Header list of 1nau.pdb file
Complete list - 27 20 Bytes
HEADER HORMONE/GROWTH FACTOR 28-NOV-02 1NAU
TITLE NMR SOLUTION STRUCTURE OF THE GLUCAGON ANTAGONIST [DESHIS1, DESPHE6,
TITLE 2 GLU9]GLUCAGON AMIDE IN THE PRESENCE OF PERDEUTERATED
TITLE 3 DODECYLPHOSPHOCHOLINE MICELLES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCAGON;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GLICENTIN-RELATED POLYPEPTIDE (GRPP);
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE WAS CHEMICALLY SYNTHESIZED. IT WAS
SOURCE 4 OBTAINED BY MODIFYING THE SEQUENCE OF GLUCAGON, WHICH OCCURS
SOURCE 5 NATURALLY IN HOMO SAPIENS (HUMAN).
KEYWDS HELIX, TURN, HORMONE-GROWTH FACTOR COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 16
MDLTYP MINIMIZED AVERAGE
AUTHOR J.YING,J.-M.AHN,N.E.JACOBSEN,M.F.BROWN,V.J.HRUBY
REVDAT 3 27-OCT-21 1NAU 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1NAU 1 VERSN
REVDAT 1 18-MAR-03 1NAU 0
JRNL AUTH J.YING,J.-M.AHN,N.E.JACOBSEN,M.F.BROWN,V.J.HRUBY
JRNL TITL NMR SOLUTION STRUCTURE OF THE GLUCAGON ANTAGONIST [DESHIS1,
JRNL TITL 2 DESPHE6, GLU9]GLUCAGON AMIDE IN THE PRESENCE OF
JRNL TITL 3 PERDEUTERATED DODECYLPHOSPHOCHOLINE MICELLES
JRNL REF BIOCHEMISTRY V. 42 2825 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12627948
JRNL DOI 10.1021/BI026629R
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : UXNMR, DISCOVER WITHIN INSIGHTII 2000
REMARK 3 AUTHORS : BRUKER (UXNMR), ACCELRYS (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 486 RESTRAINTS, 475 ARE NOE-DERIVED DISTANCE RESTRAINTS, 11
REMARK 3 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1NAU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-DEC-02.
REMARK 100 THE DEPOSITION ID IS D_1000017723.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE; 1MM
REMARK 210 SODIUM AZIDE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 7MM [DESHIS1, DESPHE6,
REMARK 210 GLU9]GLUCAGON AMIDE; 50 MM
REMARK 210 SODIUM PHOSPHATE BUFFER; 283 MM
REMARK 210 DODECYLPHOSPHOCHOLINE-D38
REMARK 210 MICELLES; 1 MM SODIUM AZIDE; 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000, DGII WITHIN
REMARK 210 INSIGHTII 2000
REMARK 210 METHOD USED : DISTANCE GEOMETRY, RESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : 15 STRUCTURES WITH THE LOWEST
REMARK 210 RESTRAINT ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: 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 THR A 5 -109.24 41.92
REMARK 500 1 ASP A 13 -115.87 -82.79
REMARK 500 1 SER A 14 -114.11 -96.68
REMARK 500 2 GLN A 2 -46.58 -164.39
REMARK 500 2 THR A 4 -149.29 -149.91
REMARK 500 2 GLU A 7 58.48 -90.37
REMARK 500 2 TYR A 8 -69.18 -160.07
REMARK 500 2 ARG A 15 -49.83 -171.73
REMARK 500 3 ARG A 15 -55.73 -179.47
REMARK 500 4 TYR A 11 47.51 -86.69
REMARK 500 4 LEU A 12 -47.00 -134.61
REMARK 500 4 ASP A 13 -95.53 -37.88
REMARK 500 4 SER A 14 -114.93 -140.73
REMARK 500 5 TYR A 11 42.08 -85.07
REMARK 500 5 ASP A 13 -138.87 -73.66
REMARK 500 5 SER A 14 -101.58 -94.30
REMARK 500 6 THR A 4 17.50 -142.38
REMARK 500 6 THR A 5 -61.37 -147.14
REMARK 500 6 TYR A 8 -60.11 -164.99
REMARK 500 6 LEU A 12 67.28 -151.22
REMARK 500 6 ASP A 13 -130.23 -140.34
REMARK 500 7 THR A 4 36.77 -162.33
REMARK 500 7 THR A 5 -70.23 -143.52
REMARK 500 7 ASP A 13 -123.06 -74.93
REMARK 500 7 SER A 14 -86.54 -120.51
REMARK 500 8 THR A 4 -95.48 -100.63
REMARK 500 8 GLU A 7 -73.27 -89.58
REMARK 500 8 ASP A 13 -118.83 -78.45
REMARK 500 8 SER A 14 -108.09 -100.73
REMARK 500 9 ASP A 13 -137.80 -70.98
REMARK 500 9 SER A 14 -106.72 -89.99
REMARK 500 10 THR A 4 -58.95 -156.28
REMARK 500 10 LEU A 12 -44.80 -138.44
REMARK 500 10 ASP A 13 -92.43 -40.34
REMARK 500 10 SER A 14 -103.96 -150.09
REMARK 500 11 THR A 5 -96.31 49.68
REMARK 500 11 TYR A 11 53.44 -91.03
REMARK 500 11 ASP A 13 -124.20 -78.22
REMARK 500 11 SER A 14 -110.82 -94.28
REMARK 500 12 THR A 5 -97.21 45.76
REMARK 500 12 LEU A 12 -43.98 -141.64
REMARK 500 12 ASP A 13 -95.65 -39.57
REMARK 500 12 SER A 14 -93.87 -150.40
REMARK 500 13 THR A 4 -62.10 -157.67
REMARK 500 13 ASP A 13 -126.09 -77.03
REMARK 500 13 SER A 14 -114.45 -104.62
REMARK 500 14 GLN A 2 -117.32 43.92
REMARK 500 14 GLU A 7 -61.48 -90.12
REMARK 500 14 SER A 14 -99.87 -130.29
REMARK 500 14 ARG A 15 29.32 -156.70
REMARK 500
REMARK 500 THIS ENTRY HAS 57 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 1 TYR A 11 0.09 SIDE CHAIN
REMARK 500 2 TYR A 8 0.08 SIDE CHAIN
REMARK 500 12 TYR A 11 0.06 SIDE CHAIN
REMARK 500 16 TYR A 11 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 28
DBREF 1NAU A 1 27 UNP P01275 GLUC_HUMAN 53 81
SEQADV 1NAU A UNP P01275 HIS 53 DELETION
SEQADV 1NAU A UNP P01275 PHE 58 DELETION
SEQADV 1NAU GLU A 7 UNP P01275 ASP 61 ENGINEERED MUTATION
SEQRES 1 A 28 SER GLN GLY THR THR SER GLU TYR SER LYS TYR LEU ASP
SEQRES 2 A 28 SER ARG ARG ALA GLN ASP PHE VAL GLN TRP LEU MET ASN
SEQRES 3 A 28 THR NH2
HET NH2 A 28 3
HETNAM NH2 AMINO GROUP
FORMUL 1 NH2 H2 N
HELIX 1 1 THR A 5 TYR A 11 1 7
HELIX 2 2 SER A 14 THR A 27 1 14
LINK C THR A 27 N NH2 A 28 1555 1555 1.34
SITE 1 AC1 2 ASN A 26 THR A 27
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 - 27 20 Bytes