Header list of 2h3j.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL GENOMICS, UNKNOWN FUNCTION 22-MAY-06 2H3J
TITLE SOLUTION NMR STRUCTURE OF PROTEIN PA4359 FROM PSEUDOMONAS AERUGINOSA:
TITLE 2 NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET PAT89
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HYPOTHETICAL PROTEIN PA4359;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;
SOURCE 3 ORGANISM_TAXID: 287;
SOURCE 4 GENE: PA4359;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS NESG, GFT NMR, STRUCTURAL GENOMICS, PAT89, PSI-2, PROTEIN STRUCTURE
KEYWDS 2 INITIATIVE, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, UNKNOWN
KEYWDS 3 FUNCTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR Q.ZHANG,G.LIU,A.YEE,C.ARROWSMITH,T.SZYPERSKI,NORTHEAST STRUCTURAL
AUTHOR 2 GENOMICS CONSORTIUM (NESG)
REVDAT 3 09-MAR-22 2H3J 1 REMARK
REVDAT 2 24-FEB-09 2H3J 1 VERSN
REVDAT 1 20-JUN-06 2H3J 0
JRNL AUTH Q.ZHANG,G.LIU,A.YEE,C.ARROWSMITH,T.SZYPERSKI
JRNL TITL SOLUTION STRUCTURE OF HYPOTHETICAL PROTEIN PA4359: NORTHEST
JRNL TITL 2 STRUCTURAL GENOMICS TARGET PAT89
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, CNS 1.1
REMARK 3 AUTHORS : PETER GNTERT (DYANA), A.T.BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2H3J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-06.
REMARK 100 THE DEPOSITION ID IS D_1000037884.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 10 MM TRIS 300 MM NACL 5%
REMARK 210 GLYCEROL 0.01% NAN3 1 MM
REMARK 210 BENZAMIDIINE
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 HETERONUCLEAR
REMARK 210 RESOLVED [1H,1H]-NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 2.3, CYANA 2.1, XEASY
REMARK 210 1.3, AUTOSTRUCTURE 2.0.0, UBNMR
REMARK 210 1.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING GFT TECHNIQUES.
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
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 3 176.84 65.24
REMARK 500 1 GLN A 5 72.27 53.21
REMARK 500 1 ARG A 42 156.14 173.30
REMARK 500 1 ASP A 48 127.16 -177.97
REMARK 500 1 PRO A 49 -168.20 -114.28
REMARK 500 1 ARG A 55 -54.68 178.61
REMARK 500 2 SER A 2 -56.30 -159.71
REMARK 500 2 ALA A 3 90.18 48.52
REMARK 500 2 GLN A 5 148.98 72.57
REMARK 500 2 ASN A 21 88.15 24.47
REMARK 500 2 ASP A 48 118.37 -179.58
REMARK 500 2 ARG A 55 -49.88 -179.63
REMARK 500 3 SER A 7 -74.71 -122.36
REMARK 500 3 PRO A 17 0.39 -62.91
REMARK 500 3 PRO A 49 150.77 -18.67
REMARK 500 3 ARG A 55 -35.22 -141.65
REMARK 500 3 GLN A 56 -35.06 -151.21
REMARK 500 4 SER A 2 53.35 -94.43
REMARK 500 4 SER A 7 -80.02 -80.54
REMARK 500 4 ASN A 21 -105.55 63.77
REMARK 500 4 ASP A 48 119.92 -176.19
REMARK 500 4 THR A 54 -73.02 -82.95
REMARK 500 4 ARG A 55 23.36 -167.82
REMARK 500 4 GLN A 56 -29.76 171.59
REMARK 500 5 SER A 2 150.87 69.12
REMARK 500 5 LEU A 4 -80.48 -88.80
REMARK 500 5 GLN A 5 77.62 58.05
REMARK 500 5 ARG A 42 142.97 -175.18
REMARK 500 5 ASP A 48 120.31 169.24
REMARK 500 5 ARG A 55 24.04 177.24
REMARK 500 5 GLN A 56 -65.71 -127.32
REMARK 500 6 SER A 2 35.66 -177.71
REMARK 500 6 GLN A 5 77.01 -151.85
REMARK 500 6 SER A 7 -61.76 -166.16
REMARK 500 6 ARG A 42 135.79 -176.52
REMARK 500 6 ASP A 48 118.53 -164.68
REMARK 500 6 ARG A 55 -61.25 178.24
REMARK 500 7 LEU A 4 98.28 61.64
REMARK 500 7 SER A 7 -63.07 -106.93
REMARK 500 7 PRO A 17 6.82 -65.98
REMARK 500 7 LEU A 46 -88.48 -65.86
REMARK 500 7 ASP A 48 124.41 -178.44
REMARK 500 7 GLN A 56 -62.37 -141.72
REMARK 500 7 LEU A 74 -71.77 -94.63
REMARK 500 8 ASN A 21 -158.99 58.58
REMARK 500 8 PRO A 49 -166.79 -117.96
REMARK 500 8 GLN A 56 -52.92 -140.91
REMARK 500 9 SER A 7 -77.04 -104.18
REMARK 500 9 PRO A 17 2.53 -67.77
REMARK 500 9 ASP A 48 124.20 -170.92
REMARK 500
REMARK 500 THIS ENTRY HAS 104 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 ASP A 48 PRO A 49 1 129.30
REMARK 500 ASP A 48 PRO A 49 2 139.31
REMARK 500 ASP A 48 PRO A 49 4 134.87
REMARK 500 ASP A 48 PRO A 49 5 137.32
REMARK 500 ASP A 48 PRO A 49 6 132.74
REMARK 500 ASP A 48 PRO A 49 7 136.54
REMARK 500 ASP A 48 PRO A 49 8 139.21
REMARK 500 ASP A 48 PRO A 49 9 143.30
REMARK 500 ASP A 48 PRO A 49 11 123.61
REMARK 500 ASP A 48 PRO A 49 13 140.32
REMARK 500 ASP A 48 PRO A 49 14 131.30
REMARK 500 ASP A 48 PRO A 49 15 132.50
REMARK 500 ASP A 48 PRO A 49 18 136.66
REMARK 500 ASP A 48 PRO A 49 19 132.43
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: PAT89 RELATED DB: TARGETDB
DBREF 2H3J A 1 75 UNP Q9HW42 Q9HW42_PSEAE 1 75
SEQRES 1 A 75 MET SER ALA LEU GLN PRO SER ARG SER TYR ARG ILE THR
SEQRES 2 A 75 GLY TYR SER PRO ALA ILE SER ASN GLY TYR ARG GLN ARG
SEQRES 3 A 75 LEU PHE SER MET GLY LEU LEU PRO GLY ALA ALA LEU ARG
SEQRES 4 A 75 VAL VAL ARG ILE ALA PRO LEU GLY ASP PRO ILE GLN VAL
SEQRES 5 A 75 GLU THR ARG GLN THR SER LEU ALA LEU ARG ARG LYS ASP
SEQRES 6 A 75 LEU ALA LEU LEU THR LEU VAL PRO LEU ASP
HELIX 1 1 GLY A 22 GLY A 31 1 10
HELIX 2 2 ARG A 62 ALA A 67 1 6
SHEET 1 A 5 SER A 58 LEU A 59 0
SHEET 2 A 5 GLN A 51 GLU A 53 -1 N VAL A 52 O LEU A 59
SHEET 3 A 5 ALA A 37 ARG A 42 -1 N VAL A 41 O GLN A 51
SHEET 4 A 5 SER A 9 TYR A 15 -1 N TYR A 10 O LEU A 38
SHEET 5 A 5 LEU A 69 PRO A 73 -1 O VAL A 72 N ARG A 11
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