Header list of 1xz9.pdb file
Complete list - r 2 2 Bytes
HEADER CELL ADHESION 12-NOV-04 1XZ9
TITLE STRUCTURE OF AF-6 PDZ DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AFADIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: AF-6 PDZ DOMAIN;
COMPND 5 SYNONYM: AF-6 PROTEIN;
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 PDZ, AF-6, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.JOSHI,P.BOISGUERIN,D.LEITNER,R.VOLKMER-ENGERT,K.MOELLING,M.SCHADE,
AUTHOR 2 P.SCHMIEDER,G.KRAUSE,H.OSCHKINAT
REVDAT 4 02-MAR-22 1XZ9 1 REMARK SEQADV
REVDAT 3 28-APR-09 1XZ9 1 JRNL
REVDAT 2 24-FEB-09 1XZ9 1 VERSN
REVDAT 1 15-NOV-05 1XZ9 0
JRNL AUTH M.JOSHI,C.VARGAS,P.BOISGUERIN,A.DIEHL,G.KRAUSE,P.SCHMIEDER,
JRNL AUTH 2 K.MOELLING,V.HAGEN,M.SCHADE,H.OSCHKINAT
JRNL TITL DISCOVERY OF LOW-MOLECULAR-WEIGHT LIGANDS FOR THE AF6 PDZ
JRNL TITL 2 DOMAIN.
JRNL REF ANGEW.CHEM.INT.ED.ENGL. V. 45 3790 2006
JRNL REFN ISSN 1433-7851
JRNL PMID 16671149
JRNL DOI 10.1002/ANIE.200503965
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, DYANA 1.0.6
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUENTERT, P. (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XZ9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-NOV-04.
REMARK 100 THE DEPOSITION ID IS D_1000030929.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 20MM PHOSPHATE, 50MM SODIUM
REMARK 210 CHLORIDE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.25MM PDZ DOMAIN U-15N; 20MM
REMARK 210 PHOSPHATE BUFFER; 50MM SODIUM
REMARK 210 CHLORIDE; 90% H2O, 10% D2O;
REMARK 210 1.25MM PDZ DOMAIN U-15N, 13C;
REMARK 210 20MM PHOSPHATE BUFFER; 50MM
REMARK 210 SODIUM CHLORIDE; 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, SPARKY 3.1, DYANA
REMARK 210 1.0.6
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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 O ALA A 80 HG1 THR A 84 1.46
REMARK 500 H VAL A 66 O ARG A 69 1.49
REMARK 500 O LEU A 71 H GLY A 73 1.55
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 5 -66.20 -148.70
REMARK 500 1 LYS A 8 174.62 53.59
REMARK 500 1 PRO A 10 -89.67 -75.01
REMARK 500 1 GLU A 11 -73.81 82.29
REMARK 500 1 LEU A 17 -149.19 -66.48
REMARK 500 1 LYS A 19 -114.67 -59.79
REMARK 500 1 ASN A 21 -73.45 158.54
REMARK 500 1 ALA A 29 -166.49 159.18
REMARK 500 1 ALA A 30 -145.87 -177.85
REMARK 500 1 LYS A 31 108.89 -172.53
REMARK 500 1 LYS A 37 91.96 178.77
REMARK 500 1 SER A 44 -168.80 -169.73
REMARK 500 1 ALA A 50 -38.71 -39.58
REMARK 500 1 ALA A 51 -76.94 -53.03
REMARK 500 1 ARG A 56 -41.21 -155.54
REMARK 500 1 ALA A 58 -169.85 168.60
REMARK 500 1 VAL A 72 55.51 -69.02
REMARK 500 1 GLN A 76 -32.79 -37.53
REMARK 500 1 THR A 84 -75.30 -69.30
REMARK 500 1 SER A 87 -178.83 82.72
REMARK 500 1 SER A 88 7.89 -66.34
REMARK 500 1 ALA A 99 -179.98 -172.13
REMARK 500 1 ILE A 100 69.92 31.33
REMARK 500 2 GLU A 11 -73.86 79.00
REMARK 500 2 LEU A 17 -150.84 -59.69
REMARK 500 2 LYS A 18 12.55 58.46
REMARK 500 2 LYS A 19 -98.02 -66.41
REMARK 500 2 ASN A 21 -29.39 159.32
REMARK 500 2 ALA A 29 -164.10 160.04
REMARK 500 2 ALA A 30 -144.38 179.01
REMARK 500 2 LYS A 31 108.85 177.50
REMARK 500 2 LYS A 37 81.37 175.53
REMARK 500 2 SER A 44 -162.41 -171.43
REMARK 500 2 ALA A 50 -38.07 -39.49
REMARK 500 2 ALA A 51 -85.67 -51.39
REMARK 500 2 ARG A 56 -42.04 -158.59
REMARK 500 2 ALA A 58 -179.97 160.13
REMARK 500 2 VAL A 72 55.25 -68.33
REMARK 500 2 LEU A 74 -76.58 -110.24
REMARK 500 2 SER A 75 127.92 152.84
REMARK 500 2 GLN A 76 -36.06 -39.92
REMARK 500 2 THR A 84 -80.02 -66.67
REMARK 500 2 ARG A 85 60.89 -67.70
REMARK 500 2 SER A 87 -178.61 81.55
REMARK 500 2 SER A 88 3.50 -61.73
REMARK 500 2 LYS A 96 -63.44 -179.13
REMARK 500 2 GLN A 97 109.83 69.81
REMARK 500 2 ALA A 99 105.95 57.44
REMARK 500 3 LEU A 6 64.97 61.62
REMARK 500 3 GLU A 9 89.02 64.97
REMARK 500
REMARK 500 THIS ENTRY HAS 459 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1XZ9 A 6 101 UNP Q5TIG6 Q5TIG6_HUMAN 985 1079
SEQADV 1XZ9 GLY A 1 UNP Q5TIG6 CLONING ARTIFACT
SEQADV 1XZ9 PRO A 2 UNP Q5TIG6 CLONING ARTIFACT
SEQADV 1XZ9 LEU A 3 UNP Q5TIG6 CLONING ARTIFACT
SEQADV 1XZ9 GLY A 4 UNP Q5TIG6 CLONING ARTIFACT
SEQADV 1XZ9 SER A 5 UNP Q5TIG6 CLONING ARTIFACT
SEQADV 1XZ9 VAL A 53 UNP Q5TIG6 SEE REMARK 999
SEQRES 1 A 101 GLY PRO LEU GLY SER LEU ARG LYS GLU PRO GLU ILE ILE
SEQRES 2 A 101 THR VAL THR LEU LYS LYS GLN ASN GLY MET GLY LEU SER
SEQRES 3 A 101 ILE VAL ALA ALA LYS GLY ALA GLY GLN ASP LYS LEU GLY
SEQRES 4 A 101 ILE TYR VAL LYS SER VAL VAL LYS GLY GLY ALA ALA ASP
SEQRES 5 A 101 VAL ASP GLY ARG LEU ALA ALA GLY ASP GLN LEU LEU SER
SEQRES 6 A 101 VAL ASP GLY ARG SER LEU VAL GLY LEU SER GLN GLU ARG
SEQRES 7 A 101 ALA ALA GLU LEU MET THR ARG THR SER SER VAL VAL THR
SEQRES 8 A 101 LEU GLU VAL ALA LYS GLN GLY ALA ILE TYR
HELIX 1 1 GLY A 49 ASP A 54 1 6
HELIX 2 2 SER A 75 ARG A 85 1 11
SHEET 1 A 4 GLU A 11 VAL A 15 0
SHEET 2 A 4 VAL A 90 ALA A 95 -1 O VAL A 90 N VAL A 15
SHEET 3 A 4 GLN A 62 VAL A 66 -1 N LEU A 64 O GLU A 93
SHEET 4 A 4 ARG A 69 SER A 70 -1 O ARG A 69 N VAL A 66
SHEET 1 B 2 LEU A 25 VAL A 28 0
SHEET 2 B 2 TYR A 41 VAL A 45 -1 O SER A 44 N SER A 26
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 2 2 Bytes