HEADER ANK-REPEAT 17-AUG-98 1MYO
TITLE SOLUTION STRUCTURE OF MYOTROPHIN, NMR, 44 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOTROPHIN;
COMPND 3 CHAIN: A
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 ORGAN: HEART
KEYWDS MYOTROPHIN, ACETYLATION, ANK-REPEAT
EXPDTA SOLUTION NMR
NUMMDL 44
AUTHOR Y.YANG,S.NANDURI,S.SEN,J.QIN
REVDAT 3 23-FEB-22 1MYO 1 REMARK
REVDAT 2 24-FEB-09 1MYO 1 VERSN
REVDAT 1 17-AUG-99 1MYO 0
JRNL AUTH Y.YANG,S.NANDURI,S.SEN,J.QIN
JRNL TITL THE STRUCTURAL BASIS OF ANKYRIN-LIKE REPEAT FUNCTION AS
JRNL TITL 2 REVEALED BY THE SOLUTION STRUCTURE OF MYOTROPHIN.
JRNL REF STRUCTURE V. 6 619 1998
JRNL REFN ISSN 0969-2126
JRNL PMID 9634699
JRNL DOI 10.1016/S0969-2126(98)00063-X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.YANG,N.S.RAO,E.WALKER,S.SEN,J.QIN
REMARK 1 TITL NUCLEAR MAGNETIC RESONANCE ASSIGNMENT AND SECONDARY
REMARK 1 TITL 2 STRUCTURE OF AN ANKYRIN-LIKE REPEAT-BEARING PROTEIN:
REMARK 1 TITL 3 MYOTROPHIN
REMARK 1 REF PROTEIN SCI. V. 6 1347 1997
REMARK 1 REFN ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MYO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175194.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 297
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 50 MM PHOSPATE BUFFER
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D- AND 4D-NOESY; 3D-TOCSY;
REMARK 210 HNCACB; HNHA; C(CO)NH; H(CCO)NH;
REMARK 210 HCCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA600
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 : 90
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 44
REMARK 210 CONFORMERS, SELECTION CRITERIA : RESTRAINT VIOLATION
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 HD21 ASN A 62 H ALA A 63 1.21
REMARK 500 O GLY A 13 H LEU A 15 1.37
REMARK 500 O ASP A 3 H MET A 7 1.45
REMARK 500 O ASP A 14 H GLU A 17 1.50
REMARK 500 O LYS A 4 H TRP A 8 1.57
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 CYS A 2 48.46 -165.50
REMARK 500 1 TRP A 8 -11.67 -48.53
REMARK 500 1 ASN A 12 21.88 -79.03
REMARK 500 1 ASP A 14 46.60 -67.21
REMARK 500 1 LEU A 15 -33.73 -39.55
REMARK 500 1 LYS A 24 -80.06 -64.55
REMARK 500 1 GLU A 26 104.92 33.26
REMARK 500 1 ASP A 27 33.15 -147.66
REMARK 500 1 ASN A 29 33.22 -173.50
REMARK 500 1 THR A 31 100.83 -59.10
REMARK 500 1 GLU A 33 -85.16 -84.59
REMARK 500 1 PRO A 38 21.02 -66.76
REMARK 500 1 CYS A 45 60.06 -163.06
REMARK 500 1 GLN A 47 15.88 47.85
REMARK 500 1 LEU A 48 -1.86 63.89
REMARK 500 1 PHE A 53 -83.71 -64.48
REMARK 500 1 LEU A 54 -5.74 -53.27
REMARK 500 1 LYS A 57 -103.38 -67.34
REMARK 500 1 ALA A 59 72.62 170.67
REMARK 500 1 ASP A 60 5.02 -69.41
REMARK 500 1 ASN A 62 -35.22 -146.28
REMARK 500 1 ALA A 63 -58.48 -14.78
REMARK 500 1 PRO A 64 134.78 -14.47
REMARK 500 1 ASP A 65 -47.83 -145.04
REMARK 500 1 HIS A 68 32.65 34.98
REMARK 500 1 TYR A 77 39.62 -76.66
REMARK 500 1 VAL A 81 12.25 38.69
REMARK 500 1 LYS A 85 -76.70 -51.22
REMARK 500 1 LEU A 87 -77.12 -75.77
REMARK 500 1 LEU A 88 -14.37 -48.92
REMARK 500 1 ALA A 92 -0.76 48.31
REMARK 500 1 ASP A 93 -140.04 35.00
REMARK 500 1 LYS A 94 -28.78 -157.22
REMARK 500 1 LYS A 97 -3.91 -158.95
REMARK 500 1 PRO A 99 -77.04 -55.07
REMARK 500 1 ASP A 100 -131.13 -144.22
REMARK 500 1 LEU A 102 -71.49 -47.21
REMARK 500 1 THR A 103 -111.60 21.11
REMARK 500 1 LEU A 105 -73.53 -58.50
REMARK 500 1 THR A 108 -151.12 -154.87
REMARK 500 1 GLN A 111 0.20 -69.34
REMARK 500 2 CYS A 2 -21.02 -149.69
REMARK 500 2 LYS A 24 -81.03 -57.35
REMARK 500 2 GLU A 26 102.33 32.44
REMARK 500 2 ASP A 27 39.66 -146.70
REMARK 500 2 ASN A 29 37.82 -179.86
REMARK 500 2 LEU A 32 -108.47 -59.48
REMARK 500 2 CYS A 45 64.70 -156.69
REMARK 500 2 GLN A 47 13.81 53.49
REMARK 500 2 LEU A 48 7.18 59.30
REMARK 500
REMARK 500 THIS ENTRY HAS 1578 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1MYO A 2 118 UNP P62775 MTPN_RAT 1 117
SEQRES 1 A 118 MET CYS ASP LYS GLU PHE MET TRP ALA LEU LYS ASN GLY
SEQRES 2 A 118 ASP LEU ASP GLU VAL LYS ASP TYR VAL ALA LYS GLY GLU
SEQRES 3 A 118 ASP VAL ASN ARG THR LEU GLU GLY GLY ARG LYS PRO LEU
SEQRES 4 A 118 HIS TYR ALA ALA ASP CYS GLY GLN LEU GLU ILE LEU GLU
SEQRES 5 A 118 PHE LEU LEU LEU LYS GLY ALA ASP ILE ASN ALA PRO ASP
SEQRES 6 A 118 LYS HIS HIS ILE THR PRO LEU LEU SER ALA VAL TYR GLU
SEQRES 7 A 118 GLY HIS VAL SER CYS VAL LYS LEU LEU LEU SER LYS GLY
SEQRES 8 A 118 ALA ASP LYS THR VAL LYS GLY PRO ASP GLY LEU THR ALA
SEQRES 9 A 118 LEU GLU ALA THR ASP ASN GLN ALA ILE LYS ALA LEU LEU
SEQRES 10 A 118 GLN
HELIX 1 1 ASP A 3 LYS A 11 1 9
HELIX 2 2 LEU A 15 VAL A 22 1 8
HELIX 3 3 HIS A 40 CYS A 45 1 6
HELIX 4 4 ILE A 50 LEU A 56 1 7
HELIX 5 5 ASP A 60 ALA A 63 1 4
HELIX 6 6 PRO A 71 GLU A 78 1 8
HELIX 7 7 SER A 82 LEU A 88 1 7
HELIX 8 8 LYS A 114 LEU A 116 5 3
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
(ATOM LINES ARE NOT SHOWN.)
END
