Header list of 2hva.pdb file
Complete list - r 9 2 Bytes
HEADER LIGAND BINDING PROTEIN 28-JUL-06 2HVA
TITLE SOLUTION STRUCTURE OF THE HAEM-BINDING PROTEIN P22HBP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEME-BINDING PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: 22 KDA HAEM-BINDING PROTEIN, P22HBP, HEBP1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: HEBP1, HBP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: K12 BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS HAEM-BINDING PROTEIN, BETA-BETA-ALPHA-BETA-BETA REPEAT, HYDROPHOBIC-
KEYWDS 2 LIGAND BINDING DOMAIN, LIGAND BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR D.A.GELL,J.P.MACKAY,B.J.WESTMAN,C.K.LIEW,D.GORMAN
REVDAT 4 09-MAR-22 2HVA 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2HVA 1 VERSN
REVDAT 2 12-SEP-06 2HVA 1 JRNL
REVDAT 1 08-AUG-06 2HVA 0
SPRSDE 08-AUG-06 2HVA 2HC6
JRNL AUTH D.A.GELL,B.J.WESTMAN,D.GORMAN,C.K.LIEW,J.J.WELCH,M.J.WEISS,
JRNL AUTH 2 J.P.MACKAY
JRNL TITL A NOVEL HAEM-BINDING INTERFACE IN THE 22 KDA HAEM-BINDING
JRNL TITL 2 PROTEIN P22HBP.
JRNL REF J.MOL.BIOL. V. 362 287 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16905148
JRNL DOI 10.1016/J.JMB.2006.07.010
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5 PATCHLEVEL 6, CNS 1.1
REMARK 3 AUTHORS : BRUKER BIOSPIN (XWINNMR), A.T. BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HVA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000038804.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.2
REMARK 210 IONIC STRENGTH : 20MM SODIUM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM P22HBP U95%-15N, U95%-13C;
REMARK 210 20MM NA2HPO4/NAH2PO4; 0.002MM 5,5-DIMETHYLSILAPENTANESULFONATE;
REMARK 210 PH 6.2; 95% H2O, 5% D2O; 1MM P22HBP U95%-15N, U95%-13C; 20MM
REMARK 210 NA2HPO4/NAH2PO4; 0.002MM 5,5-DIMETHYLSILAPENTANESULFONATE; PH
REMARK 210 6.2; 98% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNHA; 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.110
REMARK 210 METHOD USED : SIMULATED ANNEALING WITH TORSION
REMARK 210 ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
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: THE STRUCTURE WAS DETERMINED USING STANDARD TRIPLE
REMARK 210 -RESONANCE NMR SPECTROSCOPY.
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 1-21
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -1
REMARK 465 SER A 0
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 ILE A 5 37.07 -98.99
REMARK 500 1 LEU A 9 -150.27 -169.83
REMARK 500 1 PHE A 10 -37.26 92.33
REMARK 500 1 PRO A 50 -157.49 -57.70
REMARK 500 1 THR A 69 63.26 -164.27
REMARK 500 1 LYS A 72 -46.89 -148.24
REMARK 500 1 THR A 79 110.67 -164.00
REMARK 500 1 VAL A 80 166.10 49.79
REMARK 500 1 LEU A 94 171.49 -59.10
REMARK 500 1 LYS A 96 83.50 54.94
REMARK 500 1 LYS A 97 109.31 -178.22
REMARK 500 1 SER A 111 75.39 -161.64
REMARK 500 1 ARG A 125 173.36 56.00
REMARK 500 1 GLU A 126 90.79 86.71
REMARK 500 1 LYS A 140 -65.77 -105.87
REMARK 500 1 GLU A 141 -70.19 -146.73
REMARK 500 1 GLN A 163 -76.64 -79.30
REMARK 500 1 ASP A 165 27.48 -158.01
REMARK 500 1 TYR A 172 -67.88 68.77
REMARK 500 1 MET A 176 -76.33 -120.85
REMARK 500 1 TYR A 179 19.82 59.73
REMARK 500 2 LEU A 9 173.08 59.93
REMARK 500 2 TRP A 18 69.92 62.47
REMARK 500 2 THR A 23 -45.60 -152.37
REMARK 500 2 GLU A 37 77.20 -114.75
REMARK 500 2 PRO A 50 -161.55 -55.89
REMARK 500 2 ASP A 71 -1.68 78.67
REMARK 500 2 MET A 78 -39.84 -177.87
REMARK 500 2 THR A 79 -164.52 62.14
REMARK 500 2 SER A 93 -169.85 -121.41
REMARK 500 2 GLN A 95 34.59 -98.31
REMARK 500 2 SER A 111 89.44 -167.79
REMARK 500 2 SER A 116 46.39 -94.99
REMARK 500 2 ARG A 125 150.45 62.10
REMARK 500 2 GLU A 126 -167.90 -169.14
REMARK 500 2 LYS A 140 -75.70 -105.40
REMARK 500 2 GLU A 141 -61.79 -153.37
REMARK 500 2 ALA A 160 170.98 -58.77
REMARK 500 2 ASP A 165 69.42 -159.56
REMARK 500 2 PRO A 175 109.81 -49.83
REMARK 500 2 MET A 176 -55.56 -151.32
REMARK 500 3 LEU A 2 -61.69 -127.37
REMARK 500 3 LEU A 9 -68.90 -142.29
REMARK 500 3 TRP A 18 123.94 54.21
REMARK 500 3 PRO A 50 -78.26 -61.68
REMARK 500 3 VAL A 51 -62.63 -146.73
REMARK 500 3 THR A 69 33.44 -141.45
REMARK 500 3 ASP A 71 48.39 -92.43
REMARK 500 3 LYS A 72 -46.63 -148.67
REMARK 500 3 MET A 76 146.14 62.55
REMARK 500
REMARK 500 THIS ENTRY HAS 434 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2HVA A 1 190 UNP Q9R257 HEBP1_MOUSE 1 190
SEQADV 2HVA GLY A -1 UNP Q9R257 CLONING ARTIFACT
SEQADV 2HVA SER A 0 UNP Q9R257 CLONING ARTIFACT
SEQRES 1 A 192 GLY SER MET LEU GLY MET ILE ARG ASN SER LEU PHE GLY
SEQRES 2 A 192 SER VAL GLU THR TRP PRO TRP GLN VAL LEU SER THR GLY
SEQRES 3 A 192 GLY LYS GLU ASP VAL SER TYR GLU GLU ARG ALA CYS GLU
SEQRES 4 A 192 GLY GLY LYS PHE ALA THR VAL GLU VAL THR ASP LYS PRO
SEQRES 5 A 192 VAL ASP GLU ALA LEU ARG GLU ALA MET PRO LYS ILE MET
SEQRES 6 A 192 LYS TYR VAL GLY GLY THR ASN ASP LYS GLY VAL GLY MET
SEQRES 7 A 192 GLY MET THR VAL PRO VAL SER PHE ALA VAL PHE PRO ASN
SEQRES 8 A 192 GLU ASP GLY SER LEU GLN LYS LYS LEU LYS VAL TRP PHE
SEQRES 9 A 192 ARG ILE PRO ASN GLN PHE GLN GLY SER PRO PRO ALA PRO
SEQRES 10 A 192 SER ASP GLU SER VAL LYS ILE GLU GLU ARG GLU GLY ILE
SEQRES 11 A 192 THR VAL TYR SER THR GLN PHE GLY GLY TYR ALA LYS GLU
SEQRES 12 A 192 ALA ASP TYR VAL ALA HIS ALA THR GLN LEU ARG THR THR
SEQRES 13 A 192 LEU GLU GLY THR PRO ALA THR TYR GLN GLY ASP VAL TYR
SEQRES 14 A 192 TYR CYS ALA GLY TYR ASP PRO PRO MET LYS PRO TYR GLY
SEQRES 15 A 192 ARG ARG ASN GLU VAL TRP LEU VAL LYS ALA
HELIX 1 1 PRO A 50 GLY A 67 1 18
HELIX 2 2 PRO A 105 GLY A 110 1 6
HELIX 3 3 GLU A 141 GLU A 156 1 16
SHEET 1 A 3 GLN A 19 SER A 22 0
SHEET 2 A 3 GLU A 32 CYS A 36 -1 O GLU A 33 N LEU A 21
SHEET 3 A 3 ILE A 128 SER A 132 -1 O VAL A 130 N ARG A 34
SHEET 1 B 6 VAL A 120 GLU A 124 0
SHEET 2 B 6 LYS A 40 THR A 47 -1 N THR A 43 O LYS A 121
SHEET 3 B 6 LYS A 97 ARG A 103 -1 O VAL A 100 N VAL A 44
SHEET 4 B 6 SER A 83 VAL A 86 -1 N SER A 83 O TRP A 101
SHEET 5 B 6 TYR A 167 ALA A 170 -1 O TYR A 167 N VAL A 86
SHEET 6 B 6 GLU A 184 LEU A 187 -1 O TRP A 186 N TYR A 168
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 9 2 Bytes