Header list of 1ho9.pdb file
Complete list - 23 20 Bytes
HEADER MEMBRANE PROTEIN 10-DEC-00 1HO9
TITLE BEST 20 NMR CONFORMERS OF D130I MUTANT T3-I2, A 32 RESIDUE PEPTIDE
TITLE 2 FROM THE ALPHA 2A ADRENERGIC RECEPTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-2A ADRENERGIC RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SECOND INTRACELLULAR LOOP (RESIDUES 118-149);
COMPND 5 SYNONYM: ALPHA-2A ADRENOCEPTOR;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THE PEPTIDE OCCURS NATURALLY IN HOMO SAPIENS (HUMAN).
KEYWDS HELIX-LINKER-HELIX, MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.A.CHUNG,E.R.ZUIDERWEG,R.R.NEUBIG
REVDAT 4 23-FEB-22 1HO9 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1HO9 1 VERSN
REVDAT 2 01-APR-03 1HO9 1 JRNL
REVDAT 1 24-JUL-02 1HO9 0
JRNL AUTH D.A.CHUNG,E.R.ZUIDERWEG,C.B.FOWLER,O.S.SOYER,H.I.MOSBERG,
JRNL AUTH 2 R.R.NEUBIG
JRNL TITL NMR STRUCTURE OF THE SECOND INTRACELLULAR LOOP OF THE ALPHA
JRNL TITL 2 2A ADRENERGIC RECEPTOR: EVIDENCE FOR A NOVEL CYTOPLASMIC
JRNL TITL 3 HELIX.
JRNL REF BIOCHEMISTRY V. 41 3596 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11888275
JRNL DOI 10.1021/BI015811+
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA, DYANA
REMARK 3 AUTHORS : GUNTERT (DYANA), GUNTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HO9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-00.
REMARK 100 THE DEPOSITION ID IS D_1000012482.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303.00; 303.00
REMARK 210 PH : 4.50; 4.50
REMARK 210 IONIC STRENGTH : 50 MM NACL; 50 MM
REMARK 210 PRESSURE : NULL; NULL
REMARK 210 SAMPLE CONTENTS : 0.9 MM PEPTIDE NATURAL
REMARK 210 ABUNDANCE; 460 MM D38-
REMARK 210 DODECYLPHOSPHOCHOLINE, 50 MM
REMARK 210 NACL, 10 MM NAH2PO4, PH 4.5; 0.9
REMARK 210 MM PEPTIDE NATURAL ABUNDANCE;
REMARK 210 460 MM D38-
REMARK 210 DODECYLPHOSPHOCHOLINE, 50 MM
REMARK 210 NACL, 10 MM NAH2PO4, PH 4.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 2D COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY, NMRPIPE, NMRVIEW, SPSCAN
REMARK 210 METHOD USED : SIMULATED ANNEALING IN TORSION
REMARK 210 ANGLE SPACE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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
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 17 67.58 -67.99
REMARK 500 1 ILE A 18 -44.88 -160.39
REMARK 500 1 ALA A 21 69.23 -108.82
REMARK 500 1 ARG A 28 166.33 -43.95
REMARK 500 1 THR A 29 66.19 62.03
REMARK 500 1 ARG A 31 142.32 61.10
REMARK 500 2 CYS A 8 -63.59 -145.98
REMARK 500 2 SER A 11 44.97 -91.17
REMARK 500 2 SER A 17 70.23 -67.07
REMARK 500 2 ILE A 18 -43.82 -164.53
REMARK 500 2 ILE A 22 -70.95 -151.30
REMARK 500 2 THR A 29 69.66 62.70
REMARK 500 2 ARG A 31 101.04 51.72
REMARK 500 3 CYS A 8 -65.73 -152.13
REMARK 500 3 SER A 11 37.10 -91.15
REMARK 500 3 ILE A 13 -50.83 -138.90
REMARK 500 3 TYR A 15 32.30 -95.02
REMARK 500 3 ILE A 18 -47.37 -144.20
REMARK 500 3 ALA A 21 66.39 -103.52
REMARK 500 3 LEU A 26 -70.77 -44.43
REMARK 500 3 THR A 29 87.36 -157.78
REMARK 500 3 ARG A 31 136.12 -178.08
REMARK 500 4 SER A 17 63.77 -69.00
REMARK 500 4 ILE A 18 -46.01 -155.43
REMARK 500 4 ALA A 21 56.31 -116.48
REMARK 500 4 ILE A 22 -62.11 -147.08
REMARK 500 4 LEU A 26 53.88 -91.66
REMARK 500 4 LYS A 27 64.92 -177.20
REMARK 500 4 ARG A 31 96.75 -179.97
REMARK 500 5 SER A 17 79.33 -62.79
REMARK 500 5 ILE A 18 -39.43 -176.75
REMARK 500 5 ALA A 21 68.25 -115.80
REMARK 500 5 LYS A 27 67.08 -174.43
REMARK 500 5 THR A 29 81.04 52.13
REMARK 500 6 CYS A 8 -63.39 -154.99
REMARK 500 6 SER A 11 44.55 -104.67
REMARK 500 6 ILE A 13 -74.22 -54.51
REMARK 500 6 ARG A 14 -29.91 -38.83
REMARK 500 6 TYR A 15 43.68 -90.78
REMARK 500 6 ILE A 18 -47.34 -145.36
REMARK 500 6 ALA A 21 67.18 -112.22
REMARK 500 6 ILE A 22 -59.76 -131.15
REMARK 500 6 LEU A 26 59.27 -105.17
REMARK 500 6 LYS A 27 64.94 -173.64
REMARK 500 7 SER A 17 70.92 -66.63
REMARK 500 7 ILE A 18 -39.19 -177.07
REMARK 500 7 ILE A 22 -58.76 -128.02
REMARK 500 7 ARG A 31 110.00 172.80
REMARK 500 8 SER A 11 35.66 -99.26
REMARK 500 8 ILE A 13 -79.32 -63.99
REMARK 500
REMARK 500 THIS ENTRY HAS 144 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1HLL RELATED DB: PDB
REMARK 900 MEAN STRUCTURE OF WILD-TYPE T3-I2 PEPTIDE
REMARK 900 RELATED ID: 1HOF RELATED DB: PDB
REMARK 900 BEST 20 DYANA CONFORMERS OF WILD-TYPE T3-I2 PEPTIDE
REMARK 900 RELATED ID: 1HOD RELATED DB: PDB
REMARK 900 MEAN STRUCTURE OF D130I MUTANT T3-I2 PEPTIDE
DBREF 1HO9 A 1 32 UNP P08913 ADA2A_HUMAN 118 149
SEQADV 1HO9 ILE A 13 UNP P08913 ASP 130 CONFLICT
SEQRES 1 A 32 THR SER SER ILE VAL HIS LEU CYS ALA ILE SER LEU ILE
SEQRES 2 A 32 ARG TYR TRP SER ILE THR GLN ALA ILE GLU TYR ASN LEU
SEQRES 3 A 32 LYS ARG THR PRO ARG ARG
HELIX 1 1 THR A 1 TYR A 15 1 15
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 - 23 20 Bytes