Header list of 2exn.pdb file
Complete list - n 24 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 08-NOV-05 2EXN
TITLE SOLUTION STRUCTURE FOR THE PROTEIN CODED BY GENE LOCUS BB0938 OF
TITLE 2 BORDETELLA BRONCHISEPTICA. NORTHEAST STRUCTURAL GENOMICS TARGET
TITLE 3 BOR11.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN BOR11;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BORDETELLA BRONCHISEPTICA;
SOURCE 3 ORGANISM_TAXID: 518;
SOURCE 4 GENE: BB0938;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PMGK;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET21D;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBOR11-21
KEYWDS BETA BARREL CONTAINING FOLD; AUTOSTRUCTURE; AUTOASSIGN; NMR
KEYWDS 2 STRUCTURE; BOR11, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE
KEYWDS 3 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG, UNKNOWN
KEYWDS 4 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR P.ROSSI,T.RAMELOT,R.XIAO,C.K.HO,L.-C.MA,T.B.ACTON,M.A.KENNEDY,
AUTHOR 2 G.T.MONTELIONE,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG)
REVDAT 4 24-JAN-18 2EXN 1 AUTHOR JRNL REMARK
REVDAT 3 24-FEB-09 2EXN 1 VERSN
REVDAT 2 07-FEB-06 2EXN 1 JRNL
REVDAT 1 15-NOV-05 2EXN 0
SPRSDE 15-NOV-05 2EXN 2B2M
JRNL AUTH P.ROSSI,T.RAMELOT,R.XIAO,C.K.HO,L.-C.MA,T.B.ACTON,
JRNL AUTH 2 M.A.KENNEDY,G.T.MONTELIONE
JRNL TITL (1)H, (13)C, AND (15)N RESONANCE ASSIGNMENTS FOR THE PROTEIN
JRNL TITL 2 CODED BY GENE LOCUS BB0938 OF BORDETELLA BRONCHISEPTICA
JRNL REF J.BIOMOL.NMR V. 33 197 2005
JRNL REFN ISSN 0925-2738
JRNL PMID 16331425
JRNL DOI 10.1007/S10858-005-2593-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, CNS 1.1
REMARK 3 AUTHORS : VARIAN INC. (VNMR), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2EXN COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035219.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100 MM NACL
REMARK 210 PRESSURE : ATMOSPHERIC ATM
REMARK 210 SAMPLE CONTENTS : 0.7MM BOR11 (U-13C,15N), 0.02%
REMARK 210 NAN3, 10MM DTT, 5MM CACL2, 100MM
REMARK 210 NACL, 20MM MES, PH 6.5; 0.5MM
REMARK 210 BOR11 (U-13C,15N), 0.02% NAN3,
REMARK 210 10MM DTT, 5MM CACL2, 100MM NACL,
REMARK 210 20MM MES, PH 6.5; 0.8MM BOR11 (5%
REMARK 210 13C,U-15N), 0.02% NAN3, 10MM
REMARK 210 DTT, 5MM CACL2, 100MM NACL, 20MM
REMARK 210 MES, PH 6.5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; HNCA-J; HI-RES
REMARK 210 13C-HSQC FOR VL STEREOSPECIFIC;
REMARK 210 HET-NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 800 MHZ; 500
REMARK 210 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN; BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, NMRPIPE 2.1,
REMARK 210 AUTOSTRUCTURE 2.1.1, AUTOASSIGN
REMARK 210 1.15, SPARKY 3.91, XPLOR(NIH)
REMARK 210 2.0.6, DYANA 1.5
REMARK 210 METHOD USED : CS ASSIGNMENT: BACKBONE
REMARK 210 AUTOASSIGN, MANUAL SIDECHAIN
REMARK 210 HCCH-COSY AND TOCSYS.
REMARK 210 AUTOSTRUCTURE FOR NOESY ASSIGN.
REMARK 210 HYPER DIHEDRAL, DYANA, XPLOR(NIH)
REMARK 210 , AND CNS FORCE-FIELD FOR
REMARK 210 SIMULATED ANNEALING (DYANA,XPLOR
REMARK 210 RUN WITHIN AUTOSTRUCTURE GUI)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 56
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: AUTOQF SCORES AFTER CNS WITH EXPLICIT H2O REFINEMENT:
REMARK 210 FINAL M-SCORE: 0.188
REMARK 210 FINAL DP-SCORE: 0.73 (RECALL=0.986, PRECISION=0.857, F-MEASURE=
REMARK 210 0.917)
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-10
REMARK 465 RES C SSSEQI
REMARK 465 HIS A 131
REMARK 465 HIS A 132
REMARK 465 HIS A 133
REMARK 465 HIS A 134
REMARK 465 HIS A 135
REMARK 465 HIS A 136
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 HD1 HIS A 118 OD2 ASP A 120 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 ALA A 10 -70.95 -73.88
REMARK 500 1 GLU A 47 46.00 -95.66
REMARK 500 1 MET A 54 84.15 -67.50
REMARK 500 1 PRO A 62 81.23 -66.98
REMARK 500 1 LEU A 65 -158.64 -68.67
REMARK 500 1 LEU A 71 -74.22 -54.21
REMARK 500 1 ASP A 72 28.84 -150.73
REMARK 500 1 GLU A 75 23.82 -144.79
REMARK 500 1 ASP A 76 -160.53 -109.38
REMARK 500 1 VAL A 80 99.74 -68.35
REMARK 500 1 PRO A 111 90.88 -62.64
REMARK 500 1 ALA A 122 -77.97 67.42
REMARK 500 1 VAL A 124 -30.14 -133.90
REMARK 500 1 ARG A 125 -37.97 78.13
REMARK 500 1 TRP A 126 138.35 77.73
REMARK 500 1 SER A 128 24.12 -79.01
REMARK 500 2 SER A 2 -38.21 -131.55
REMARK 500 2 LEU A 28 -177.27 -177.78
REMARK 500 2 MET A 54 91.85 -68.38
REMARK 500 2 PRO A 62 107.08 -46.16
REMARK 500 2 LEU A 65 -165.87 -67.70
REMARK 500 2 ASP A 72 88.55 75.29
REMARK 500 2 GLU A 75 29.72 -73.53
REMARK 500 2 PRO A 111 96.71 -60.26
REMARK 500 2 GLU A 123 -140.07 65.79
REMARK 500 2 VAL A 124 100.63 65.67
REMARK 500 2 TRP A 126 151.50 72.58
REMARK 500 2 LEU A 129 79.78 64.64
REMARK 500 3 SER A 2 -158.72 62.57
REMARK 500 3 THR A 16 31.66 -87.41
REMARK 500 3 GLU A 47 54.62 -92.68
REMARK 500 3 PRO A 62 98.03 -60.95
REMARK 500 3 LEU A 65 -154.38 -69.71
REMARK 500 3 ILE A 74 -85.48 -86.15
REMARK 500 3 GLU A 88 16.08 -143.81
REMARK 500 3 PRO A 111 97.91 -55.20
REMARK 500 3 GLU A 123 -135.00 -140.37
REMARK 500 3 VAL A 124 94.44 67.34
REMARK 500 3 TRP A 126 151.56 70.61
REMARK 500 3 PRO A 127 120.50 -37.02
REMARK 500 3 SER A 128 40.35 -96.07
REMARK 500 4 THR A 4 -137.61 40.34
REMARK 500 4 ALA A 10 -73.03 -72.89
REMARK 500 4 GLU A 47 38.97 -85.69
REMARK 500 4 MET A 54 98.13 -59.81
REMARK 500 4 PRO A 62 102.74 -57.71
REMARK 500 4 LEU A 65 -159.10 -69.99
REMARK 500 4 ASP A 76 -89.44 -87.07
REMARK 500 4 PRO A 111 90.53 -66.48
REMARK 500 4 PRO A 119 -5.36 -57.58
REMARK 500
REMARK 500 THIS ENTRY HAS 121 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6693 RELATED DB: BMRB
REMARK 900 COMPLETE NMR RESONANCE ASSIGNMENT. CONTAINS RAW DATA FILES
REMARK 900 RELATED ID: BER44 RELATED DB: TARGETDB
DBREF 2EXN A 1 120 UNP Q7WNU7 Q7WNU7_BORBR 1 120
SEQADV 2EXN MET A 121 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN ALA A 122 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN GLU A 123 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN VAL A 124 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN ARG A 125 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN TRP A 126 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN PRO A 127 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN SER A 128 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN LEU A 129 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN GLU A 130 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN HIS A 131 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN HIS A 132 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN HIS A 133 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN HIS A 134 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN HIS A 135 UNP Q7WNU7 EXPRESSION TAG
SEQADV 2EXN HIS A 136 UNP Q7WNU7 EXPRESSION TAG
SEQRES 1 A 136 MET SER THR THR ALA TYR GLN PRO ILE ALA GLU CYS GLY
SEQRES 2 A 136 ALA THR THR GLN SER GLU ALA ALA ALA TYR GLN LYS ARG
SEQRES 3 A 136 TRP LEU VAL ALA ASN ASP ALA GLY GLN TRP LEU ASN ARG
SEQRES 4 A 136 ASP LEU CYS PRO ARG LEU ALA GLU VAL SER VAL GLU LEU
SEQRES 5 A 136 ARG MET GLY TYR LEU VAL LEU LYS ALA PRO GLY MET LEU
SEQRES 6 A 136 ARG LEU ASP ILE PRO LEU ASP VAL ILE GLU ASP ASP ASP
SEQRES 7 A 136 SER VAL ARG TYR GLN MET LEU VAL GLY GLU GLN THR VAL
SEQRES 8 A 136 ASP VAL VAL ASP GLU GLY GLU LEU ALA ALA ALA TRP ILE
SEQRES 9 A 136 SER ASN HIS ALA GLY VAL PRO CYS ARG ILE LEU LYS VAL
SEQRES 10 A 136 HIS PRO ASP MET ALA GLU VAL ARG TRP PRO SER LEU GLU
SEQRES 11 A 136 HIS HIS HIS HIS HIS HIS
HELIX 1 1 GLN A 17 TYR A 23 5 7
HELIX 2 2 CYS A 42 GLU A 47 5 6
HELIX 3 3 GLY A 97 ALA A 108 1 12
SHEET 1 A 2 TYR A 6 ILE A 9 0
SHEET 2 A 2 GLY A 13 THR A 15 -1 O THR A 15 N TYR A 6
SHEET 1 B 5 TRP A 36 LEU A 37 0
SHEET 2 B 5 TRP A 27 ASN A 31 -1 N VAL A 29 O LEU A 37
SHEET 3 B 5 CYS A 112 VAL A 117 -1 O LEU A 115 N LEU A 28
SHEET 4 B 5 GLN A 89 VAL A 94 -1 N VAL A 94 O LYS A 116
SHEET 5 B 5 TYR A 82 VAL A 86 -1 N TYR A 82 O VAL A 93
SHEET 1 C 3 SER A 49 LEU A 52 0
SHEET 2 C 3 TYR A 56 LYS A 60 -1 O LYS A 60 N SER A 49
SHEET 3 C 3 ARG A 66 PRO A 70 -1 O ILE A 69 N LEU A 57
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 - n 24 2 Bytes