Header list of 1nyo.pdb file
Complete list - b 23 2 Bytes
HEADER IMMUNE SYSTEM 13-FEB-03 1NYO
TITLE SOLUTION STRUCTURE OF THE ANTIGENIC TB PROTEIN MPT70/MPB70
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: IMMUNOGENIC PROTEIN MPT70;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MYCOBACTERIAL PROTEIN MPT70, MPB70;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;
SOURCE 3 ORGANISM_TAXID: 1773;
SOURCE 4 GENE: MPT70/MPB70;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBLUESCRIPT KS+
KEYWDS SEVEN-STRANDED BETA-BARREL, FASCICLIN DOMAIN, STRUCTURAL GENOMICS,
KEYWDS 2 PSI, PROTEIN STRUCTURE INITIATIVE, TB STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, TBSGC, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 38
AUTHOR M.J.BLOEMINK,E.DENTTEN,R.G.HEWINSON,R.A.WILLIAMSON,M.D.CARR,TB
AUTHOR 2 STRUCTURAL GENOMICS CONSORTIUM (TBSGC)
REVDAT 5 23-FEB-22 1NYO 1 REMARK
REVDAT 4 24-FEB-09 1NYO 1 VERSN
REVDAT 3 01-FEB-05 1NYO 1 AUTHOR KEYWDS REMARK SOURCE
REVDAT 2 23-DEC-03 1NYO 1 JRNL
REVDAT 1 19-AUG-03 1NYO 0
JRNL AUTH M.D.CARR,M.J.BLOEMINK,E.DENTTEN,A.O.WHELAN,S.V.GORDON,
JRNL AUTH 2 G.KELLY,T.A.FRENKIEL,R.G.HEWINSON,R.A.WILLIAMSON
JRNL TITL SOLUTION STRUCTURE OF THE MYCOBACTERIUM TUBERCULOSIS COMPLEX
JRNL TITL 2 PROTEIN MPB70: FROM TUBERCULOSIS PATHOGENESIS TO INHERITED
JRNL TITL 3 HUMAN CORNEAL DESEASE
JRNL REF J.BIOL.CHEM. V. 278 43736 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12917404
JRNL DOI 10.1074/JBC.M307235200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.J.BLOEMINK,J.KEMMINK,E.DENTTEN,F.W.MUSKETT,A.WHELAN,
REMARK 1 AUTH 2 A.SHEIKH,G.HEWINSON,R.A.WILLIAMSON,M.D.CARR
REMARK 1 TITL SEQUENCE-SPECIFIC ASSIGNMENT AND DETERMINATION OF THE
REMARK 1 TITL 2 SECONDARY STRUCTURE OF THE 163-RESIDUE M.TUBERCULOSIS AND
REMARK 1 TITL 3 M.BOVIS ANTIGENIC PROTEIN MPB70
REMARK 1 REF J.BIOMOL.NMR V. 20 185 2001
REMARK 1 REFN ISSN 0925-2738
REMARK 1 DOI 10.1023/A:1011239727839
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, CYANA 1.0.3
REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE SOLUTION STRUCTURES ARE BASED ON A
REMARK 3 TOTAL OF 2892 NOE-DERIVED DISTANCE CONSTRAINTS, 98 DISTANCE
REMARK 3 CONSTRAINTS FROM HYDROGEN BONDS AND 35 TORSION ANGLE CONSTRAINTS
REMARK 4
REMARK 4 1NYO COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018357.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 20MM PHOSPHATE/100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7MM MPB70 U-15N,13C, 20MM
REMARK 210 PHOSPHATE BUFFER/100MM NACL;
REMARK 210 1.0MM MPB70 U-15N, 20MM
REMARK 210 PHOSPHATE BUFFER/100MM NACL;
REMARK 210 1.0MM MPB70 U-15N,U-13C (EXCEPT
REMARK 210 Y,H,F(12C)), 20MM PHOSPHATE
REMARK 210 BUFFER/100MM NACL; 1.0MM MPB70 U-
REMARK 210 14N,12C, 20MM PHOSPHATE BUFFER/
REMARK 210 100MM NACL; 1.0MM MPB70 U-14N,
REMARK 210 12C, 20MM PHOSPHATE BUFFER/100MM
REMARK 210 NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHB; 3D_15N-
REMARK 210 SEPARATED_TOCSY (SHORT TMIX); 2D
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE SGI6X, XEASY 1.3.11,
REMARK 210 CYANA 1.0.3
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS WITH
REMARK 210 SIMMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 38
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
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 HG1 THR A 72 O ILE A 155 1.40
REMARK 500 O PHE A 69 HD1 HIS A 101 1.45
REMARK 500 O TYR A 11 H ASN A 15 1.51
REMARK 500 HH TYR A 11 O ALA A 20 1.51
REMARK 500 O GLY A 7 H TYR A 11 1.52
REMARK 500 HG SER A 26 O THR A 147 1.53
REMARK 500 O PRO A 29 H ALA A 33 1.53
REMARK 500 O ALA A 81 H ASP A 85 1.57
REMARK 500 O VAL A 135 H ALA A 138 1.58
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 ALA A 9 -73.44 -68.23
REMARK 500 1 ALA A 31 -97.33 -55.98
REMARK 500 1 VAL A 32 -33.94 -38.78
REMARK 500 1 ASN A 36 -39.38 -136.49
REMARK 500 1 THR A 41 -35.52 -34.58
REMARK 500 1 ALA A 46 -71.63 -66.09
REMARK 500 1 ASN A 56 110.99 -169.73
REMARK 500 1 SER A 63 110.55 -163.16
REMARK 500 1 GLN A 65 109.06 -50.46
REMARK 500 1 THR A 67 87.97 -152.16
REMARK 500 1 THR A 72 175.55 -53.50
REMARK 500 1 THR A 89 -41.09 -160.87
REMARK 500 1 SER A 91 26.37 -159.48
REMARK 500 1 SER A 92 -44.62 -148.86
REMARK 500 1 GLN A 106 120.57 77.58
REMARK 500 1 ALA A 110 -45.51 -135.33
REMARK 500 1 LEU A 119 -30.84 -39.69
REMARK 500 1 THR A 125 96.14 -68.59
REMARK 500 1 GLN A 129 -75.36 -136.16
REMARK 500 1 ASN A 131 40.41 -91.96
REMARK 500 1 ASN A 137 -14.29 84.25
REMARK 500 1 VAL A 140 98.03 -55.50
REMARK 500 1 THR A 147 -105.04 -87.63
REMARK 500 1 ASN A 149 38.88 -150.98
REMARK 500 1 ALA A 150 141.89 -172.13
REMARK 500 1 LEU A 159 148.63 -33.24
REMARK 500 2 ASP A 2 169.74 57.62
REMARK 500 2 ALA A 9 -70.37 -84.73
REMARK 500 2 THR A 17 -157.42 -129.50
REMARK 500 2 VAL A 30 -109.22 28.65
REMARK 500 2 ALA A 31 -70.46 -11.45
REMARK 500 2 THR A 41 -39.51 -32.64
REMARK 500 2 ALA A 46 -71.70 -68.29
REMARK 500 2 GLN A 50 -29.47 -37.79
REMARK 500 2 LEU A 61 -38.62 -37.98
REMARK 500 2 SER A 63 109.05 -166.26
REMARK 500 2 THR A 67 87.10 -151.54
REMARK 500 2 THR A 72 -179.96 -62.57
REMARK 500 2 ALA A 81 -30.95 -39.45
REMARK 500 2 THR A 89 10.17 -141.66
REMARK 500 2 SER A 91 23.94 -144.91
REMARK 500 2 SER A 92 -45.62 -141.35
REMARK 500 2 VAL A 102 111.70 -162.58
REMARK 500 2 PRO A 109 50.00 -74.92
REMARK 500 2 ALA A 110 -46.48 -132.83
REMARK 500 2 THR A 125 73.27 -69.80
REMARK 500 2 GLN A 129 -37.59 90.45
REMARK 500 2 SER A 132 42.45 85.92
REMARK 500 2 LEU A 133 168.75 -45.11
REMARK 500 2 ASN A 137 -39.66 88.05
REMARK 500
REMARK 500 THIS ENTRY HAS 1138 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 69 ALA A 70 1 -138.30
REMARK 500 PHE A 69 ALA A 70 2 -139.98
REMARK 500 PHE A 69 ALA A 70 3 -136.92
REMARK 500 PHE A 69 ALA A 70 4 -139.21
REMARK 500 PHE A 69 ALA A 70 5 -138.59
REMARK 500 PHE A 69 ALA A 70 6 -136.03
REMARK 500 PHE A 69 ALA A 70 7 -139.53
REMARK 500 PHE A 69 ALA A 70 8 -137.08
REMARK 500 PHE A 69 ALA A 70 9 -138.85
REMARK 500 ASN A 36 ASN A 37 10 139.99
REMARK 500 PHE A 69 ALA A 70 10 -137.24
REMARK 500 PHE A 69 ALA A 70 11 -135.31
REMARK 500 PHE A 69 ALA A 70 12 -137.35
REMARK 500 PHE A 69 ALA A 70 13 -139.35
REMARK 500 PHE A 69 ALA A 70 14 -140.61
REMARK 500 PHE A 69 ALA A 70 15 -140.30
REMARK 500 PHE A 69 ALA A 70 16 -135.68
REMARK 500 PHE A 69 ALA A 70 17 -136.51
REMARK 500 PHE A 69 ALA A 70 18 -137.66
REMARK 500 PHE A 69 ALA A 70 19 -135.98
REMARK 500 ASN A 36 ASN A 37 20 146.95
REMARK 500 PHE A 69 ALA A 70 20 -136.51
REMARK 500 ASN A 36 ASN A 37 21 127.26
REMARK 500 PHE A 69 ALA A 70 21 -138.65
REMARK 500 PHE A 69 ALA A 70 22 -137.72
REMARK 500 PHE A 69 ALA A 70 23 -141.45
REMARK 500 PHE A 69 ALA A 70 24 -136.07
REMARK 500 PHE A 69 ALA A 70 25 -139.43
REMARK 500 PHE A 69 ALA A 70 26 -135.48
REMARK 500 PHE A 69 ALA A 70 27 -137.84
REMARK 500 PHE A 69 ALA A 70 28 -135.58
REMARK 500 PHE A 69 ALA A 70 29 -136.30
REMARK 500 PHE A 69 ALA A 70 30 -136.47
REMARK 500 VAL A 4 GLY A 5 31 144.51
REMARK 500 PHE A 69 ALA A 70 31 -139.79
REMARK 500 PHE A 69 ALA A 70 32 -138.35
REMARK 500 ASN A 36 ASN A 37 33 129.96
REMARK 500 PHE A 69 ALA A 70 33 -139.39
REMARK 500 PHE A 69 ALA A 70 34 -137.55
REMARK 500 PHE A 69 ALA A 70 35 -138.62
REMARK 500 PHE A 69 ALA A 70 36 -137.32
REMARK 500 PHE A 69 ALA A 70 37 -138.50
REMARK 500 ASN A 36 ASN A 37 38 128.82
REMARK 500 PHE A 69 ALA A 70 38 -137.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: RV2875 RELATED DB: TARGETDB
DBREF 1NYO A 1 163 UNP P0A668 MP70_MYCTU 31 193
SEQRES 1 A 163 GLY ASP LEU VAL GLY PRO GLY CYS ALA GLU TYR ALA ALA
SEQRES 2 A 163 ALA ASN PRO THR GLY PRO ALA SER VAL GLN GLY MET SER
SEQRES 3 A 163 GLN ASP PRO VAL ALA VAL ALA ALA SER ASN ASN PRO GLU
SEQRES 4 A 163 LEU THR THR LEU THR ALA ALA LEU SER GLY GLN LEU ASN
SEQRES 5 A 163 PRO GLN VAL ASN LEU VAL ASP THR LEU ASN SER GLY GLN
SEQRES 6 A 163 TYR THR VAL PHE ALA PRO THR ASN ALA ALA PHE SER LYS
SEQRES 7 A 163 LEU PRO ALA SER THR ILE ASP GLU LEU LYS THR ASN SER
SEQRES 8 A 163 SER LEU LEU THR SER ILE LEU THR TYR HIS VAL VAL ALA
SEQRES 9 A 163 GLY GLN THR SER PRO ALA ASN VAL VAL GLY THR ARG GLN
SEQRES 10 A 163 THR LEU GLN GLY ALA SER VAL THR VAL THR GLY GLN GLY
SEQRES 11 A 163 ASN SER LEU LYS VAL GLY ASN ALA ASP VAL VAL CYS GLY
SEQRES 12 A 163 GLY VAL SER THR ALA ASN ALA THR VAL TYR MET ILE ASP
SEQRES 13 A 163 SER VAL LEU MET PRO PRO ALA
HELIX 1 1 PRO A 6 ASN A 15 1 10
HELIX 2 2 GLN A 23 ASP A 28 1 6
HELIX 3 3 PRO A 29 SER A 35 1 7
HELIX 4 4 LEU A 40 GLY A 49 1 10
HELIX 5 5 LEU A 57 ASN A 62 1 6
HELIX 6 6 THR A 72 LEU A 79 1 8
HELIX 7 7 PRO A 80 LYS A 88 1 9
HELIX 8 8 SER A 92 HIS A 101 1 10
SHEET 1 A 3 VAL A 102 ALA A 104 0
SHEET 2 A 3 TYR A 66 VAL A 68 -1 N THR A 67 O VAL A 103
SHEET 3 A 3 ALA A 150 VAL A 152 1 O THR A 151 N VAL A 68
SHEET 1 B 4 GLY A 114 GLN A 117 0
SHEET 2 B 4 SER A 123 GLY A 128 -1 O VAL A 126 N GLY A 114
SHEET 3 B 4 LEU A 133 VAL A 135 -1 O LYS A 134 N THR A 127
SHEET 4 B 4 ALA A 138 ASP A 139 -1 O ALA A 138 N VAL A 135
SSBOND 1 CYS A 8 CYS A 142 1555 1555 1.95
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 - b 23 2 Bytes