Header list of 2hfd.pdb file
Complete list - n 31 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 23-JUN-06 2HFD
TITLE NMR STRUCTURE OF PROTEIN HYDROGENASE-1 OPERON PROTEIN HYAE FROM
TITLE 2 ESCHERICHIA COLI: NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET
TITLE 3 ER415
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYDROGENASE-1 OPERON PROTEIN HYAE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 STRAIN: XL-10;
SOURCE 5 GENE: HYAE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)+MAGIC;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS PROTEIN STRUCTURE, NESGC, ALFA-BETA, STRUCTURAL GENOMICS, PSI-2,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, NORTHEAST STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR K.K.SINGARAPU,G.LIU,A.ELETSKY,D.PARISH,H.S.ATREYA,D.XU,H.JANJUA,
AUTHOR 2 K.CUNNINGHAM,L.C.MA,R.XIAO,J.LIU,M.BARAN,G.V.T.SWAPNA,T.ACTON,
AUTHOR 3 B.ROST,G.T.MONTELIONE,T.SZYPERSKI,NORTHEAST STRUCTURAL GENOMICS
AUTHOR 4 CONSORTIUM (NESG)
REVDAT 5 31-JAN-18 2HFD 1 AUTHOR REMARK
REVDAT 4 09-JUN-09 2HFD 1 REVDAT
REVDAT 3 24-FEB-09 2HFD 1 VERSN
REVDAT 2 20-JAN-09 2HFD 1 JRNL
REVDAT 1 22-AUG-06 2HFD 0
JRNL AUTH D.PARISH,J.BENACH,G.LIU,K.K.SINGARAPU,R.XIAO,T.ACTON,M.SU,
JRNL AUTH 2 S.BANSAL,J.H.PRESTEGARD,J.HUNT,G.T.MONTELIONE,T.SZYPERSKI
JRNL TITL PROTEIN CHAPERONES Q8ZP25_SALTY FROM SALMONELLA TYPHIMURIUM
JRNL TITL 2 AND HYAE_ECOLI FROM ESCHERICHIA COLI EXHIBIT
JRNL TITL 3 THIOREDOXIN-LIKE STRUCTURES DESPITE LACK OF CANONICAL
JRNL TITL 4 THIOREDOXIN ACTIVE SITE SEQUENCE MOTIF.
JRNL REF J.STRUCT.FUNCT.GENOM. V. 9 41 2008
JRNL REFN ISSN 1345-711X
JRNL PMID 19039680
JRNL DOI 10.1007/S10969-008-9050-Y
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2004.061.12.44, CYANA 2.1, CNS 1.1
REMARK 3 AUTHORS : DELAGLIO ET AL (NMRPIPE), GUNTERT ET AL (CYANA),
REMARK 3 BRUNGER ET AL (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1996 RESTRAINTS, 1523 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 473
REMARK 3 DIHEDRAL ANGLE RESTRAINTS,
REMARK 4
REMARK 4 2HFD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1000038285.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 100
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6MM PROTEIN HYDROGENASE-1
REMARK 210 OPERON PROTEIN HYAE; 0.02% NAN3,
REMARK 210 100MM DTT, 5MM CACL2, 100MM NACL,
REMARK 210 20MM MES, 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HNCACB; 3D CBCA(CO)NH; 3D
REMARK 210 HBHA(CO)NH; 3D HCCH-COSY; 3D_13C-
REMARK 210 SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 3D ARO NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5, AUTOSTRUCTURE 2.0.0,
REMARK 210 CYANA 1.5
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
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 : 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 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 LEU A 133
REMARK 465 GLU A 134
REMARK 465 HIS A 135
REMARK 465 HIS A 136
REMARK 465 HIS A 137
REMARK 465 HIS A 138
REMARK 465 HIS A 139
REMARK 465 HIS A 140
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 ASN A 3 72.81 67.65
REMARK 500 1 THR A 5 -57.72 -159.28
REMARK 500 1 SER A 43 -73.92 -95.13
REMARK 500 1 ARG A 47 -58.65 -175.74
REMARK 500 1 THR A 48 141.76 66.45
REMARK 500 1 GLU A 50 -97.27 -110.18
REMARK 500 1 VAL A 51 -69.59 -139.32
REMARK 500 1 ASP A 53 -22.26 72.42
REMARK 500 1 ASN A 54 99.54 83.05
REMARK 500 1 PHE A 65 78.85 -116.81
REMARK 500 1 ARG A 91 -31.33 -179.61
REMARK 500 1 ALA A 94 -175.73 -171.24
REMARK 500 1 ILE A 110 -56.82 -136.53
REMARK 500 1 GLN A 127 -41.48 71.29
REMARK 500 1 GLU A 129 121.60 76.42
REMARK 500 1 ARG A 130 36.27 -149.31
REMARK 500 2 SER A 2 89.58 -67.15
REMARK 500 2 ASP A 4 115.28 38.45
REMARK 500 2 THR A 5 -54.11 -162.00
REMARK 500 2 SER A 42 -153.31 -102.40
REMARK 500 2 SER A 43 135.24 75.28
REMARK 500 2 LYS A 46 -69.73 -98.65
REMARK 500 2 ARG A 47 -28.35 -179.45
REMARK 500 2 ASP A 53 -69.21 64.38
REMARK 500 2 PRO A 55 44.36 -79.44
REMARK 500 2 PRO A 126 99.72 -69.61
REMARK 500 2 GLN A 127 79.47 -101.84
REMARK 500 3 SER A 2 -90.61 62.69
REMARK 500 3 THR A 5 -61.74 -157.15
REMARK 500 3 ASP A 36 -158.40 68.82
REMARK 500 3 SER A 43 94.55 -69.75
REMARK 500 3 ASP A 53 -77.97 -54.40
REMARK 500 3 ASN A 54 139.19 -171.39
REMARK 500 3 PRO A 55 42.76 -103.30
REMARK 500 3 PHE A 87 -65.60 -90.85
REMARK 500 3 ALA A 94 -175.76 -171.91
REMARK 500 3 GLN A 128 91.45 57.07
REMARK 500 3 ARG A 130 -51.13 76.80
REMARK 500 3 ALA A 131 94.11 60.57
REMARK 500 4 SER A 2 -72.32 68.78
REMARK 500 4 THR A 5 -57.18 -159.29
REMARK 500 4 SER A 43 -86.43 -80.97
REMARK 500 4 ASN A 54 81.67 63.08
REMARK 500 4 HIS A 111 -54.58 -135.48
REMARK 500 4 GLU A 129 81.75 -68.71
REMARK 500 5 ASN A 3 75.94 -117.82
REMARK 500 5 ASP A 4 174.93 64.46
REMARK 500 5 THR A 5 -57.25 -160.70
REMARK 500 5 ASP A 36 167.07 73.91
REMARK 500 5 ASP A 44 80.38 53.75
REMARK 500
REMARK 500 THIS ENTRY HAS 249 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 GLU A 24 SER A 25 16 149.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: ER415 RELATED DB: TARGETDB
DBREF 2HFD A 1 132 UNP P19931 HYAE_ECOLI 1 132
SEQADV 2HFD LEU A 133 UNP P19931 CLONING ARTIFACT
SEQADV 2HFD GLU A 134 UNP P19931 CLONING ARTIFACT
SEQADV 2HFD HIS A 135 UNP P19931 EXPRESSION TAG
SEQADV 2HFD HIS A 136 UNP P19931 EXPRESSION TAG
SEQADV 2HFD HIS A 137 UNP P19931 EXPRESSION TAG
SEQADV 2HFD HIS A 138 UNP P19931 EXPRESSION TAG
SEQADV 2HFD HIS A 139 UNP P19931 EXPRESSION TAG
SEQADV 2HFD HIS A 140 UNP P19931 EXPRESSION TAG
SEQRES 1 A 140 MET SER ASN ASP THR PRO PHE ASP ALA LEU TRP GLN ARG
SEQRES 2 A 140 MET LEU ALA ARG GLY TRP THR PRO VAL SER GLU SER ARG
SEQRES 3 A 140 LEU ASP ASP TRP LEU THR GLN ALA PRO ASP GLY VAL VAL
SEQRES 4 A 140 LEU LEU SER SER ASP PRO LYS ARG THR PRO GLU VAL SER
SEQRES 5 A 140 ASP ASN PRO VAL MET ILE GLY GLU LEU LEU ARG GLU PHE
SEQRES 6 A 140 PRO ASP TYR THR TRP GLN VAL ALA ILE ALA ASP LEU GLU
SEQRES 7 A 140 GLN SER GLU ALA ILE GLY ASP ARG PHE GLY VAL PHE ARG
SEQRES 8 A 140 PHE PRO ALA THR LEU VAL PHE THR GLY GLY ASN TYR ARG
SEQRES 9 A 140 GLY VAL LEU ASN GLY ILE HIS PRO TRP ALA GLU LEU ILE
SEQRES 10 A 140 ASN LEU MET ARG GLY LEU VAL GLU PRO GLN GLN GLU ARG
SEQRES 11 A 140 ALA SER LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 THR A 5 ALA A 16 1 12
HELIX 2 2 SER A 23 ALA A 34 1 12
HELIX 3 3 PRO A 55 ARG A 63 1 9
HELIX 4 4 ASP A 76 GLY A 88 1 13
HELIX 5 5 PRO A 112 GLU A 125 1 14
SHEET 1 A 5 THR A 20 VAL A 22 0
SHEET 2 A 5 TRP A 70 ALA A 75 1 O ILE A 74 N VAL A 22
SHEET 3 A 5 ASP A 36 LEU A 41 1 N VAL A 38 O ALA A 73
SHEET 4 A 5 ALA A 94 THR A 99 -1 O LEU A 96 N VAL A 39
SHEET 5 A 5 ASN A 102 LEU A 107 -1 O LEU A 107 N THR A 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 - n 31 2 Bytes