Header list of 1t0v.pdb file
Complete list - r 2 2 Bytes
HEADER LIGAND BINDING PROTEIN 13-APR-04 1T0V
TITLE NMR SOLUTION STRUCTURE OF THE ENGINEERED LIPOCALIN FLUA(R95K)
TITLE 2 NORTHEAST STRUCTURAL GENOMICS TARGET OR17
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BILIN-BINDING PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: BBP; ANTICALIN FLUA;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PIERIS BRASSICAE;
SOURCE 3 ORGANISM_COMMON: LARGE CABBAGE WHITE;
SOURCE 4 ORGANISM_TAXID: 7116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM83;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PBBP21-FLUA
KEYWDS PIERIS BRASSICAE, LIPOCALIN, ANTICALIN, PROTEIN ENGINEERING, BETA-
KEYWDS 2 BARREL, LIGAND BINDING PROTEIN, STRUCTURAL GENOMICS, PSI-2, PROTEIN
KEYWDS 3 STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, NESG
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.L.MILLS,G.LIU,A.SKERRA,T.SZYPERSKI,NORTHEAST STRUCTURAL GENOMICS
AUTHOR 2 CONSORTIUM (NESG)
REVDAT 4 02-MAR-22 1T0V 1 REMARK
REVDAT 3 07-APR-10 1T0V 1 JRNL KEYWDS TITLE
REVDAT 2 24-FEB-09 1T0V 1 VERSN
REVDAT 1 14-JUN-05 1T0V 0
JRNL AUTH J.L.MILLS,G.LIU,A.SKERRA,T.SZYPERSKI
JRNL TITL NMR STRUCTURE AND DYNAMICS OF THE ENGINEERED
JRNL TITL 2 FLUORESCEIN-BINDING LIPOCALIN FLUA REVEAL RIGIDIFICATION OF
JRNL TITL 3 BETA-BARREL AND VARIABLE LOOPS UPON ENTHALPY-DRIVEN LIGAND
JRNL TITL 4 BINDING.
JRNL REF BIOCHEMISTRY V. 48 7411 2009
JRNL REFN ISSN 0006-2960
JRNL PMID 19603796
JRNL DOI 10.1021/BI900535J
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, DYANA 1.5
REMARK 3 AUTHORS : VARIAN (VNMR), GUNTERT (DYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2347 RESTRAINTS, 2089 ARE
REMARK 3 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 258 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1T0V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-APR-04.
REMARK 100 THE DEPOSITION ID IS D_1000022172.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : 150 MM NACL; 10 MM NA-PO4; 50 MM
REMARK 210 BENZAMIDINE; 0.2 MM EDTA
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7 MM FLUA(R95K) U-13C,15N 150
REMARK 210 MM NACL 10 MM NA-PO4 0.2 MM EDTA
REMARK 210 50 MM BENZAMIDINE PH 6.4; 0.7 MM
REMARK 210 FLUA(R95K) U-50% 2H,15N 150 MM
REMARK 210 NACL 10 MM NA-PO4 0.2 MM EDTA 50
REMARK 210 MM BENZAMIDINE PH 6.4; 0.7 MM
REMARK 210 FLUA(R95K) U-15N 150 MM NACL 10
REMARK 210 MM NA-PO4 0.2 MM EDTA 50 MM
REMARK 210 BENZAMIDINE PH 6.4; 0.7 MM
REMARK 210 FLUA(R95K) 150 MM NACL 10 MM NA-
REMARK 210 PO4 0.2 MM EDTA 50 MM
REMARK 210 BENZAMIDINE PH 6.4; 0.7 MM
REMARK 210 FLUA(R95K) 150 MM NACL 10 MM NA-
REMARK 210 PO4 0.2 MM EDTA 50 MM
REMARK 210 BENZAMIDINE PH 6.4
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ; 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : PROSA 6.0.2, XEASY 1.3.13, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS AND
REMARK 210 SIMULATED ANNEALING (DYANA)
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 HG CYS A 42 SG CYS A 170 0.96
REMARK 500 HG CYS A 42 HG CYS A 170 1.11
REMARK 500 HH TYR A 32 HD2 ASP A 156 1.23
REMARK 500 O THR A 143 H ASN A 147 1.49
REMARK 500 H VAL A 76 O LYS A 83 1.50
REMARK 500 H GLU A 50 O SER A 53 1.54
REMARK 500 O VAL A 90 H TYR A 93 1.55
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 7 -168.75 -112.68
REMARK 500 1 TYR A 22 84.30 -57.36
REMARK 500 1 HIS A 23 -168.95 -175.61
REMARK 500 1 VAL A 29 -88.81 -126.48
REMARK 500 1 TYR A 32 136.33 -31.92
REMARK 500 1 SER A 34 171.13 56.49
REMARK 500 1 CYS A 42 46.96 -163.03
REMARK 500 1 LYS A 52 -47.45 87.14
REMARK 500 1 HIS A 63 79.84 38.45
REMARK 500 1 LYS A 65 115.79 -167.71
REMARK 500 1 LYS A 80 -78.60 -56.23
REMARK 500 1 ILE A 81 157.46 -43.02
REMARK 500 1 LEU A 102 -88.96 -37.49
REMARK 500 1 LYS A 107 -77.02 -134.17
REMARK 500 1 ASN A 108 14.32 -140.58
REMARK 500 1 LYS A 122 -58.38 80.75
REMARK 500 1 VAL A 154 -44.22 -141.14
REMARK 500 1 VAL A 155 89.78 -54.03
REMARK 500 1 LEU A 160 172.19 -53.33
REMARK 500 1 SER A 163 145.11 -36.07
REMARK 500 1 ASP A 164 83.05 176.38
REMARK 500 1 SER A 166 148.21 71.24
REMARK 500 1 ASN A 174 80.48 44.03
REMARK 500 1 ASN A 176 83.14 40.39
REMARK 500 2 CYS A 8 156.01 -45.84
REMARK 500 2 VAL A 11 116.14 -160.74
REMARK 500 2 ASN A 16 87.19 -155.93
REMARK 500 2 TYR A 22 89.86 -56.75
REMARK 500 2 HIS A 23 -175.96 -176.29
REMARK 500 2 VAL A 29 -91.11 -132.41
REMARK 500 2 SER A 34 167.32 -43.73
REMARK 500 2 LYS A 41 57.60 -117.99
REMARK 500 2 CYS A 42 57.55 -162.58
REMARK 500 2 GLU A 50 125.16 -174.16
REMARK 500 2 LYS A 52 -39.41 88.94
REMARK 500 2 HIS A 63 66.53 38.99
REMARK 500 2 LYS A 65 125.10 -170.21
REMARK 500 2 ASP A 78 107.64 -44.70
REMARK 500 2 LYS A 80 -75.17 -54.93
REMARK 500 2 ILE A 81 157.03 -38.73
REMARK 500 2 LEU A 102 -87.14 -38.07
REMARK 500 2 ASN A 106 63.57 38.59
REMARK 500 2 LYS A 107 -69.47 -135.38
REMARK 500 2 ASN A 108 -42.17 -133.55
REMARK 500 2 LYS A 122 -60.68 78.79
REMARK 500 2 VAL A 155 103.59 -51.59
REMARK 500 2 LEU A 160 166.79 -44.65
REMARK 500 2 SER A 163 157.47 -39.44
REMARK 500 2 ASP A 164 98.59 167.51
REMARK 500 2 SER A 166 149.69 74.02
REMARK 500
REMARK 500 THIS ENTRY HAS 573 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5756 RELATED DB: BMRB
REMARK 900 1H, 13C, AND 15N RESONANCE ASSIGNMENTS
REMARK 900 RELATED ID: 1N0S RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF THE HOLO PROTEIN
REMARK 900 RELATED ID: 1BBP RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF THE NATIVE HOLO PROTEIN
REMARK 900 RELATED ID: OR17 RELATED DB: TARGETDB
DBREF 1T0V A 1 174 UNP P09464 BBP_PIEBR 16 189
SEQADV 1T0V ASP A 1 UNP P09464 ASN 16 SEE REMARK 999
SEQADV 1T0V GLN A 21 UNP P09464 ASN 36 SEE REMARK 999
SEQADV 1T0V SER A 34 UNP P09464 ASN 49 SEE REMARK 999
SEQADV 1T0V PRO A 35 UNP P09464 SER 50 SEE REMARK 999
SEQADV 1T0V ASN A 36 UNP P09464 VAL 51 SEE REMARK 999
SEQADV 1T0V GLY A 37 UNP P09464 GLU 52 SEE REMARK 999
SEQADV 1T0V ARG A 58 UNP P09464 ASN 73 SEE REMARK 999
SEQADV 1T0V ASP A 60 UNP P09464 HIS 75 SEE REMARK 999
SEQADV 1T0V MET A 69 UNP P09464 ILE 84 SEE REMARK 999
SEQADV 1T0V SER A 87 UNP P09464 LYS 102 SEE REMARK 999
SEQADV 1T0V ARG A 88 UNP P09464 LEU 103 SEE REMARK 999
SEQADV 1T0V VAL A 90 UNP P09464 TYR 105 SEE REMARK 999
SEQADV 1T0V TYR A 93 UNP P09464 VAL 108 SEE REMARK 999
SEQADV 1T0V LYS A 96 UNP P09464 GLU 111 SEE REMARK 999
SEQADV 1T0V THR A 97 UNP P09464 ASN 112 SEE REMARK 999
SEQADV 1T0V SER A 114 UNP P09464 TYR 129 SEE REMARK 999
SEQADV 1T0V ARG A 116 UNP P09464 LYS 131 SEE REMARK 999
SEQADV 1T0V TRP A 125 UNP P09464 GLN 140 SEE REMARK 999
SEQADV 1T0V HIS A 127 UNP P09464 PHE 142 SEE REMARK 999
SEQADV 1T0V MET A 135 UNP P09464 LYS 150 SEE REMARK 999
SEQADV 1T0V SER A 175 UNP P09464 SEE REMARK 999
SEQADV 1T0V ASN A 176 UNP P09464 SEE REMARK 999
SEQADV 1T0V TRP A 177 UNP P09464 SEE REMARK 999
SEQADV 1T0V SER A 178 UNP P09464 SEE REMARK 999
SEQADV 1T0V HIS A 179 UNP P09464 SEE REMARK 999
SEQADV 1T0V PRO A 180 UNP P09464 SEE REMARK 999
SEQADV 1T0V GLN A 181 UNP P09464 SEE REMARK 999
SEQADV 1T0V PHE A 182 UNP P09464 SEE REMARK 999
SEQADV 1T0V GLU A 183 UNP P09464 SEE REMARK 999
SEQADV 1T0V LYS A 184 UNP P09464 SEE REMARK 999
SEQRES 1 A 184 ASP VAL TYR HIS ASP GLY ALA CYS PRO GLU VAL LYS PRO
SEQRES 2 A 184 VAL ASP ASN PHE ASP TRP SER GLN TYR HIS GLY LYS TRP
SEQRES 3 A 184 TRP GLU VAL ALA LYS TYR PRO SER PRO ASN GLY LYS TYR
SEQRES 4 A 184 GLY LYS CYS GLY TRP ALA GLU TYR THR PRO GLU GLY LYS
SEQRES 5 A 184 SER VAL LYS VAL SER ARG TYR ASP VAL ILE HIS GLY LYS
SEQRES 6 A 184 GLU TYR PHE MET GLU GLY THR ALA TYR PRO VAL GLY ASP
SEQRES 7 A 184 SER LYS ILE GLY LYS ILE TYR HIS SER ARG THR VAL GLY
SEQRES 8 A 184 GLY TYR THR LYS LYS THR VAL PHE ASN VAL LEU SER THR
SEQRES 9 A 184 ASP ASN LYS ASN TYR ILE ILE GLY TYR SER CYS ARG TYR
SEQRES 10 A 184 ASP GLU ASP LYS LYS GLY HIS TRP ASP HIS VAL TRP VAL
SEQRES 11 A 184 LEU SER ARG SER MET VAL LEU THR GLY GLU ALA LYS THR
SEQRES 12 A 184 ALA VAL GLU ASN TYR LEU ILE GLY SER PRO VAL VAL ASP
SEQRES 13 A 184 SER GLN LYS LEU VAL TYR SER ASP PHE SER GLU ALA ALA
SEQRES 14 A 184 CYS LYS VAL ASN ASN SER ASN TRP SER HIS PRO GLN PHE
SEQRES 15 A 184 GLU LYS
HELIX 1 1 GLY A 139 GLY A 151 1 13
HELIX 2 2 PHE A 165 LYS A 171 1 7
SHEET 1 A 3 TYR A 3 HIS A 4 0
SHEET 2 A 3 HIS A 124 ASP A 126 -1 O HIS A 124 N HIS A 4
SHEET 3 A 3 CYS A 115 TYR A 117 -1 N ARG A 116 O TRP A 125
SHEET 1 B 2 TRP A 27 GLU A 28 0
SHEET 2 B 2 LEU A 131 SER A 132 -1 O SER A 132 N TRP A 27
SHEET 1 C 3 GLU A 46 PRO A 49 0
SHEET 2 C 3 VAL A 54 VAL A 61 -1 O LYS A 55 N THR A 48
SHEET 3 C 3 GLU A 66 GLU A 70 -1 O TYR A 67 N ASP A 60
SHEET 1 D 3 ALA A 73 PRO A 75 0
SHEET 2 D 3 ILE A 84 VAL A 90 -1 O TYR A 85 N TYR A 74
SHEET 3 D 3 TYR A 93 PHE A 99 -1 O TYR A 93 N VAL A 90
SSBOND 1 CYS A 8 CYS A 115 1555 1555 1.92
SSBOND 2 CYS A 42 CYS A 170 1555 1555 1.99
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 - r 2 2 Bytes