Header list of 2fgx.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 22-DEC-05 2FGX
TITLE SOLUTION NMR STRUCTURE OF PROTEIN NE2328 FROM NITROSOMONAS EUROPAEA.
TITLE 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET NET3.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PUTATIVE THIOREDOXIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: NITROSOMONAS EUROPAEA;
SOURCE 3 ORGANISM_TAXID: 915;
SOURCE 4 GENE: NE2328;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21-GOLD (DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET P11
KEYWDS NET3, NESG, GFT-NMR, GLUTAREDOXIN-LIKE, PUTATIVE THIOREDOXIN,
KEYWDS 2 STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, NORTHEAST
KEYWDS 3 STRUCTURAL GENOMICS CONSORTIUM, UNKNOWN FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.ELETSKY,G.LIU,A.YEE,C.H.ARROWSMITH,T.SZYPERSKI,NORTHEAST STRUCTURAL
AUTHOR 2 GENOMICS CONSORTIUM (NESG)
REVDAT 3 09-MAR-22 2FGX 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2FGX 1 VERSN
REVDAT 1 21-FEB-06 2FGX 0
JRNL AUTH A.ELETSKY,G.LIU,A.YEE,C.H.ARROWSMITH,T.SZYPERSKI
JRNL TITL SOLUTION NMR STRUCTURE OF NITROSOMONAS EUROPAEA HYPOTHETICAL
JRNL TITL 2 PROTEIN NE2328: NORTHEAST STRUCTURAL GENOMICS CONSORTIUM
JRNL TITL 3 TARGET NET3
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.3, CNS 1.1
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE),
REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,
REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2FGX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JAN-06.
REMARK 100 THE DEPOSITION ID IS D_1000035864.
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 : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 10 MM MOPS, 450 MM NACL, 10 MM
REMARK 210 DTT, ~10 UM ZN++, 0.01 % NAN3, 1
REMARK 210 MM BENZAMIDINE, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : GFT (4,3)D HNNCABCA; GFT (4,3)D
REMARK 210 CABCA(CO)NHN; GFT (4,3)D
REMARK 210 HABCAB(CO)NHN; GFT (4,3)D HCCH;
REMARK 210 SIMULTANEOUS 13C-, 15N-RESOLVED
REMARK 210 [1H, 1H] NOESY; AROMATIC 13C-
REMARK 210 RESOLVED [1H, 1H] NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1C, CARA 1.5, CYANA 2.1
REMARK 210 METHOD USED : SIMULATED ANNEALING, TORSION
REMARK 210 ANGLE DYNAMICS, EXPLICIT WATER
REMARK 210 BATH REFINEMENT
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: B-FACTOR COLUMN STORES ADDITIONAL COORDINATE DIGITS.
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 MET A -21
REMARK 465 GLY A -20
REMARK 465 THR A -19
REMARK 465 SER A -18
REMARK 465 HIS A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 SER A -11
REMARK 465 SER A -10
REMARK 465 GLY A -9
REMARK 465 ARG A -8
REMARK 465 GLU A -7
REMARK 465 ASN A -6
REMARK 465 LEU A -5
REMARK 465 TYR A -4
REMARK 465 PHE A -3
REMARK 465 GLN A -2
REMARK 465 GLY 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 O GLY A 81 O SER A 85 2.14
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 3 114.49 -171.58
REMARK 500 1 GLU A 16 -171.39 61.93
REMARK 500 1 PHE A 37 13.80 -145.46
REMARK 500 1 GLU A 38 179.86 57.64
REMARK 500 1 TYR A 54 -64.18 -108.65
REMARK 500 1 ASN A 55 -85.37 55.37
REMARK 500 1 VAL A 58 -122.71 -85.73
REMARK 500 1 PRO A 59 66.45 -10.33
REMARK 500 1 GLU A 66 -39.38 -157.44
REMARK 500 1 ASP A 67 60.15 69.96
REMARK 500 1 LEU A 70 -64.52 -105.23
REMARK 500 1 TYR A 73 134.05 -39.67
REMARK 500 1 PHE A 74 95.76 73.31
REMARK 500 1 SER A 77 -51.25 69.98
REMARK 500 2 ASN A 3 63.27 -104.44
REMARK 500 2 GLU A 16 17.93 57.68
REMARK 500 2 PHE A 37 16.66 -144.82
REMARK 500 2 GLU A 38 -175.32 58.58
REMARK 500 2 VAL A 58 -135.07 -80.37
REMARK 500 2 PRO A 59 68.21 -5.45
REMARK 500 2 ASN A 65 -49.00 79.02
REMARK 500 2 ASP A 67 82.18 63.02
REMARK 500 2 LEU A 70 -79.21 -94.76
REMARK 500 2 PHE A 74 103.35 70.78
REMARK 500 2 SER A 77 -60.40 71.27
REMARK 500 3 LYS A 9 113.66 72.03
REMARK 500 3 CYS A 18 95.76 70.69
REMARK 500 3 GLU A 38 175.30 59.92
REMARK 500 3 TYR A 54 -67.68 -108.42
REMARK 500 3 ASN A 55 -87.38 50.86
REMARK 500 3 VAL A 58 -127.10 -92.00
REMARK 500 3 PRO A 59 71.33 -12.96
REMARK 500 3 GLU A 66 -44.41 -152.56
REMARK 500 3 ASP A 67 81.41 70.89
REMARK 500 3 TYR A 73 -44.95 74.97
REMARK 500 4 GLN A 4 85.21 55.51
REMARK 500 4 GLU A 38 -178.64 58.67
REMARK 500 4 ASP A 45 98.10 -64.88
REMARK 500 4 ASP A 56 -59.42 -154.34
REMARK 500 4 VAL A 58 -107.06 -80.12
REMARK 500 4 PRO A 59 72.60 -9.62
REMARK 500 4 ASP A 67 74.07 62.23
REMARK 500 4 PHE A 74 98.59 70.67
REMARK 500 4 SER A 77 -54.63 72.91
REMARK 500 5 ARG A 15 110.01 -174.78
REMARK 500 5 GLU A 16 -87.66 65.06
REMARK 500 5 GLU A 38 -178.23 59.01
REMARK 500 5 VAL A 58 -108.09 -83.16
REMARK 500 5 PRO A 59 68.01 -15.01
REMARK 500 5 ASN A 65 -54.46 176.23
REMARK 500
REMARK 500 THIS ENTRY HAS 220 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 VAL A 58 PRO A 59 1 -142.23
REMARK 500 VAL A 58 PRO A 59 2 -139.80
REMARK 500 VAL A 58 PRO A 59 3 -143.11
REMARK 500 VAL A 58 PRO A 59 4 -140.13
REMARK 500 VAL A 58 PRO A 59 5 -144.68
REMARK 500 VAL A 58 PRO A 59 6 -139.82
REMARK 500 VAL A 58 PRO A 59 7 -149.06
REMARK 500 VAL A 58 PRO A 59 8 -136.75
REMARK 500 VAL A 58 PRO A 59 9 -138.17
REMARK 500 VAL A 58 PRO A 59 10 -139.24
REMARK 500 VAL A 58 PRO A 59 11 -140.82
REMARK 500 VAL A 58 PRO A 59 12 -139.44
REMARK 500 VAL A 58 PRO A 59 13 -141.67
REMARK 500 VAL A 58 PRO A 59 14 -145.01
REMARK 500 VAL A 58 PRO A 59 16 -129.83
REMARK 500 VAL A 58 PRO A 59 17 -144.68
REMARK 500 VAL A 58 PRO A 59 19 -146.27
REMARK 500 VAL A 58 PRO A 59 20 -145.54
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: NET3 RELATED DB: TARGETDB
DBREF 2FGX A 1 85 GB 30181050 CAD86240 1 85
SEQADV 2FGX MET A -21 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX GLY A -20 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX THR A -19 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX SER A -18 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX HIS A -17 GB 30181050 EXPRESSION TAG
SEQADV 2FGX HIS A -16 GB 30181050 EXPRESSION TAG
SEQADV 2FGX HIS A -15 GB 30181050 EXPRESSION TAG
SEQADV 2FGX HIS A -14 GB 30181050 EXPRESSION TAG
SEQADV 2FGX HIS A -13 GB 30181050 EXPRESSION TAG
SEQADV 2FGX HIS A -12 GB 30181050 EXPRESSION TAG
SEQADV 2FGX SER A -11 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX SER A -10 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX GLY A -9 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX ARG A -8 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX GLU A -7 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX ASN A -6 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX LEU A -5 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX TYR A -4 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX PHE A -3 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX GLN A -2 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX GLY A -1 GB 30181050 CLONING ARTIFACT
SEQADV 2FGX HIS A 0 GB 30181050 CLONING ARTIFACT
SEQRES 1 A 107 MET GLY THR SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 107 ARG GLU ASN LEU TYR PHE GLN GLY HIS MET ASN ASN GLN
SEQRES 3 A 107 VAL GLU PRO ARG LYS LEU VAL VAL TYR GLY ARG GLU GLY
SEQRES 4 A 107 CYS HIS LEU CYS GLU GLU MET ILE ALA SER LEU ARG VAL
SEQRES 5 A 107 LEU GLN LYS LYS SER TRP PHE GLU LEU GLU VAL ILE ASN
SEQRES 6 A 107 ILE ASP GLY ASN GLU HIS LEU THR ARG LEU TYR ASN ASP
SEQRES 7 A 107 ARG VAL PRO VAL LEU PHE ALA VAL ASN GLU ASP LYS GLU
SEQRES 8 A 107 LEU CYS HIS TYR PHE LEU ASP SER ASP VAL ILE GLY ALA
SEQRES 9 A 107 TYR LEU SER
HELIX 1 1 CYS A 18 SER A 35 1 18
HELIX 2 2 ASN A 47 TYR A 54 1 8
HELIX 3 3 SER A 77 SER A 85 1 9
SHEET 1 A 4 GLU A 40 ASN A 43 0
SHEET 2 A 4 LEU A 10 GLY A 14 1 N VAL A 12 O GLU A 40
SHEET 3 A 4 VAL A 60 ALA A 63 -1 O PHE A 62 N VAL A 11
SHEET 4 A 4 LYS A 68 CYS A 71 -1 O LYS A 68 N ALA A 63
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