Header list of 1nnv.pdb file
Complete list - b 23 2 Bytes
HEADER UNKNOWN FUNCTION 14-JAN-03 1NNV
TITLE THE SOLUTION STRUCTURE OF HI1450
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN HI1450;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;
SOURCE 3 ORGANISM_TAXID: 727;
SOURCE 4 GENE: HI1450;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS HYPOTHETICAL PROTEIN, STRUCTURE 2 FUNCTION PROJECT, S2F, STRUCTURAL
KEYWDS 2 GENOMICS, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.M.PARSONS,J.ORBAN,STRUCTURE 2 FUNCTION PROJECT (S2F)
REVDAT 4 23-FEB-22 1NNV 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1NNV 1 VERSN
REVDAT 2 24-FEB-04 1NNV 1 JRNL
REVDAT 1 27-JAN-04 1NNV 0
JRNL AUTH L.M.PARSONS,D.C.YEH,J.ORBAN
JRNL TITL SOLUTION STRUCTURE OF THE HIGHLY ACIDIC PROTEIN HI1450 FROM
JRNL TITL 2 HAEMOPHILUS INFLUENZAE, A PUTATIVE DOUBLE-STRANDED DNA
JRNL TITL 3 MIMIC.
JRNL REF PROTEINS V. 54 375 2004
JRNL REFN ISSN 0887-3585
JRNL PMID 14747986
JRNL DOI 10.1002/PROT.10607
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER ET AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1NNV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-FEB-03.
REMARK 100 THE DEPOSITION ID IS D_1000018045.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE, 100MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 50MM PHOSPHATE, 100MM NACL,90%
REMARK 210 H20, 10% D20; 50MM PHOSPHATE,
REMARK 210 100MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 2D NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1, NMRPIPE 5.0.3, SPARKY
REMARK 210 3.106, NOEID 1.0
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 65
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
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 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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
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
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 THR A 3 -155.78 -132.27
REMARK 500 1 ALA A 25 96.49 -45.59
REMARK 500 1 PHE A 41 -38.62 -163.90
REMARK 500 1 VAL A 47 68.82 -150.35
REMARK 500 1 ASP A 55 46.20 -84.89
REMARK 500 1 GLU A 57 64.39 -65.84
REMARK 500 1 GLU A 58 -48.68 -161.88
REMARK 500 1 GLU A 59 -73.16 -79.87
REMARK 500 1 VAL A 62 132.51 179.50
REMARK 500 1 GLU A 67 22.67 46.02
REMARK 500 1 ASN A 78 -164.18 -103.78
REMARK 500 1 ASP A 81 96.03 64.91
REMARK 500 1 GLU A 82 -148.32 -140.12
REMARK 500 1 MET A 83 58.28 -178.51
REMARK 500 1 ARG A 95 162.98 -44.20
REMARK 500 1 ASP A 98 116.80 61.86
REMARK 500 1 LYS A 106 89.43 36.09
REMARK 500 2 GLU A 27 -29.18 -171.64
REMARK 500 2 ASN A 38 -74.35 -82.19
REMARK 500 2 ASP A 54 36.83 -98.45
REMARK 500 2 ASP A 55 33.20 -157.12
REMARK 500 2 GLU A 58 -47.31 -160.03
REMARK 500 2 VAL A 62 139.88 164.53
REMARK 500 2 ASP A 65 108.10 -58.77
REMARK 500 2 GLU A 67 -10.53 76.03
REMARK 500 2 LEU A 76 50.47 -117.17
REMARK 500 2 VAL A 77 171.81 -43.23
REMARK 500 2 ASN A 78 -165.95 -120.86
REMARK 500 2 MET A 83 94.29 30.11
REMARK 500 2 ARG A 95 177.35 -55.74
REMARK 500 2 ASP A 98 112.23 64.16
REMARK 500 3 ALA A 25 -174.52 -57.40
REMARK 500 3 GLU A 27 -28.74 -157.84
REMARK 500 3 GLN A 40 -146.16 -101.91
REMARK 500 3 PHE A 41 -58.20 70.61
REMARK 500 3 ARG A 44 52.14 -119.08
REMARK 500 3 ASP A 55 44.37 -92.98
REMARK 500 3 GLU A 57 61.35 -68.27
REMARK 500 3 GLU A 58 -46.08 -162.63
REMARK 500 3 GLU A 59 -78.52 -75.74
REMARK 500 3 VAL A 62 146.05 170.67
REMARK 500 3 ASP A 65 106.29 -55.56
REMARK 500 3 GLU A 67 -9.24 75.25
REMARK 500 3 ASN A 78 -168.12 -118.53
REMARK 500 3 ASP A 81 72.60 69.51
REMARK 500 3 ARG A 95 174.31 -54.06
REMARK 500 3 GLU A 96 -65.49 -98.67
REMARK 500 3 ASP A 98 112.94 63.20
REMARK 500 4 THR A 3 136.42 -177.13
REMARK 500 4 ALA A 25 162.50 -48.68
REMARK 500
REMARK 500 THIS ENTRY HAS 316 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HI1450 RELATED DB: TARGETDB
DBREF 1NNV A 1 107 UNP P44199 Y1450_HAEIN 1 107
SEQADV 1NNV GLY A -2 UNP P44199 CLONING ARTIFACT
SEQADV 1NNV SER A -1 UNP P44199 CLONING ARTIFACT
SEQADV 1NNV HIS A 0 UNP P44199 CLONING ARTIFACT
SEQRES 1 A 110 GLY SER HIS MET THR THR GLU ILE LYS LYS LEU ASP PRO
SEQRES 2 A 110 ASP THR ALA ILE ASP ILE ALA TYR ASP ILE PHE LEU GLU
SEQRES 3 A 110 MET ALA GLY GLU ASN LEU ASP PRO ALA ASP ILE LEU LEU
SEQRES 4 A 110 PHE ASN LEU GLN PHE GLU GLU ARG GLY GLY VAL GLU PHE
SEQRES 5 A 110 VAL GLU THR ALA ASP ASP TRP GLU GLU GLU ILE GLY VAL
SEQRES 6 A 110 LEU ILE ASP PRO GLU GLU TYR ALA GLU VAL TRP VAL GLY
SEQRES 7 A 110 LEU VAL ASN GLU GLN ASP GLU MET ASP ASP VAL PHE ALA
SEQRES 8 A 110 LYS PHE LEU ILE SER HIS ARG GLU GLU ASP ARG GLU PHE
SEQRES 9 A 110 HIS VAL ILE TRP LYS LYS
HELIX 1 1 ASP A 9 ALA A 25 1 17
HELIX 2 2 ASP A 30 GLN A 40 1 11
SHEET 1 A 4 GLY A 46 VAL A 50 0
SHEET 2 A 4 ALA A 70 GLY A 75 -1 O TRP A 73 N GLU A 48
SHEET 3 A 4 VAL A 86 ILE A 92 -1 O PHE A 90 N VAL A 72
SHEET 4 A 4 PHE A 101 TRP A 105 -1 O ILE A 104 N LYS A 89
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