Header list of 2adz.pdb file
Complete list - r 9 2 Bytes
HEADER PROTEIN BINDING 21-JUL-05 2ADZ
TITLE SOLUTION STRUCTURE OF THE JOINED PH DOMAIN OF ALPHA1-SYNTROPHIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-1-SYNTROPHIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: PH DOMAIN;
COMPND 5 SYNONYM: ALPHA-SYNTROPHIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET32A(A MODIFIED VERSION)
KEYWDS PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.YAN,W.WEN,W.XU,J.F.LONG,M.E.ADAMS,S.C.FROEHNER,M.ZHANG
REVDAT 3 09-MAR-22 2ADZ 1 REMARK
REVDAT 2 24-FEB-09 2ADZ 1 VERSN
REVDAT 1 24-JAN-06 2ADZ 0
JRNL AUTH J.YAN,W.WEN,W.XU,J.F.LONG,M.E.ADAMS,S.C.FROEHNER,M.ZHANG
JRNL TITL STRUCTURE OF THE SPLIT PH DOMAIN AND DISTINCT LIPID-BINDING
JRNL TITL 2 PROPERTIES OF THE PH-PDZ SUPRAMODULE OF ALPHA-SYNTROPHIN
JRNL REF EMBO J. V. 24 3985 2005
JRNL REFN ISSN 0261-4189
JRNL PMID 16252003
JRNL DOI 10.1038/SJ.EMBOJ.7600858
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1940 RESTRAINTS, 1776 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 84
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,80 DISTANCE RESTRAINTS FROM HYDROGEN
REMARK 3 BONDS.
REMARK 4
REMARK 4 2ADZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033780.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PROTEIN 15N; 100MM POTASSIUM
REMARK 210 PHOSPHATE PH 7.0; 1MM PROTEIN
REMARK 210 15N, 13C; 100MM POTASSIUM
REMARK 210 PHOSPHATE PH 7.0; 1MM UNLABELLED
REMARK 210 PROTEIN; 100MM POTASSIUM
REMARK 210 PHOSPHATE PH 7.0
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY; 2D
REMARK 210 TOCSY; HCCH_TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 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 : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
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 : 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: 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 LEU A 31 O SER A 42 1.60
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 2 78.53 -153.58
REMARK 500 1 ARG A 5 90.72 -65.46
REMARK 500 1 CYS A 16 41.66 -169.63
REMARK 500 1 SER A 20 -68.46 -169.93
REMARK 500 1 ALA A 22 30.58 -151.25
REMARK 500 1 TRP A 27 168.77 -48.98
REMARK 500 1 SER A 33 88.90 -69.95
REMARK 500 1 ASP A 37 38.14 -152.87
REMARK 500 1 ALA A 38 119.92 -175.20
REMARK 500 1 ASN A 58 -63.11 -108.81
REMARK 500 1 PRO A 71 -166.32 -66.53
REMARK 500 1 GLU A 72 72.58 67.21
REMARK 500 1 ALA A 73 -43.34 168.89
REMARK 500 1 GLN A 77 55.25 -95.16
REMARK 500 1 GLU A 79 39.95 -96.99
REMARK 500 1 VAL A 80 -44.76 -133.94
REMARK 500 1 TYR A 83 -168.92 55.07
REMARK 500 1 LYS A 85 -63.72 71.12
REMARK 500 1 ASN A 86 35.18 -95.91
REMARK 500 1 THR A 91 -47.37 -136.59
REMARK 500 1 PRO A 98 108.19 -57.92
REMARK 500 1 SER A 101 61.38 -166.95
REMARK 500 1 GLN A 104 116.67 -161.52
REMARK 500 1 SER A 109 -61.53 -179.50
REMARK 500 1 PRO A 110 -167.17 -71.65
REMARK 500 1 PRO A 112 -160.73 -57.71
REMARK 500 1 PRO A 114 92.56 -52.36
REMARK 500 1 ASN A 116 -56.58 -166.07
REMARK 500 1 SER A 118 -80.99 62.61
REMARK 500 1 ALA A 120 179.61 -58.99
REMARK 500 1 MET A 127 -36.29 179.30
REMARK 500 1 ALA A 128 -176.66 -53.85
REMARK 500 1 ASP A 138 73.82 59.99
REMARK 500 1 GLU A 140 -63.06 -174.88
REMARK 500 1 ALA A 149 30.40 -95.14
REMARK 500 1 ALA A 159 172.35 -54.92
REMARK 500 2 LEU A 11 103.99 -59.03
REMARK 500 2 ARG A 15 -178.07 -69.54
REMARK 500 2 CYS A 16 103.77 -174.16
REMARK 500 2 ALA A 18 154.45 61.77
REMARK 500 2 SER A 20 -67.54 -93.75
REMARK 500 2 GLU A 25 95.63 -60.23
REMARK 500 2 TRP A 27 95.57 -59.42
REMARK 500 2 PRO A 43 44.43 -75.24
REMARK 500 2 GLU A 53 89.82 -153.02
REMARK 500 2 PRO A 54 -172.91 -53.35
REMARK 500 2 GLN A 56 105.54 59.50
REMARK 500 2 PRO A 71 -168.60 -67.71
REMARK 500 2 GLU A 72 72.07 66.09
REMARK 500 2 ALA A 73 -47.19 170.64
REMARK 500
REMARK 500 THIS ENTRY HAS 733 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z87 RELATED DB: PDB
REMARK 900 THE ISOLATED PH DOMAIN OF THE PROTEIN
DBREF 2ADZ A 1 78 UNP Q61234 SNTA1_MOUSE 2 79
DBREF 2ADZ A 79 178 UNP Q61234 SNTA1_MOUSE 165 264
SEQRES 1 A 178 ALA SER GLY ARG ARG ALA PRO ARG THR GLY LEU LEU GLU
SEQRES 2 A 178 LEU ARG CYS GLY ALA GLY SER GLY ALA GLY GLY GLU ARG
SEQRES 3 A 178 TRP GLN ARG VAL LEU LEU SER LEU ALA GLU ASP ALA LEU
SEQRES 4 A 178 THR VAL SER PRO ALA ASP GLY GLU PRO GLY PRO GLU PRO
SEQRES 5 A 178 GLU PRO ALA GLN LEU ASN GLY ALA ALA GLU PRO GLY ALA
SEQRES 6 A 178 ALA PRO PRO GLN LEU PRO GLU ALA LEU LEU LEU GLN ARG
SEQRES 7 A 178 GLU VAL SER PRO TYR PHE LYS ASN SER ALA GLY GLY THR
SEQRES 8 A 178 SER VAL GLY TRP ASP SER PRO PRO ALA SER PRO LEU GLN
SEQRES 9 A 178 ARG GLN PRO SER SER PRO GLY PRO GLN PRO ARG ASN LEU
SEQRES 10 A 178 SER GLU ALA LYS HIS VAL SER LEU LYS MET ALA TYR VAL
SEQRES 11 A 178 SER ARG ARG CYS THR PRO THR ASP PRO GLU PRO ARG TYR
SEQRES 12 A 178 LEU GLU ILE CYS ALA ALA ASP GLY GLN ASP ALA VAL PHE
SEQRES 13 A 178 LEU ARG ALA LYS ASP GLU ALA SER ALA ARG SER TRP ALA
SEQRES 14 A 178 GLY ALA ILE GLN ALA GLN ILE GLY THR
HELIX 1 1 LEU A 74 VAL A 80 5 7
HELIX 2 2 ASP A 161 THR A 178 1 18
SHEET 1 A 4 ARG A 8 LEU A 14 0
SHEET 2 A 4 GLN A 28 ALA A 35 -1 O GLN A 28 N LEU A 14
SHEET 3 A 4 ALA A 38 SER A 42 -1 O THR A 40 N SER A 33
SHEET 4 A 4 LYS A 121 VAL A 123 -1 O VAL A 123 N LEU A 39
SHEET 1 B 3 TYR A 129 ARG A 133 0
SHEET 2 B 3 TYR A 143 ALA A 148 -1 O TYR A 143 N ARG A 133
SHEET 3 B 3 ASP A 153 ARG A 158 -1 O LEU A 157 N LEU A 144
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 9 2 Bytes