Header list of 1ozi.pdb file
Complete list - b 23 2 Bytes
HEADER HYDROLASE 09-APR-03 1OZI
TITLE THE ALTERNATIVELY SPLICED PDZ2 DOMAIN OF PTP-BL
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN TYROSINE PHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ2 OF PTP-BL;
COMPND 5 SYNONYM: NONRECEPTOR-TYPE, 13, PROTEIN-TYROSINE PHOSPHATASE RIP,
COMPND 6 PHOSPHOPROTEIN PHOSPHATASE, PROTEIN-TYROSINE-PHOSPHATASE,
COMPND 7 PHOSPHOTYROSINE PHOSPHATASE, PTPASE, PTP36, BAS-LIKE;
COMPND 8 EC: 3.1.3.48;
COMPND 9 ENGINEERED: YES;
COMPND 10 MUTATION: YES;
COMPND 11 OTHER_DETAILS: LONGER ALTERNATIVE SPLICE VARIANT
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PTP-BL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ESCHERICHIA COLI BL21 CODON PLUS (DE3) RIL
SOURCE 9 COMPETENT;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS ALL-BETA PROTEIN, PDZ DOMAIN, INTERACTION WITH C-TERMINI, APC,
KEYWDS 2 ADENOMATOUS POLYPOSIS COLI, RIL, REVERSION INDUCED LIM, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR T.WALMA,J.AELEN,M.OOSTENDORP,L.VAN DEN BERK,W.HENDRIKS,G.W.VUISTER
REVDAT 3 23-FEB-22 1OZI 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1OZI 1 VERSN
REVDAT 1 27-JAN-04 1OZI 0
JRNL AUTH T.WALMA,J.AELEN,S.B.NABUURS,M.OOSTENDORP,L.VAN DEN BERK,
JRNL AUTH 2 W.HENDRIKS,G.W.VUISTER
JRNL TITL A CLOSED BINDING POCKET AND GLOBAL DESTABILIZATION MODIFY
JRNL TITL 2 THE BINDING PROPERTIES OF AN ALTERNATIVELY SPLICED FORM OF
JRNL TITL 3 THE SECOND PDZ DOMAIN OF PTP-BL.
JRNL REF STRUCTURE V. 12 11 2004
JRNL REFN ISSN 0969-2126
JRNL PMID 14725761
JRNL DOI 10.1016/J.STR.2003.11.023
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE, X-PLOR 3.851, X-PLOR NIH
REMARK 3 AUTHORS : DELAGLIO ET AL. (NMRPIPE), BRUNGER (X-PLOR),
REMARK 3 BRUNGER, NIH (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1459 RESTRAINTS: 1354 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 76 DIHEDRAL ANGLE RESTRAINTS, 29 DISTANCE
REMARK 3 RESTRAINTS
REMARK 3 FROM HYDROGEN BONDS
REMARK 4
REMARK 4 1OZI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018838.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 100
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.4MM PDZ2_AS, 13C/15N LABELLED,
REMARK 210 50MM POTASSIUM PHOSPHATE BUFFER,
REMARK 210 50MM KCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : CARTESIAN SPACE DISTANCE
REMARK 210 GEOMETRY, RESTRAINED MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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
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 ASP A 22 -68.80 -164.84
REMARK 500 1 SER A 24 -170.34 62.01
REMARK 500 1 LEU A 32 124.19 -170.82
REMARK 500 1 ASP A 34 99.36 -62.55
REMARK 500 1 ASN A 39 -30.93 -166.17
REMARK 500 1 PRO A 54 -110.19 -17.25
REMARK 500 1 LYS A 55 -67.06 70.69
REMARK 500 1 ALA A 57 -110.29 59.04
REMARK 500 1 LYS A 66 43.35 -79.76
REMARK 500 2 VAL A 31 -63.64 -94.04
REMARK 500 2 HIS A 44 132.38 77.30
REMARK 500 2 PRO A 54 -152.97 -56.40
REMARK 500 2 LYS A 55 -44.97 72.80
REMARK 500 2 ALA A 57 -99.48 71.27
REMARK 500 2 THR A 93 -177.81 -67.18
REMARK 500 2 VAL A 106 87.86 44.06
REMARK 500 3 THR A 21 -84.00 -90.36
REMARK 500 3 SER A 24 -109.94 76.69
REMARK 500 3 PHE A 33 13.89 -166.88
REMARK 500 3 ASP A 34 -80.58 -75.13
REMARK 500 3 LYS A 35 115.84 -169.89
REMARK 500 3 ASN A 39 164.78 70.05
REMARK 500 3 SER A 41 -90.22 -59.85
REMARK 500 3 HIS A 44 -102.14 53.63
REMARK 500 3 PRO A 54 -77.38 -59.47
REMARK 500 3 ALA A 57 -71.31 167.25
REMARK 500 3 ARG A 63 -58.87 -128.70
REMARK 500 4 PRO A 10 44.38 -70.10
REMARK 500 4 ASP A 22 -72.01 -105.75
REMARK 500 4 LYS A 35 -50.41 -170.94
REMARK 500 4 VAL A 38 -84.00 -78.80
REMARK 500 4 ASN A 39 -69.37 -122.13
REMARK 500 4 HIS A 44 -81.55 -151.25
REMARK 500 4 PRO A 54 78.55 -65.25
REMARK 500 4 ALA A 57 -103.48 69.79
REMARK 500 4 VAL A 106 80.00 52.02
REMARK 500 5 ASP A 22 -154.84 -111.65
REMARK 500 5 ASP A 34 90.83 -68.11
REMARK 500 5 ALA A 57 -86.02 37.66
REMARK 500 6 ASP A 22 -50.35 -170.20
REMARK 500 6 SER A 24 -160.15 69.10
REMARK 500 6 ALA A 57 -86.71 75.98
REMARK 500 6 ARG A 63 -39.19 -136.43
REMARK 500 7 SER A 24 -153.73 72.40
REMARK 500 7 VAL A 38 -63.72 -107.36
REMARK 500 7 ASN A 39 -77.08 63.39
REMARK 500 7 THR A 40 -20.54 165.84
REMARK 500 7 SER A 41 33.25 -80.46
REMARK 500 7 ARG A 43 75.08 -114.09
REMARK 500 7 ILE A 53 -89.38 -103.30
REMARK 500
REMARK 500 THIS ENTRY HAS 226 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 5 ARG A 69 0.08 SIDE CHAIN
REMARK 500 5 ARG A 91 0.08 SIDE CHAIN
REMARK 500 6 ARG A 63 0.08 SIDE CHAIN
REMARK 500 23 ARG A 63 0.07 SIDE CHAIN
REMARK 500 24 ARG A 43 0.07 SIDE CHAIN
REMARK 500 26 ARG A 91 0.09 SIDE CHAIN
REMARK 500 29 ARG A 63 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5762 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT AND J COUPLING INFORMATION
REMARK 900 RELATED ID: 1GM1 RELATED DB: PDB
REMARK 900 PDZ2 OF PTP-BL
REMARK 900 RELATED ID: 5131 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT AND J COUPLING INFORMATION FOR PDZ2 OF PTP-BL
DBREF 1OZI A 9 107 UNP Q64512 PTN13_MOUSE 1351 1444
SEQADV 1OZI VAL A 31 UNP Q64512 INSERTION
SEQADV 1OZI LEU A 32 UNP Q64512 INSERTION
SEQADV 1OZI PHE A 33 UNP Q64512 INSERTION
SEQADV 1OZI ASP A 34 UNP Q64512 INSERTION
SEQADV 1OZI LYS A 35 UNP Q64512 INSERTION
SEQRES 1 A 99 LYS PRO GLY ASP THR PHE GLU VAL GLU LEU ALA LYS THR
SEQRES 2 A 99 ASP GLY SER LEU GLY ILE SER VAL THR VAL LEU PHE ASP
SEQRES 3 A 99 LYS GLY GLY VAL ASN THR SER VAL ARG HIS GLY GLY ILE
SEQRES 4 A 99 TYR VAL LYS ALA ILE ILE PRO LYS GLY ALA ALA GLU SER
SEQRES 5 A 99 ASP GLY ARG ILE HIS LYS GLY ASP ARG VAL LEU ALA VAL
SEQRES 6 A 99 ASN GLY VAL SER LEU GLU GLY ALA THR HIS LYS GLN ALA
SEQRES 7 A 99 VAL GLU THR LEU ARG ASN THR GLY GLN VAL VAL HIS LEU
SEQRES 8 A 99 LEU LEU GLU LYS GLY GLN VAL PRO
HELIX 1 1 GLY A 56 GLY A 62 1 7
HELIX 2 2 THR A 82 THR A 93 1 12
SHEET 1 A 5 THR A 13 ALA A 19 0
SHEET 2 A 5 VAL A 96 GLU A 102 -1 O VAL A 97 N LEU A 18
SHEET 3 A 5 ARG A 69 VAL A 73 -1 N ARG A 69 O GLU A 102
SHEET 4 A 5 ILE A 47 ILE A 52 -1 N ILE A 47 O VAL A 70
SHEET 5 A 5 ILE A 27 THR A 30 -1 N THR A 30 O TYR A 48
SHEET 1 B 4 THR A 13 ALA A 19 0
SHEET 2 B 4 VAL A 96 GLU A 102 -1 O VAL A 97 N LEU A 18
SHEET 3 B 4 ARG A 69 VAL A 73 -1 N ARG A 69 O GLU A 102
SHEET 4 B 4 VAL A 76 SER A 77 -1 O VAL A 76 N VAL A 73
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