Header list of 1kef.pdb file
Complete list - 23 20 Bytes
HEADER PROTEIN BINDING 15-NOV-01 1KEF
TITLE PDZ1 OF SAP90
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNAPSE ASSOCIATED PROTEIN-90;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ1 DOMAIN;
COMPND 5 SYNONYM: (SAP90), PRESYNAPTIC DENSITY PROTEIN 95, PSD-95;
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 BETA-SHEET, ANTI-PARALLEL BETA-SANDWICH, GLGF LOOP, PROTEIN BINDING
EXPDTA SOLUTION NMR
AUTHOR A.PISERCHIO,M.PELLEGRINI,S.MEHTA,S.M.BLACKMAN,E.P.GARCIA,J.MARSHALL,
AUTHOR 2 D.F.MIERKE
REVDAT 3 23-FEB-22 1KEF 1 REMARK
REVDAT 2 24-FEB-09 1KEF 1 VERSN
REVDAT 1 06-MAR-02 1KEF 0
JRNL AUTH A.PISERCHIO,M.PELLEGRINI,S.MEHTA,S.M.BLACKMAN,E.P.GARCIA,
JRNL AUTH 2 J.MARSHALL,D.F.MIERKE
JRNL TITL THE PDZ1 DOMAIN OF SAP90. CHARACTERIZATION OF STRUCTURE AND
JRNL TITL 2 BINDING.
JRNL REF J.BIOL.CHEM. V. 277 6967 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11744724
JRNL DOI 10.1074/JBC.M109453200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 3.0, X-PLOR CNS
REMARK 3 AUTHORS : DELAGLIO F. (NMRPIPE), BRUENGER, A. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1KEF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-NOV-01.
REMARK 100 THE DEPOSITION ID IS D_1000014866.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 150 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.0 MM PROTEIN, 10 MM PHOSPHATE
REMARK 210 BUFFER, 150 MM NACL, PH 6.8
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING WITH TORSION
REMARK 210 ANGLE RESTRAINTS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : AVERAGE STRUCTURE FROM ENSEMBLE
REMARK 210 OF 28 STRUCTURES, CHOSEN BY
REMARK 210 ENERGY AND PENALTY FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 69 CG HIS A 69 CD2 0.058
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 9 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 HIS A 26 ND1 - CE1 - NE2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG A 49 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 51 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 ARG A 65 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 HIS A 69 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ARG A 84 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG A 90 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
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 SER A 12 -139.58 70.21
REMARK 500 LEU A 14 -72.19 -121.55
REMARK 500 ASP A 23 -53.94 -123.65
REMARK 500 PRO A 25 90.98 -60.31
REMARK 500 ASP A 29 -62.24 -158.97
REMARK 500 THR A 36 -72.05 -103.43
REMARK 500 ALA A 43 -43.92 175.95
REMARK 500 ARG A 49 -35.34 -144.07
REMARK 500 PHE A 58 73.76 -162.92
REMARK 500 ASN A 60 -144.17 66.57
REMARK 500 GLU A 61 59.50 -94.68
REMARK 500 ARG A 65 -49.67 -179.15
REMARK 500 LYS A 91 -63.97 -148.50
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1KEF A 1 93 UNP P78352 DLG4_HUMAN 105 197
SEQRES 1 A 93 GLU TYR GLU GLU ILE THR LEU GLU ARG GLY ASN SER GLY
SEQRES 2 A 93 LEU GLY PHE SER ILE ALA GLY GLY THR ASP ASN PRO HIS
SEQRES 3 A 93 ILE GLY ASP ASP PRO SER ILE PHE ILE THR LYS ILE ILE
SEQRES 4 A 93 PRO GLY GLY ALA ALA ALA GLN ASP GLY ARG LEU ARG VAL
SEQRES 5 A 93 ASN ASP SER ILE LEU PHE VAL ASN GLU VAL ASP VAL ARG
SEQRES 6 A 93 GLU VAL THR HIS SER ALA ALA VAL GLU ALA LEU LYS GLU
SEQRES 7 A 93 ALA GLY SER ILE VAL ARG LEU TYR VAL MET ARG ARG LYS
SEQRES 8 A 93 PRO PRO
HELIX 1 1 ALA A 43 GLY A 48 1 6
HELIX 2 2 THR A 68 GLY A 80 1 13
SHEET 1 A 2 GLU A 3 LEU A 7 0
SHEET 2 A 2 VAL A 83 VAL A 87 -1 O VAL A 83 N LEU A 7
SHEET 1 B 3 PHE A 16 ALA A 19 0
SHEET 2 B 3 ILE A 33 ILE A 38 -1 O THR A 36 N SER A 17
SHEET 3 B 3 SER A 55 ILE A 56 -1 O ILE A 56 N ILE A 33
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
Complete list - 23 20 Bytes