2 ALA A 39 178.85 -58.68
REMARK 500 2 ARG A 40 35.53 -150.56
REMARK 500 2 ARG A 71 -166.94 -166.06
REMARK 500 2 ALA A 72 -87.34 55.45
REMARK 500 2 GLU A 73 27.09 -152.06
REMARK 500 2 ASP A 74 176.37 -53.84
REMARK 500 2 ILE A 84 73.07 -155.05
REMARK 500 2 SER A 88 42.01 -97.67
REMARK 500 2 HIS A 98 39.69 -97.97
REMARK 500 2 GLU A 100 -128.52 -164.26
REMARK 500 2 ASP A 102 -72.74 -41.28
REMARK 500 2 PHE A 103 -52.76 176.21
REMARK 500 2 SER A 113 31.92 -154.63
REMARK 500 3 TYR A 25 61.57 -114.32
REMARK 500 3 ALA A 36 -173.55 -64.92
REMARK 500 3 ARG A 40 30.74 -149.84
REMARK 500 3 HIS A 69 28.37 49.68
REMARK 500 3 ALA A 72 -89.94 52.08
REMARK 500 3 GLU A 73 29.29 -157.11
REMARK 500 3 ASP A 74 176.69 -48.39
REMARK 500 3 ILE A 84 68.53 -155.00
REMARK 500 3 SER A 88 41.23 -94.27
REMARK 500 3 HIS A 98 38.65 -99.38
REMARK 500 3 GLU A 100 -79.97 72.02
REMARK 500 3 GLU A 101 -63.95 -121.76
REMARK 500 3 ASP A 102 157.65 172.47
REMARK 500 3 PHE A 103 -20.93 78.26
REMARK 500 3 GLU A 112 145.04 59.67
REMARK 500 3 TYR A 115 -159.41 -79.99
REMARK 500 4 TYR A 25 64.19 -114.73
REMARK 500 4 ARG A 28 -168.08 -103.60
REMARK 500 4 ALA A 36 -173.22 -65.09
REMARK 500 4 ARG A 40 34.24 -150.30
REMARK 500 4 ARG A 71 -168.20 -165.83
REMARK 500
REMARK 500 THIS ENTRY HAS 308 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 22 0.27 SIDE CHAIN
REMARK 500 1 ARG A 28 0.17 SIDE CHAIN
REMARK 500 1 ARG A 65 0.23 SIDE CHAIN
REMARK 500 1 ARG A 67 0.17 SIDE CHAIN
REMARK 500 1 ARG A 71 0.24 SIDE CHAIN
REMARK 500 2 ARG A 22 0.31 SIDE CHAIN
REMARK 500 2 ARG A 28 0.29 SIDE CHAIN
REMARK 500 2 ARG A 40 0.31 SIDE CHAIN
REMARK 500 2 ARG A 65 0.18 SIDE CHAIN
REMARK 500 2 ARG A 67 0.30 SIDE CHAIN
REMARK 500 2 ARG A 71 0.17 SIDE CHAIN
REMARK 500 3 ARG A 22 0.30 SIDE CHAIN
REMARK 500 3 ARG A 28 0.31 SIDE CHAIN
REMARK 500 3 ARG A 40 0.30 SIDE CHAIN
REMARK 500 3 ARG A 65 0.16 SIDE CHAIN
REMARK 500 3 ARG A 67 0.27 SIDE CHAIN
REMARK 500 3 ARG A 71 0.28 SIDE CHAIN
REMARK 500 4 ARG A 22 0.31 SIDE CHAIN
REMARK 500 4 ARG A 28 0.28 SIDE CHAIN
REMARK 500 4 ARG A 40 0.17 SIDE CHAIN
REMARK 500 4 ARG A 65 0.31 SIDE CHAIN
REMARK 500 4 ARG A 67 0.13 SIDE CHAIN
REMARK 500 4 ARG A 71 0.26 SIDE CHAIN
REMARK 500 5 ARG A 22 0.32 SIDE CHAIN
REMARK 500 5 ARG A 28 0.26 SIDE CHAIN
REMARK 500 5 ARG A 40 0.12 SIDE CHAIN
REMARK 500 5 ARG A 65 0.25 SIDE CHAIN
REMARK 500 5 ARG A 67 0.31 SIDE CHAIN
REMARK 500 5 ARG A 71 0.28 SIDE CHAIN
REMARK 500 6 ARG A 22 0.31 SIDE CHAIN
REMARK 500 6 ARG A 28 0.23 SIDE CHAIN
REMARK 500 6 ARG A 40 0.30 SIDE CHAIN
REMARK 500 6 ARG A 65 0.26 SIDE CHAIN
REMARK 500 6 ARG A 67 0.20 SIDE CHAIN
REMARK 500 6 ARG A 71 0.30 SIDE CHAIN
REMARK 500 7 ARG A 22 0.29 SIDE CHAIN
REMARK 500 7 ARG A 28 0.27 SIDE CHAIN
REMARK 500 7 ARG A 40 0.32 SIDE CHAIN
REMARK 500 7 ARG A 65 0.25 SIDE CHAIN
REMARK 500 7 ARG A 67 0.29 SIDE CHAIN
REMARK 500 7 ARG A 71 0.28 SIDE CHAIN
REMARK 500 8 ARG A 22 0.28 SIDE CHAIN
REMARK 500 8 ARG A 28 0.31 SIDE CHAIN
REMARK 500 8 ARG A 40 0.08 SIDE CHAIN
REMARK 500 8 ARG A 65 0.21 SIDE CHAIN
REMARK 500 8 ARG A 67 0.19 SIDE CHAIN
REMARK 500 8 ARG A 71 0.23 SIDE CHAIN
REMARK 500 9 ARG A 22 0.30 SIDE CHAIN
REMARK 500 9 ARG A 28 0.21 SIDE CHAIN
REMARK 500 9 ARG A 40 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 116 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1KM7 RELATED DB: PDB
REMARK 900 1KM7 IS THE MINIMIZED AVERAGE STRUCTURE.
DBREF 1KLV A 1 117 UNP O95166 GBRAP_HUMAN 1 117
SEQRES 1 A 117 MET LYS PHE VAL TYR LYS GLU GLU HIS PRO PHE GLU LYS
SEQRES 2 A 117 ARG ARG SER GLU GLY GLU LYS ILE ARG LYS LYS TYR PRO
SEQRES 3 A 117 ASP ARG VAL PRO VAL ILE VAL GLU LYS ALA PRO LYS ALA
SEQRES 4 A 117 ARG ILE GLY ASP LEU ASP LYS LYS LYS TYR LEU VAL PRO
SEQRES 5 A 117 SER ASP LEU THR VAL GLY GLN PHE TYR PHE LEU ILE ARG
SEQRES 6 A 117 LYS ARG ILE HIS LEU ARG ALA GLU ASP ALA LEU PHE PHE
SEQRES 7 A 117 PHE VAL ASN ASN VAL ILE PRO PRO THR SER ALA THR MET
SEQRES 8 A 117 GLY GLN LEU TYR GLN GLU HIS HIS GLU GLU ASP PHE PHE
SEQRES 9 A 117 LEU TYR ILE ALA TYR SER ASP GLU SER VAL TYR GLY LEU
HELIX 1 1 GLY A 18 TYR A 25 1 8
HELIX 2 2 THR A 56 LYS A 66 1 11
HELIX 3 3 ARG A 67 HIS A 69 5 3
HELIX 4 4 THR A 90 HIS A 98 1 9
SHEET 1 A 4 LYS A 48 PRO A 52 0
SHEET 2 A 4 ARG A 28 LYS A 35 -1 N VAL A 29 O VAL A 51
SHEET 3 A 4 LEU A 105 SER A 110 1 O ILE A 107 N GLU A 34
SHEET 4 A 4 PHE A 77 PHE A 79 -1 N PHE A 79 O ALA A 108
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