Header list of 3pdz.pdb file
Complete list - r 16 2 Bytes
HEADER HYDROLASE 10-MAY-99 3PDZ
TITLE SOLUTION STRUCTURE OF THE PDZ2 DOMAIN FROM HUMAN PHOSPHATASE HPTP1E
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (TYROSINE PHOSPHATASE (PTP-BAS, TYPE 1));
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PDZ2 DOMAIN;
COMPND 5 EC: 3.1.3.48;
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 BL21;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PBR322;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PGEX
KEYWDS PDZ DOMAIN, HUMAN PHOSPHATASE, HPTP1E, PTP-BAS, SPECIFICITY OF
KEYWDS 2 BINDING, HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR G.KOZLOV,K.GEHRING,I.EKIEL
REVDAT 3 16-MAR-22 3PDZ 1 REMARK
REVDAT 2 24-FEB-09 3PDZ 1 VERSN
REVDAT 1 17-MAR-00 3PDZ 0
JRNL AUTH G.KOZLOV,K.GEHRING,I.EKIEL
JRNL TITL SOLUTION STRUCTURE OF THE PDZ2 DOMAIN FROM HUMAN PHOSPHATASE
JRNL TITL 2 HPTP1E AND ITS INTERACTIONS WITH C-TERMINAL PEPTIDES FROM
JRNL TITL 3 THE FAS RECEPTOR.
JRNL REF BIOCHEMISTRY V. 39 2572 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10704206
JRNL DOI 10.1021/BI991913C
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ,RICE,SIMONSON,WARREN
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE
REMARK 3 -KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN
REMARK 3 PRIMARY REFERENCE
REMARK 4
REMARK 4 3PDZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-99.
REMARK 100 THE DEPOSITION ID IS D_1000001032.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 10% D2O/90% WATER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D AND 3D EXPERIMENTS
REMARK 210 USING UNLABELED, 15N- LABELED, AND DOUBLE-LABELED PROTEIN
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 VAL A 9 O LEU A 87 1.58
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 PRO A 3 -162.78 -63.89
REMARK 500 1 GLU A 10 72.11 -105.87
REMARK 500 1 ASP A 15 -27.91 88.67
REMARK 500 1 VAL A 26 144.33 -33.13
REMARK 500 1 THR A 28 -67.68 -151.71
REMARK 500 1 HIS A 32 -57.36 -132.88
REMARK 500 1 PRO A 42 61.56 -61.56
REMARK 500 1 GLN A 43 -47.94 -149.93
REMARK 500 1 SER A 48 -71.12 -53.64
REMARK 500 1 ASN A 80 58.52 -66.06
REMARK 500 1 THR A 81 -71.46 -95.57
REMARK 500 1 GLN A 83 -82.77 -64.67
REMARK 500 1 LEU A 89 -164.91 -104.11
REMARK 500 1 LYS A 91 102.04 -52.11
REMARK 500 2 PRO A 3 -166.77 -69.06
REMARK 500 2 GLU A 10 74.33 -106.18
REMARK 500 2 ASP A 15 -38.27 179.81
REMARK 500 2 VAL A 26 138.58 -30.63
REMARK 500 2 THR A 28 -50.76 -151.70
REMARK 500 2 HIS A 32 -46.76 -163.90
REMARK 500 2 PRO A 42 59.94 -62.01
REMARK 500 2 GLN A 43 -47.69 -147.53
REMARK 500 2 SER A 48 -71.49 -53.76
REMARK 500 2 GLU A 67 106.17 -46.53
REMARK 500 2 ASN A 80 62.90 -65.88
REMARK 500 2 THR A 81 -70.87 -91.70
REMARK 500 2 GLN A 83 -77.88 -65.25
REMARK 500 2 LEU A 89 -162.83 -103.88
REMARK 500 2 PRO A 95 109.19 -53.47
REMARK 500 3 PRO A 3 -161.78 -70.73
REMARK 500 3 GLU A 10 70.54 -105.98
REMARK 500 3 ASP A 15 -42.93 84.02
REMARK 500 3 VAL A 26 161.30 -40.46
REMARK 500 3 THR A 28 -58.23 -151.71
REMARK 500 3 HIS A 32 -80.61 61.67
REMARK 500 3 PRO A 42 62.01 -61.16
REMARK 500 3 GLN A 43 -48.60 -150.55
REMARK 500 3 LYS A 54 133.76 -36.23
REMARK 500 3 GLU A 67 95.07 -48.23
REMARK 500 3 ASN A 80 62.28 -66.00
REMARK 500 3 THR A 81 -68.68 -93.80
REMARK 500 3 GLN A 83 -77.26 -65.47
REMARK 500 3 LEU A 89 -165.19 -105.66
REMARK 500 3 LYS A 91 103.63 -46.89
REMARK 500 4 LYS A 2 89.26 -155.17
REMARK 500 4 GLU A 10 72.42 -106.09
REMARK 500 4 LEU A 18 -168.68 -101.14
REMARK 500 4 VAL A 26 145.13 -30.54
REMARK 500 4 THR A 28 -64.96 -151.69
REMARK 500 4 HIS A 32 -84.71 58.18
REMARK 500
REMARK 500 THIS ENTRY HAS 497 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3PDZ A 1 96 UNP Q12923 PTN13_HUMAN 1361 1456
SEQRES 1 A 96 PRO LYS PRO GLY ASP ILE PHE GLU VAL GLU LEU ALA LYS
SEQRES 2 A 96 ASN ASP ASN SER LEU GLY ILE SER VAL THR GLY GLY VAL
SEQRES 3 A 96 ASN THR SER VAL ARG HIS GLY GLY ILE TYR VAL LYS ALA
SEQRES 4 A 96 VAL ILE PRO GLN GLY ALA ALA GLU SER ASP GLY ARG ILE
SEQRES 5 A 96 HIS LYS GLY ASP ARG VAL LEU ALA VAL ASN GLY VAL SER
SEQRES 6 A 96 LEU GLU GLY ALA THR HIS LYS GLN ALA VAL GLU THR LEU
SEQRES 7 A 96 ARG ASN THR GLY GLN VAL VAL HIS LEU LEU LEU GLU LYS
SEQRES 8 A 96 GLY GLN SER PRO THR
HELIX 1 1 ALA A 45 ASP A 49 1 5
HELIX 2 2 HIS A 71 ARG A 79 1 9
SHEET 1 A 3 ILE A 6 LEU A 11 0
SHEET 2 A 3 VAL A 85 GLU A 90 -1 N LEU A 89 O PHE A 7
SHEET 3 A 3 ARG A 57 VAL A 61 -1 N ALA A 60 O LEU A 88
SHEET 1 B 2 ILE A 20 THR A 23 0
SHEET 2 B 2 TYR A 36 VAL A 40 -1 N ALA A 39 O SER A 21
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 16 2 Bytes